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Conserved domains on  [gi|636808205|ref|WP_024334403|]
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M48 family metallopeptidase [Desulfotignum balticum]

Protein Classification

M48 family metallopeptidase( domain architecture ID 11574954)

M48 family metallopeptidase, a member of a zinc metalloprotease family, which typically contains an HExxH motif characteristic of zinc metallopeptidases, and proteolytically removes the C-terminal three residues of farnesylated proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
M48A_Ste24p-like cd07345
Peptidase M48 subfamily A-like, putative CaaX prenyl protease; This family contains peptidase ...
 76-423 6.84e-139

Peptidase M48 subfamily A-like, putative CaaX prenyl protease; This family contains peptidase family M48 subfamily A-like CaaX prenyl protease 1, most of which are uncharacterized. Some of these contain tetratricopeptide (TPR) repeats at the C-terminus. Proteins in this family contain the zinc metalloprotease motif (HEXXH), likely exposed on the cytoplasmic side. They are thought to be possibly associated with the endoplasmic reticulum (ER), regardless of whether their genes possess the conventional signal motif (KKXX) in the C-terminal. These proteins putatively remove the C-terminal three residues of farnesylated proteins proteolytically.


:

Pssm-ID: 320704 [Multi-domain]  Cd Length: 346  Bit Score: 407.82  E-value: 6.84e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205  76 LSVLALLVFAVNIYVFRLNTAFSHVQLFQKVPTLEALLFLGLFVSYLVMVWHAAYPVQKHLFSRPVSCKQYIFSQLSFAL 155
Cdd:cd07345    1 LSVLALLLFAIDIYALDLKYYLSFIPLFGSSPTLLALLFLLLFLLLLLLVWYAAYPVYKKLFSGLESRRAYVLSNLRFLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 156 PTLLPWLCLSLFVDLIRFIAYPPLDDLMNGPAGEMIIIMVFMAGIAVFGPVFIKTIWQCRPMEKGPGRSRIEAVCHMAGL 235
Cdd:cd07345   81 PILLPWLLLSLLQDLLSLLPLAILKNLLSSSLGLLGFLLLFLLLLLLFPPLLIRLIWGCKPLPPGPLRDRLEAFCRRAGF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 236 RYADILIWDLFAGSMITAGVMGLVGKFRYILVTPALLGSLNDEELAAVILHEIGHVKHWHMLYYLVFFAGFIACNAVLYD 315
Cdd:cd07345  161 KVADILVWPLFEGRVATAGVMGILPRFRYILITDALLDSLSPEELEAVLAHEIGHVKKRHLLLYLLFFLGFILLLALLSL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 316 PLMLLVLAGATYFPEpvFSGIDISQVHSVLMGAILICFFIVYFRFVFGFFMRNFERQADLYLFRFFPNAFPLIRTFYKIG 395
Cdd:cd07345  241 LLSLLLLLLLPLLIL--LLGSSAEILLTLLLALPLLLLLVLYFRFVFGFFSRNFERQADLYALRALGSAEPLISALEKIA 318

                        330       340
                 ....*....|....*....|....*...
gi 636808205 396 AISRQDMERPNWHHFSIGQRIRFLEKCQ 423
Cdd:cd07345  319 ELSGNSRDKPSWHHFSIAQRIAFLEKCE 346
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 477-597 9.20e-15

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 71.19  E-value: 9.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 477 EQLKMDPENADLHVVAGDFHYASQNFIQAIAAYESAIGINSNHVHALNNLAWLLAtcpvtEIQDPGRALNLAGRAVGLAP 556
Cdd:COG4235    8 QALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALL-----AAGDTEEAEELLERALALDP 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 636808205 557 QSPFVQDTYAEALFANHRVAEAVSAARKALELARDRQNYYQ 597
Cdd:COG4235   83 DNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPADAPARL 123
 
Name Accession Description Interval E-value
M48A_Ste24p-like cd07345
Peptidase M48 subfamily A-like, putative CaaX prenyl protease; This family contains peptidase ...
 76-423 6.84e-139

Peptidase M48 subfamily A-like, putative CaaX prenyl protease; This family contains peptidase family M48 subfamily A-like CaaX prenyl protease 1, most of which are uncharacterized. Some of these contain tetratricopeptide (TPR) repeats at the C-terminus. Proteins in this family contain the zinc metalloprotease motif (HEXXH), likely exposed on the cytoplasmic side. They are thought to be possibly associated with the endoplasmic reticulum (ER), regardless of whether their genes possess the conventional signal motif (KKXX) in the C-terminal. These proteins putatively remove the C-terminal three residues of farnesylated proteins proteolytically.


Pssm-ID: 320704 [Multi-domain]  Cd Length: 346  Bit Score: 407.82  E-value: 6.84e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205  76 LSVLALLVFAVNIYVFRLNTAFSHVQLFQKVPTLEALLFLGLFVSYLVMVWHAAYPVQKHLFSRPVSCKQYIFSQLSFAL 155
Cdd:cd07345    1 LSVLALLLFAIDIYALDLKYYLSFIPLFGSSPTLLALLFLLLFLLLLLLVWYAAYPVYKKLFSGLESRRAYVLSNLRFLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 156 PTLLPWLCLSLFVDLIRFIAYPPLDDLMNGPAGEMIIIMVFMAGIAVFGPVFIKTIWQCRPMEKGPGRSRIEAVCHMAGL 235
Cdd:cd07345   81 PILLPWLLLSLLQDLLSLLPLAILKNLLSSSLGLLGFLLLFLLLLLLFPPLLIRLIWGCKPLPPGPLRDRLEAFCRRAGF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 236 RYADILIWDLFAGSMITAGVMGLVGKFRYILVTPALLGSLNDEELAAVILHEIGHVKHWHMLYYLVFFAGFIACNAVLYD 315
Cdd:cd07345  161 KVADILVWPLFEGRVATAGVMGILPRFRYILITDALLDSLSPEELEAVLAHEIGHVKKRHLLLYLLFFLGFILLLALLSL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 316 PLMLLVLAGATYFPEpvFSGIDISQVHSVLMGAILICFFIVYFRFVFGFFMRNFERQADLYLFRFFPNAFPLIRTFYKIG 395
Cdd:cd07345  241 LLSLLLLLLLPLLIL--LLGSSAEILLTLLLALPLLLLLVLYFRFVFGFFSRNFERQADLYALRALGSAEPLISALEKIA 318

                        330       340
                 ....*....|....*....|....*...
gi 636808205 396 AISRQDMERPNWHHFSIGQRIRFLEKCQ 423
Cdd:cd07345  319 ELSGNSRDKPSWHHFSIAQRIAFLEKCE 346
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 477-597 9.20e-15

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 71.19  E-value: 9.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 477 EQLKMDPENADLHVVAGDFHYASQNFIQAIAAYESAIGINSNHVHALNNLAWLLAtcpvtEIQDPGRALNLAGRAVGLAP 556
Cdd:COG4235    8 QALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALL-----AAGDTEEAEELLERALALDP 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 636808205 557 QSPFVQDTYAEALFANHRVAEAVSAARKALELARDRQNYYQ 597
Cdd:COG4235   83 DNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPADAPARL 123
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 479-589 7.40e-14

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 75.12  E-value: 7.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205  479 LKMDPENADLHVVAGDFHYASQNFIQAIAAYESAIGINSNHVHALNNLAWLLATcpvteiQDPGRALNLAGRAVGLAPQS 558
Cdd:TIGR02917 763 LKTHPNDAVLRTALAELYLAQKDYDKAIKHYQTVVKKAPDNAVVLNNLAWLYLE------LKDPRALEYAERALKLAPNI 836

                          90       100       110
                  ....*....|....*....|....*....|.
gi 636808205  559 PFVQDTYAEALFANHRVAEAVSAARKALELA 589
Cdd:TIGR02917 837 PAILDTLGWLLVEKGEADRALPLLRKAVNIA 867
HtpX COG0501
Zn-dependent protease with chaperone function [Posttranslational modification, protein ...
 223-421 4.84e-13

Zn-dependent protease with chaperone function [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440267 [Multi-domain]  Cd Length: 210  Bit Score: 68.37  E-value: 4.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 223 RSRIEAVCHMAGLRYADILIWDlfaGSMITAGVMGLVGKFRYILVTPALLGSLNDEELAAVILHEIGHVKHWHMLYYLV- 301
Cdd:COG0501    5 YRLVEELAARAGIPMPEVYVMD---SPAPNAFATGRGPNNARIVVTDGLLELLDRDELEAVLAHELGHIKNGDILLMTLa 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 302 -FFAGFIacnavlydplMLLVLAGATYFPEPVFSGIdisqvhsVLMGAILICFFIVyFRFVFGFFMRNFERQADLYLFRF 380
Cdd:COG0501   82 sGLLGLI----------GFLARLLPLAFGRDRDAGL-------LLGLLLGILAPFL-ATLIQLALSRKREYEADRAAAEL 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 381 FPNAFPLIRTFYKIGAISRQDMERPNW----HHF---------------SIGQRIRFLEK 421
Cdd:COG0501  144 TGDPDALASALRKLAGGNLSIPLRRAFpaqaHAFiinplklsslfsthpPLEERIARLRE 203
Peptidase_M48 pfam01435
Peptidase family M48; Peptidase_M48 is the largely extracellular catalytic region of CAAX ...
 264-421 2.04e-10

Peptidase family M48; Peptidase_M48 is the largely extracellular catalytic region of CAAX prenyl protease homologs such as Human FACE-1 protease. These are metallopeptidases, with the characteriztic HExxH motif giving the two histidine-zinc-ligands and an adjacent glutamate on the next helix being the third. The whole molecule folds to form a deep groove/cleft into which the substrate can fit.


Pssm-ID: 426263 [Multi-domain]  Cd Length: 201  Bit Score: 60.52  E-value: 2.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205  264 YILVTPALLGSL-NDEELAAVILHEIGHVKHWHMLYYLVFFAGFIACNAVLYDPLMLLVLAGATYFpepvfsGIDISQVH 342
Cdd:pfam01435  48 RVVVTTGLLDLLeTEDELAAVLGHEIGHIKARHSVESLSIMGGLSLAQLFLALLLLGAAASGFANF------GIIFLLLI 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205  343 SVLMGAIlicffivyfRFVFGFFMRNFERQADLYLFRFFPNAFPLIRTFYKI-GAISR-----QDMERPNWH--HFSIGQ 414
Cdd:pfam01435 122 GPLAALL---------TLLLLPYSRAQEYEADRLGAELMARAGYDPRALIKLwGEIDNngrasDGALYPELLstHPSLVE 192


                  ....*..
gi 636808205  415 RIRFLEK 421
Cdd:pfam01435 193 RIAALRE 199
PRK03982 PRK03982
heat shock protein HtpX; Provisional
 267-293 2.04e-03

heat shock protein HtpX; Provisional


Pssm-ID: 235186 [Multi-domain]  Cd Length: 288  Bit Score: 40.37  E-value: 2.04e-03
                         10        20
                 ....*....|....*....|....*..
gi 636808205 267 VTPALLGSLNDEELAAVILHEIGHVKH 293
Cdd:PRK03982 112 VTEGILNLLNEDELEGVIAHELTHIKN 138
 
Name Accession Description Interval E-value
M48A_Ste24p-like cd07345
Peptidase M48 subfamily A-like, putative CaaX prenyl protease; This family contains peptidase ...
 76-423 6.84e-139

Peptidase M48 subfamily A-like, putative CaaX prenyl protease; This family contains peptidase family M48 subfamily A-like CaaX prenyl protease 1, most of which are uncharacterized. Some of these contain tetratricopeptide (TPR) repeats at the C-terminus. Proteins in this family contain the zinc metalloprotease motif (HEXXH), likely exposed on the cytoplasmic side. They are thought to be possibly associated with the endoplasmic reticulum (ER), regardless of whether their genes possess the conventional signal motif (KKXX) in the C-terminal. These proteins putatively remove the C-terminal three residues of farnesylated proteins proteolytically.


Pssm-ID: 320704 [Multi-domain]  Cd Length: 346  Bit Score: 407.82  E-value: 6.84e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205  76 LSVLALLVFAVNIYVFRLNTAFSHVQLFQKVPTLEALLFLGLFVSYLVMVWHAAYPVQKHLFSRPVSCKQYIFSQLSFAL 155
Cdd:cd07345    1 LSVLALLLFAIDIYALDLKYYLSFIPLFGSSPTLLALLFLLLFLLLLLLVWYAAYPVYKKLFSGLESRRAYVLSNLRFLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 156 PTLLPWLCLSLFVDLIRFIAYPPLDDLMNGPAGEMIIIMVFMAGIAVFGPVFIKTIWQCRPMEKGPGRSRIEAVCHMAGL 235
Cdd:cd07345   81 PILLPWLLLSLLQDLLSLLPLAILKNLLSSSLGLLGFLLLFLLLLLLFPPLLIRLIWGCKPLPPGPLRDRLEAFCRRAGF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 236 RYADILIWDLFAGSMITAGVMGLVGKFRYILVTPALLGSLNDEELAAVILHEIGHVKHWHMLYYLVFFAGFIACNAVLYD 315
Cdd:cd07345  161 KVADILVWPLFEGRVATAGVMGILPRFRYILITDALLDSLSPEELEAVLAHEIGHVKKRHLLLYLLFFLGFILLLALLSL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 316 PLMLLVLAGATYFPEpvFSGIDISQVHSVLMGAILICFFIVYFRFVFGFFMRNFERQADLYLFRFFPNAFPLIRTFYKIG 395
Cdd:cd07345  241 LLSLLLLLLLPLLIL--LLGSSAEILLTLLLALPLLLLLVLYFRFVFGFFSRNFERQADLYALRALGSAEPLISALEKIA 318

                        330       340
                 ....*....|....*....|....*...
gi 636808205 396 AISRQDMERPNWHHFSIGQRIRFLEKCQ 423
Cdd:cd07345  319 ELSGNSRDKPSWHHFSIAQRIAFLEKCE 346
M48A_Ste24p cd07330
Peptidase M48 CaaX prenyl protease type 1, an integral membrane, Zn-dependent protein; This ...
 107-421 5.83e-41

Peptidase M48 CaaX prenyl protease type 1, an integral membrane, Zn-dependent protein; This family of M48 CaaX prenyl protease 1-like family includes a number of well characterized genes such as those found in Taenia solium metacestode (TsSte24p), Arabidopsis (AtSte24), yeast Ste24p and human (Hs Ste24p) as well as several uncharacterized genes such as YhfN, some of which also containing tetratricopeptide (TPR) repeats. All members of this family contain the zinc metalloprotease motif (HEXXH), likely exposed on the cytoplasmic side. They are thought to be intimately associated with the endoplasmic reticulum (ER), regardless of whether their genes possess the conventional signal motif (KKXX) in the C-terminal. Proteins in this family proteolytically remove the C-terminal three residues of farnesylated proteins. The gene ZmpSte24, also known as FACE-1 in humans, a member of this family, is involved in the post-translational processing of prelamin A to mature lamin A, a major component of the nuclear envelope. ZmpSte24 deficiency causes an accumulation of prelamin A leading to lipodystrophy and other disease phenotypes while mutations in the protein lead to diseases of lamin processing (laminopathies), such as premature aging disease progeria and metabolic disorders. Some of these mutations map to the peptide-binding site.


Pssm-ID: 320689 [Multi-domain]  Cd Length: 285  Bit Score: 150.29  E-value: 5.83e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 107 PTLEALLFLGLFVSYLVMVWHAAYPVQKHLFSRPVSCKQYIFSQLSFALPTLLPW-LCLSL--FVDLIRFIAYPPLDdlm 183
Cdd:cd07330    2 PILAALVFLLVFTGLMVLVELPFGWVARFRVEERFGYMRETRSLWSKRTVALLTVgLLVALpvSALLLPFEEPGGGA--- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 184 nGPAGEMIIIMVFMAGIAVFGPVFIKTIWQC-RPMEKGPGRSRIEAVCHMAGLRYADILIWDLFAGSMITAGVMGLV--G 260
Cdd:cd07330   79 -WWLGEWLAWLFYLFWRWKLSPFYAQFWKRRsRPLANGELRERIESMMNREGFGCAEILKVELSGGSMIHANAYFPGsgK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 261 KFRYILVTPALLGSLNDEELAAVILHEIGHVKHWHMLYYLVFFAGFIACNAVLYdplmllvlagatyfpepvfsgidisq 340
Cdd:cd07330  158 RRRVVVFADALVSLMTPDELLAVIAHELGHVKHHHHLFRLAASQAVSFIVCALF-------------------------- 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 341 vhsvlmgailicFFIVYFRFVFGFFMRNFERQADLYLFRFFpNAFPLIRTFYKIGAISRQ----DMERPNWHHFSI--GQ 414
Cdd:cd07330  212 ------------ILIYPLRFLLNFFARRFEYQADAYAAKLA-GADALISALVKLHRDNLTtltpSRLYSLWHYSHPhaAM 278


                 ....*..
gi 636808205 415 RIRFLEK 421
Cdd:cd07330  279 RVAHLLR 285
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 477-597 9.20e-15

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 71.19  E-value: 9.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 477 EQLKMDPENADLHVVAGDFHYASQNFIQAIAAYESAIGINSNHVHALNNLAWLLAtcpvtEIQDPGRALNLAGRAVGLAP 556
Cdd:COG4235    8 QALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALL-----AAGDTEEAEELLERALALDP 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 636808205 557 QSPFVQDTYAEALFANHRVAEAVSAARKALELARDRQNYYQ 597
Cdd:COG4235   83 DNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPADAPARL 123
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 479-589 7.40e-14

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 75.12  E-value: 7.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205  479 LKMDPENADLHVVAGDFHYASQNFIQAIAAYESAIGINSNHVHALNNLAWLLATcpvteiQDPGRALNLAGRAVGLAPQS 558
Cdd:TIGR02917 763 LKTHPNDAVLRTALAELYLAQKDYDKAIKHYQTVVKKAPDNAVVLNNLAWLYLE------LKDPRALEYAERALKLAPNI 836

                          90       100       110
                  ....*....|....*....|....*....|.
gi 636808205  559 PFVQDTYAEALFANHRVAEAVSAARKALELA 589
Cdd:TIGR02917 837 PAILDTLGWLLVEKGEADRALPLLRKAVNIA 867
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 473-591 1.02e-13

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 68.68  E-value: 1.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 473 RLVLEQLKMDPENADLHVVAGDFHYASQNFIQAIAAYESAIGINSNHVHALNNLAWLLAtcpvtEIQDPGRALNLAGRAV 552
Cdd:COG4783   25 ALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALL-----KAGDYDEALALLEKAL 99

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 636808205 553 GLAPQSPFVQDTYAEALFANHRVAEAVSAARKALELARD 591
Cdd:COG4783  100 KLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDPD 138
M48A_Zmpste24p_like cd07343
Peptidase M48 subfamily A, a type 1 CaaX endopeptidase; This family contains peptidase family ...
 58-421 2.82e-13

Peptidase M48 subfamily A, a type 1 CaaX endopeptidase; This family contains peptidase family M48 subfamily A which includes a number of well-characterized genes such as those found in humans (ZMPSTE24, also known as farnesylated protein-converting enzyme 1 or FACE-1 or Hs Ste24), Taenia solium metacestode (TsSte24p), Arabidopsis (AtSte24) and yeast (Ste24p). Ste24p contains the zinc metalloprotease motif (HEXXH), likely exposed on the cytoplasmic side. It is thought to be intimately associated with the endoplasmic reticulum (ER), regardless of whether its genes possess the conventional signal motif (KKXX) in the C-terminal. Proteins in this family proteolytically remove the C-terminal three residues of farnesylated proteins. Ste24p is involved in the post-translational processing of prelamin A to mature lamin A, a major component of the nuclear envelope. ZmpSte24 deficiency causes an accumulation of prelamin A leading to lipodystrophy and other disease phenotypes, while mutations in this gene or in that encoding its substrate, prelamin A, result in a series of human inherited diseases known as laminopathies, the most severe of which are Hutchinson Gilford progeria syndrome (HGPS) and restrictive dermopathy (RD) which arise due to unsuccessful maturation of prelamin A. Two forms of mandibuloacral dysplasia, a condition that causes a variety of abnormalities involving bone development, skin pigmentation, and fat distribution, are caused by mutations in two different genes; mutations in the LMNA gene, which normally provides instructions for making lamin A and lamin C, cause mandibuloacral dysplasia with A-type lipodystrophy (MAD-A), and mutations in the ZMPSTE24 gene cause mandibuloacral dysplasia with B-type lipodystrophy (MAD-B). Within cells, these genes are involved in maintaining the structure of the nucleus and may play a role in many cellular processes. Certain HIV protease inhibitors have been shown to inhibit the enzymatic activity of ZMPSTE24, but not enzymes involved in prelamin A processing.


Pssm-ID: 320702 [Multi-domain]  Cd Length: 405  Bit Score: 71.74  E-value: 2.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205  58 KKSVTFQEDRAVSSTISrlSVLALLVFAVNIYVFRLNTAFSHVQLFQKVPTLEALLFLGLF--VSYLVM----VWHAAYP 131
Cdd:cd07343   45 EKAQAYSLDKSRFSIVS--SLLSLLLLLLLLLFGLLPLLDLLLRSLGGNEILQSLLFFLLLslISTLLSlpfsLYSTFVI 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 132 VQKHLFSRpVSCKQYIFSQL-SFALPTLLPWLCLSLFVDLIRFiaypplddlmngpAGE------MIIIMVFMAGIAVFG 204
Cdd:cd07343  123 EEKFGFNK-QTLGLFIKDLLkSLLLSLVLGGPLLALLLWIIKK-------------FGKywwlyaWLFVVVFSLLLMFIY 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 205 PVFI------KTiwqcrPMEKGPGRSRIEAVCHMAGLRYADILIWDlfaGSMITAG----VMGLvGKFRYILV--TpaLL 272
Cdd:cd07343  189 PTLIaplfnkFT-----PLEDGELKTKIEALAKRAGFPLKKVYVMD---GSKRSTHsnayFTGF-GKNKRIVLfdT--LL 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 273 GSLNDEELAAVILHEIGHVKHWHMLYYLVFFAGFIacnavlydpLMLLVLAGATYFPEPVFSGIDISQvHSVLMGAILIC 352
Cdd:cd07343  258 EQLTEDEILAVLAHELGHWKHGHILKGLILSQLLL---------FLGFYLFGLLLNNPSLYRAFGFFG-PSDQPALIGFL 327

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 636808205 353 FFIVYFRFVFGFFM----RNFERQADLYLFRFFpNAFPLIRTFYKIGAISRQDMERPNWHHF------SIGQRIRFLEK 421
Cdd:cd07343  328 LLLSPLSFLLSPLMnalsRKFEYEADAFAVELG-YGEALISALVKLSKDNLSNLTPDPLYSAfhyshpPLLERIAALEK 405
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 479-605 4.47e-13

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 72.33  E-value: 4.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 479 LKMDPENADLHVVAGDFHYASQNFIQAIAAYESAIGINSNHVHALNNLAWLLATCpvteiQDPGRALNLAGRAVGLAPQS 558
Cdd:COG3914  105 LALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRL-----GRLEEAIAALRRALELDPDN 179

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 636808205 559 PFVQDTYAEALFANHRVAEAVSAARKALELARDRQNYYQNQVRRFQR 605
Cdd:COG3914  180 AEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFALRQ 226
HtpX COG0501
Zn-dependent protease with chaperone function [Posttranslational modification, protein ...
 223-421 4.84e-13

Zn-dependent protease with chaperone function [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440267 [Multi-domain]  Cd Length: 210  Bit Score: 68.37  E-value: 4.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 223 RSRIEAVCHMAGLRYADILIWDlfaGSMITAGVMGLVGKFRYILVTPALLGSLNDEELAAVILHEIGHVKHWHMLYYLV- 301
Cdd:COG0501    5 YRLVEELAARAGIPMPEVYVMD---SPAPNAFATGRGPNNARIVVTDGLLELLDRDELEAVLAHELGHIKNGDILLMTLa 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 302 -FFAGFIacnavlydplMLLVLAGATYFPEPVFSGIdisqvhsVLMGAILICFFIVyFRFVFGFFMRNFERQADLYLFRF 380
Cdd:COG0501   82 sGLLGLI----------GFLARLLPLAFGRDRDAGL-------LLGLLLGILAPFL-ATLIQLALSRKREYEADRAAAEL 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 381 FPNAFPLIRTFYKIGAISRQDMERPNW----HHF---------------SIGQRIRFLEK 421
Cdd:COG0501  144 TGDPDALASALRKLAGGNLSIPLRRAFpaqaHAFiinplklsslfsthpPLEERIARLRE 203
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
479-598 1.40e-12

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 67.72  E-value: 1.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 479 LKMDPENADLHVVAGDFHYASQNFIQAIAAYESAIGINSNHVHALNNLAWLLAtcpvtEIQDPGRALNLAGRAVGLAPQS 558
Cdd:COG0457    1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYL-----RLGRYEEALADYEQALELDPDD 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 636808205 559 PFVQDTYAEALFANHRVAEAVSAARKALELARDRQNYYQN 598
Cdd:COG0457   76 AEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYN 115
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
479-609 2.70e-12

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 66.95  E-value: 2.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 479 LKMDPENADLHVVAGDFHYASQNFIQAIAAYESAIGINSNHVHALNNLAWLLAtcpvtEIQDPGRALNLAGRAVGLAPQS 558
Cdd:COG0457   69 LELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALL-----ELGRYDEAIEAYERALELDPDD 143

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 636808205 559 PFVQDTYAEALFANHRVAEAVSAARKALELARDRQNYYQNQVRRFQRHLER 609
Cdd:COG0457  144 ADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAE 194
M48B_HtpX_like cd07338
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ...
 263-421 5.01e-11

Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of peptidase M48 subfamily B includes uncharacterized HtpX homologs and consists of proteins smaller than Ste24p, with homology restricted to the C-terminal half of Ste24p. HtpX expression is controlled by the Cpx stress response system, which senses abnormal membrane proteins. HtpX participates in the proteolytic quality control of these misfolded proteins by undergoing self-degradation and collaborating with FtsH, a membrane-bound and ATP-dependent protease, to eliminate them. HtpX, a zinc metalloprotease with an active site motif HEXXH, has an FtsH-like topology, and is capable of introducing endoproteolytic cleavages into SecY (also an FtsH substrate). However, HtpX does not have an ATPase activity and will only act against cytoplasmic regions of a target membrane protein. Thus, HtpX and FtsH have overlapping and/or complementary functions, which are especially important at high temperature; in E. coli and Xylella fastidiosa, HtpX is heat-inducible, while in Streptococcus gordonii it is not.


Pssm-ID: 320697 [Multi-domain]  Cd Length: 216  Bit Score: 62.60  E-value: 5.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 263 RYILVTPALLGSLNDEELAAVILHEIGHVKHWHMLYYLVFfaGFIacnavlydPLMLLVLAGATYFpepvFSGIDISQVH 342
Cdd:cd07338   73 ARVAVTRGLLDILNRDELEAVIGHELGHIKHRDVAIMTAI--GLI--------PSIIYYIGRSLLF----SGGSSGGRNG 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 343 SVLMGAILICFFIVYfrFVFGFFMRNFER----QADLYLFRFFPNAFPLIRTFYKIGAISRQDMerpNWHHFSIGQRIRF 418
Cdd:cd07338  139 GGALLAVGIAAFAVY--FLFQLLVLGFSRlreyYADAHSAKVTGNGRALQSALAKIAYGYLAEI---FSTHPLPAKRIQA 213


                 ...
gi 636808205 419 LEK 421
Cdd:cd07338  214 LEK 216
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 476-598 7.75e-11

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 65.01  E-value: 7.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 476 LEQLKMDPENADLHVVAGDFHYASQNFIQAIAAYESAIGINSNHVHALNNLAWLLAtcpvtEIQDPGRALNLAGRAVGLA 555
Cdd:COG3914   68 AAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLL-----ALGRLEEALAALRRALALN 142

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 636808205 556 PQSPFVQDTYAEALFANHRVAEAVSAARKALELARDRQNYYQN 598
Cdd:COG3914  143 PDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNN 185
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 496-589 1.23e-10

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 60.36  E-value: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 496 HYASQNFIQAIAAYESAIGINSNHVHALNNLAWLLAtcpvtEIQDPGRALNLAGRAVGLAPQSPFVQDTYAEALFANHRV 575
Cdd:COG5010   64 YNKLGDFEESLALLEQALQLDPNNPELYYNLALLYS-----RSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQD 138

                         90
                 ....*....|....
gi 636808205 576 AEAVSAARKALELA 589
Cdd:COG5010  139 DEAKAALQRALGTS 152
Peptidase_M48 pfam01435
Peptidase family M48; Peptidase_M48 is the largely extracellular catalytic region of CAAX ...
 264-421 2.04e-10

Peptidase family M48; Peptidase_M48 is the largely extracellular catalytic region of CAAX prenyl protease homologs such as Human FACE-1 protease. These are metallopeptidases, with the characteriztic HExxH motif giving the two histidine-zinc-ligands and an adjacent glutamate on the next helix being the third. The whole molecule folds to form a deep groove/cleft into which the substrate can fit.


Pssm-ID: 426263 [Multi-domain]  Cd Length: 201  Bit Score: 60.52  E-value: 2.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205  264 YILVTPALLGSL-NDEELAAVILHEIGHVKHWHMLYYLVFFAGFIACNAVLYDPLMLLVLAGATYFpepvfsGIDISQVH 342
Cdd:pfam01435  48 RVVVTTGLLDLLeTEDELAAVLGHEIGHIKARHSVESLSIMGGLSLAQLFLALLLLGAAASGFANF------GIIFLLLI 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205  343 SVLMGAIlicffivyfRFVFGFFMRNFERQADLYLFRFFPNAFPLIRTFYKI-GAISR-----QDMERPNWH--HFSIGQ 414
Cdd:pfam01435 122 GPLAALL---------TLLLLPYSRAQEYEADRLGAELMARAGYDPRALIKLwGEIDNngrasDGALYPELLstHPSLVE 192


                  ....*..
gi 636808205  415 RIRFLEK 421
Cdd:pfam01435 193 RIAALRE 199
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
496-591 3.39e-10

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 57.10  E-value: 3.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 496 HYASQNFIQAIAAYESAIGINSNHVHALNNLAWLLAtcpvtEIQDPGRALNLAgRAVGLAPQSPFVQDTYAEALFANHRV 575
Cdd:COG3063    2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLL-----EQGRYDEAIALE-KALKLDPNNAEALLNLAELLLELGDY 75

                         90
                 ....*....|....*.
gi 636808205 576 AEAVSAARKALELARD 591
Cdd:COG3063   76 DEALAYLERALELDPS 91
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 456-596 1.01e-09

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 59.74  E-value: 1.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 456 HLSYGQFKPGIDNFvtgrlvLEQLKMDPENADLHVVAGDFHYASQNFIQAIAAYESAIGINSNHVHALNNLAWLLAtcpv 535
Cdd:COG2956   18 YLLNGQPDKAIDLL------EEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYL---- 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 636808205 536 tEIQDPGRALNLAGRAVGLAPQSPFVQDTYAEALFANHRVAEAVSAARKALELARDRQNYY 596
Cdd:COG2956   88 -KAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAY 147
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 479-591 1.09e-09

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 59.74  E-value: 1.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 479 LKMDPENADLHVVAGDFHYASQNFIQAIAAYESAIGINSNHVHALNNLAWLLAtcpvtEIQDPGRALNLAGRAVGLAPQS 558
Cdd:COG2956   69 LERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYE-----QEGDWEKAIEVLERLLKLGPEN 143

                         90       100       110
                 ....*....|....*....|....*....|...
gi 636808205 559 PFVQDTYAEALFANHRVAEAVSAARKALELARD 591
Cdd:COG2956  144 AHAYCELAELYLEQGDYDEAIEALEKALKLDPD 176
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 484-598 7.40e-09

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 54.43  E-value: 7.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 484 ENADLHVVAGDFHYASQNFIQAIAAYESAIGINSNHVHALNNLAWLLAtcpvtEIQDPGRALNLAGRAVGLAPQSPFVQD 563
Cdd:COG4783    2 ACAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILL-----QLGDLDEAIVLLHEALELDPDEPEARL 76

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 636808205 564 TYAEALFANHRVAEAVSAARKALELARDRQNYYQN 598
Cdd:COG4783   77 NLGLALLKAGDYDEALALLEKALKLDPEHPEAYLR 111
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 476-587 1.05e-08

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 56.66  E-value: 1.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 476 LEQ-LKMDPENADLHVVAGDFHYASQNFIQAIAAYESAIGINSNHVHALNNLAWLLAtcpvtEIQDPGRALNLAGRAVGL 554
Cdd:COG2956  167 LEKaLKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYE-----KLGDPEEALELLRKALEL 241

                         90       100       110
                 ....*....|....*....|....*....|...
gi 636808205 555 APQSPfVQDTYAEALFANHRVAEAVSAARKALE 587
Cdd:COG2956  242 DPSDD-LLLALADLLERKEGLEAALALLERQLR 273
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 475-591 1.21e-08

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 56.66  E-value: 1.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 475 VLEQL-KMDPENADLHVVAGDFHYASQNFIQAIAAYESAIGINSNHVHALNNLAWLLAtcpvtEIQDPGRALNLAGRAVG 553
Cdd:COG2956  132 VLERLlKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYL-----EQGDYEEAIAALERALE 206

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 636808205 554 LAPQSPFVQDTYAEALFANHRVAEAVSAARKALELARD 591
Cdd:COG2956  207 QDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPS 244
M56_like cd07329
Peptidase M56-like, integral membrane metallopeptidase in bacteria; This family contains ...
 259-409 5.36e-08

Peptidase M56-like, integral membrane metallopeptidase in bacteria; This family contains peptidase M56, which includes zinc metalloprotease domain in MecR1 as well as BlaR1. MecR1 is a transmembrane beta-lactam sensor/signal transducer protein that regulates the expression of an altered penicillin-binding protein PBP2a, which resists inactivation by beta-lactam antibiotics, in methicillin-resistant Staphylococcus aureus (MRSA). BlaR1 regulates the inducible expression of a class A beta-lactamase that hydrolytically destroys certain beta-lactam antibiotics in MRSA. Both, MecR1 and BlaR1, are transmembrane proteins that consist of four transmembrane helices, a cytoplasmic zinc protease domain, and the soluble C-terminal extracellular sensor domain, and are highly similar in sequence and function. The signal for protein expression is transmitted by site-specific proteolytic cleavage of both the transducer, which auto-activates, and the repressor, which is inactivated, unblocking gene transcription. All members contain the zinc metalloprotease motif (HEXXH). Homologs of this peptidase domain are also found in a number of other bacterial genome sequences, most of which are as yet uncharacterized.


Pssm-ID: 320688 [Multi-domain]  Cd Length: 188  Bit Score: 53.22  E-value: 5.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 259 VGKFR--YILVTPALLGSLNDEELAAVILHEIGHVKHWHMLYYLVFfagfiacnavlyDPLMLLVLAGATYFpepVFSGI 336
Cdd:cd07329   27 VGRSRgpTVVVTTGLLDLLDDDELEAVLAHELAHLKRRDVLVLLLF------------DPLLLLVVGLLLFL---SLFIF 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 636808205 337 DISQVHSVLMGAILICFFIVYFRFVFGFFMRNFERQADLYLFRFFPNAfpLIRTFYKIGAISRQDMERPNWHH 409
Cdd:cd07329   92 ELLGFFFQPLLFLAFFALLRLAELLADALAVARTSAARRARLTGLPAA--LASALEKIEDASDRALEAGLVLP 162
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 457-609 5.60e-08

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 55.86  E-value: 5.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205  457 LSYGQFKPGIdnfvtgRLVLEQLKMDPENADLHVVAGDFHYASQNFIQAIAAYESAIGINSNHVHALNNLAWLLatcpvT 536
Cdd:TIGR02917 170 LAENRFDEAR------ALIDEVLTADPGNVDALLLKGDLLLSLGNIELALAAYRKAIALRPNNIAVLLALATIL-----I 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205  537 EIQDPGRALNLAGRAVGLAPQSPFVqdTYAEAL--FANHRVAEAVSAARKALELARDRQN---------YYQNQVRRFQR 605
Cdd:TIGR02917 239 EAGEFEEAEKHADALLKKAPNSPLA--HYLKALvdFQKKNYEDARETLQDALKSAPEYLPalllagaseYQLGNLEQAYQ 316


                  ....
gi 636808205  606 HLER 609
Cdd:TIGR02917 317 YLNQ 320
M48_Ste24p_like cd07325
M48 Ste24 endopeptidase-like, integral membrane metallopeptidase; This family contains ...
 248-323 5.64e-08

M48 Ste24 endopeptidase-like, integral membrane metallopeptidase; This family contains peptidase M48 family Ste24p-like proteins that are as yet uncharacterized, but probably function as intracellular, membrane-associated zinc metalloproteases; they all contain the HEXXH Zn-binding motif, which is critical for Ste24p activity. They likely remove the C-terminal three residues of farnesylated proteins proteolytically and are possibly associated with the endoplasmic reticulum and golgi. Some members also contain ankyrin domains which occur in very diverse families of proteins and mediate protein-protein interactions.


Pssm-ID: 320684 [Multi-domain]  Cd Length: 199  Bit Score: 53.38  E-value: 5.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 248 GSMITAGVMGLVGKfRYILVTPALLGSLNDEELAAVILHEIGHVK----HWHMLYYLVFFAGFIACNAVLYDPLMLLVLA 323
Cdd:cd07325   39 SPVLNAFALGFEGR-PFIVLNSGLVELLDDDELRFVIGHELGHIKsghvLYRTLLLLLLLLGELIGILLLSSALPLALLA 117
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 504-588 5.97e-08

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 51.55  E-value: 5.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 504 QAIAAYESAIGINSNHVHALNNLAWLLAtcpvtEIQDPGRALNLAGRAVGLAPQSPFVQDTYAEALFANHRVAEAVSAAR 583
Cdd:COG4235    1 EAIARLRQALAANPNDAEGWLLLGRAYL-----RLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLE 75


                 ....*
gi 636808205 584 KALEL 588
Cdd:COG4235   76 RALAL 80
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 479-578 7.10e-08

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 51.55  E-value: 7.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 479 LKMDPENADLHVVAGDFHYASQNFIQAIAAYESAIGINSNHVHALNNLAWLLAtcpvtEIQDPGRALNLAGRAVGLAPQS 558
Cdd:COG4235   44 LRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAF-----QQGDYAEAIAAWQKLLALLPAD 118

                         90       100
                 ....*....|....*....|
gi 636808205 559 pfvqdtyAEALFANHRVAEA 578
Cdd:COG4235  119 -------APARLLEASIAEA 131
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 479-605 7.56e-08

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 53.96  E-value: 7.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 479 LKMDPENADLHVVAGDFHYASQNFIQAIAAYESAIGINSNHVHALNNLAWLLAtcpvtEIQDPGRALNLAGRAVGLAPQS 558
Cdd:COG2956  103 LELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYL-----EQGDYDEAIEALEKALKLDPDC 177

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 636808205 559 PFVQDTYAEALFANHRVAEAVSAARKALELARDRQNYYQNQVRRFQR 605
Cdd:COG2956  178 ARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEK 224
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 479-594 1.14e-06

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 51.53  E-value: 1.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 479 LKMDPENADLHVVAGDFHYASQNFIQAIAAYESAIGINSNHVHALNNLAWLLAtcpvtEIQDPGRALNLAGRAVGLAPQS 558
Cdd:COG3914  139 LALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQ-----DLGRLEEAIAAYRRALELDPDN 213

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 636808205 559 PFVqdtYAEALFANHRVAEAVSAARKALELARDRQN 594
Cdd:COG3914  214 ADA---HSNLLFALRQACDWEVYDRFEELLAALARG 246
M48C_Oma1_like cd07332
Peptidase M48C Ste24p, integral membrane endopeptidase; This subfamily contains peptidase M48C ...
 264-421 1.46e-06

Peptidase M48C Ste24p, integral membrane endopeptidase; This subfamily contains peptidase M48C Oma1 (also called mitochondrial metalloendopeptidase OMA1) protease homologs that are mostly uncharacterized. Oma1 is part of the quality control system in the inner membrane of mitochondria, with its catalytic site facing the matrix space. It cleaves and thereby promotes the turnover of mistranslated or misfolded membrane proteins. Oma1 can cleave the misfolded multi-pass membrane protein Oxa1, thus exerting a function similar to the ATP-dependent m-AAA protease for quality control of inner membrane proteins; it cleaves a misfolded polytopic membrane protein at multiple sites. It has been proposed that in the absence of m-AAA protease, proteolysis of Oxa1 is mediated by Oma1 in an ATP-independent manner. Oma1 is part of highly conserved mitochondrial metallopeptidases, with homologs present in higher eukaryotes, eubacteria and archaebacteria, all containing the zinc binding motif (HEXXH). It forms a high molecular mass complex in the inner membrane, possibly a homo-hexamer.


Pssm-ID: 320691 [Multi-domain]  Cd Length: 222  Bit Score: 49.49  E-value: 1.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 264 YILVTPALLGSL-NDEELAAVILHEIGHVKHWHMLyylvffagfiacNAVLYDPLMLLVLAgatyfpepVFSGiDISQVH 342
Cdd:cd07332   87 TIVVTDGLVELAeSPEELAAVLAHEIGHVEHRHSL------------RQLIRSSGLSLLVS--------LLTG-DVSGLS 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 343 SVLMGAIlicffivyfRFVFGF-FMRNFERQADLYLFRFFPNA----FPLIRTFYKIGAISRQDMERPNW--HHFSIGQR 415
Cdd:cd07332  146 DLLAGLP---------ALLLSLsYSRDFEREADAFALELLKAAgispEGLADFFERLEEEHGDGGSLPEWlsTHPDTEER 216


                 ....*.
gi 636808205 416 IRFLEK 421
Cdd:cd07332  217 IEAIRE 222
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
479-556 1.53e-06

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 46.70  E-value: 1.53e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 636808205 479 LKMDPENADLHVVAGDFHYASQNFIQAIaAYESAIGINSNHVHALNNLAWLLAtcpvtEIQDPGRALNLAGRAVGLAP 556
Cdd:COG3063   19 LELDPDNADALNNLGLLLLEQGRYDEAI-ALEKALKLDPNNAEALLNLAELLL-----ELGDYDEALAYLERALELDP 90
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 479-556 3.87e-06

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 47.26  E-value: 3.87e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 636808205 479 LKMDPENADLHVVAGDFHYASQNFIQAIAAYESAIGINSNHVHALNNLAWLLAtcpvtEIQDPGRALNLAGRAVGLAP 556
Cdd:COG5010   81 LQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLL-----SLGQDDEAKAALQRALGTSP 153
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 491-605 4.03e-06

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 48.96  E-value: 4.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 491 VAGDFHYASQNFIQAIAAYESAIGINSNHVHALNNLAWLLAtcpvtEIQDPGRALNLAGRAVGLAPQSPFVQDTYAEALF 570
Cdd:COG2956   13 FKGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLYR-----RRGEYDRAIRIHQKLLERDPDRAEALLELAQDYL 87

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 636808205 571 ANHRVAEAVSAARKALELARDRQNYYQNQVRRFQR 605
Cdd:COG2956   88 KAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQ 122
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
479-599 6.01e-06

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 47.60  E-value: 6.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 479 LKMDPENADLHVVAGDFHYASQNFIQAIAAYESAIGINSNHVHALNNLAWLLAtcpvtEIQDPGRALNLAGRAVGLAPQS 558
Cdd:COG4785  100 LELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLNRGIALY-----YLGRYELAIADLEKALELDPND 174

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 636808205 559 PFvqdTYAEALFANHRVAEAvsAARKalELARDRQNYYQNQ 599
Cdd:COG4785  175 PE---RALWLYLAERKLDPE--KALA--LLLEDWATAYLLQ 208
Peptidase_M48_M56 cd05843
Peptidases M48 (Ste24 endopeptidase or htpX homolog) and M56 (in MecR1 and BlaR1), integral ...
 263-292 7.45e-06

Peptidases M48 (Ste24 endopeptidase or htpX homolog) and M56 (in MecR1 and BlaR1), integral membrane metallopeptidases; This family contains peptidase M48 (also known as Ste24 peptidase, Ste24p, Ste24 endopeptidase, a-factor converting enzyme, AFC1), M56 (also known as BlaR1 peptidase) as well as a novel family called minigluzincins. Peptidase M48 belongs to Ste24 endopeptidase family. Members of this family include Ste24 protease (peptidase M48A), protease htpX homolog (peptidase M48B), or CAAX prenyl protease 1, and mitochondrial metalloendopeptidase OMA1 (peptidase M48C). They proteolytically remove the C-terminal three residues of farnesylated proteins. They are integral membrane proteins associated with the endoplasmic reticulum and golgi, binding one zinc ion per subunit. In eukaryotes, Ste24p is required for the first NH2-terminal proteolytic processing event within the a-factor precursor, which takes place after COOH-terminal CAAX modification (C is cysteine; A is usually aliphatic; X is one of several amino acids) is complete. The Ste24p contains multiple membrane spans, a zinc metalloprotease motif (HEXXH), and a COOH-terminal ER retrieval signal (KKXX). Mutation studies have shown that the HEXXH protease motif, which is extracellular but adjacent to a transmembrane domain and therefore close to the membrane surface, is critical for Ste24p activity. Ste24p has limited homology to HtpX family of prokaryotic proteins; HtpX proteins, also part of the M48 peptidase family, are smaller and homology is restricted to the C-terminal half of Ste24p. HtpX expression is controlled by the Cpx stress response system, which senses abnormal membrane proteins; HtpX then undergoes self-degradation and collaborates with FtsH to eliminate these misfolded proteins. Peptidase M56 includes zinc metalloprotease domain in MecR1 and BlaR1. MecR1 is a transmembrane beta-lactam sensor/signal transducer protein that regulates the expression of an altered penicillin-binding protein PBP2a, which resists inactivation by beta-lactam antibiotics, in methicillin-resistant Staphylococcus aureus (MRSA). BlaR1 regulates the inducible expression of a class A beta-lactamase that hydrolytically destroys certain beta-lactam antibiotics in MRSA. Also included are a novel family of related proteins that consist of the soluble minimal scaffold similar to the catalytic domains of the integral-membrane metallopeptidase M48 and M56, thus called minigluzincins.


Pssm-ID: 320682 [Multi-domain]  Cd Length: 94  Bit Score: 44.75  E-value: 7.45e-06
                         10        20        30
                 ....*....|....*....|....*....|
gi 636808205 263 RYILVTPALLGSLNDEELAAVILHEIGHVK 292
Cdd:cd05843   38 KRVVLTTALLELLSEEELAAVIAHELGHFK 67
M56_BlaR1_MecR1_like cd07326
Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; ...
 259-317 1.11e-05

Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; This family contains peptidase M56, which includes zinc metalloprotease domain in MecR1 as well as BlaR1. MecR1 is a transmembrane beta-lactam sensor/signal transducer protein that regulates the expression of an altered penicillin-binding protein PBP2a, which resists inactivation by beta-lactam antibiotics, in methicillin-resistant Staphylococcus aureus (MRSA). BlaR1 regulates the inducible expression of a class A beta-lactamase that hydrolytically destroys certain ?-lactam antibiotics in MRSA. Both, MecR1 and BlaR1, are transmembrane proteins that consist of four transmembrane helices, a cytoplasmic zinc protease domain, and the soluble C-terminal extracellular sensor domain, and are highly similar in sequence and function. The signal for protein expression is transmitted by site-specific proteolytic cleavage of both the transducer, which auto-activates, and the repressor, which is inactivated, unblocking gene transcription. All members contain the zinc metalloprotease motif (HEXXH). Homologs of this peptidase domain are also found in a number of other bacterial genome sequences, most of which are as yet uncharacterized.


Pssm-ID: 320685 [Multi-domain]  Cd Length: 165  Bit Score: 46.15  E-value: 1.11e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 259 VGKFR-YILVTPALLGSLNDEELAAVILHEIGHVKHWHMLyyLVFFAGFIAcNAVLYDPL 317
Cdd:cd07326   42 LGGRRpRIVLSTGLLELLSPEELRAVLAHERAHLRRRDPL--LLLLASALA-RALPFLPL 98
MecR1 COG4219
Signal transducer regulating beta-lactamase production, contains metallopeptidase domain ...
 191-309 3.00e-05

Signal transducer regulating beta-lactamase production, contains metallopeptidase domain [Signal transduction mechanisms];


Pssm-ID: 443363 [Multi-domain]  Cd Length: 337  Bit Score: 46.58  E-value: 3.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 191 IIIMVFMAGIAVFGPV-FIKTIWQCRPMEKGPGRSRIEAVCHMAGLRYA-DILIWDLFAGSMitagVMGLVgkFRYILVt 268
Cdd:COG4219    2 LAGVLLLLLRLLISLLrLRRLLRRARPVTDEELLELLERLARRLGIRRPvRLLESDRITSPF----SFGLL--RPVILL- 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 636808205 269 PALLGSLNDEELAAVILHEIGHVKHWHmlYYLVFFAGFIAC 309
Cdd:COG4219   75 PAGLEELSEEELEAILAHELAHIRRRD--LLDNLLAELLLA 113
M48B_HtpX_like cd07336
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ...
 267-293 3.87e-05

Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of peptidase M48 subfamily B includes uncharacterized HtpX homologs and consists of proteins smaller than Ste24p, with homology restricted to the C-terminal half of Ste24p. HtpX expression is controlled by the Cpx stress response system, which senses abnormal membrane proteins. HtpX participates in the proteolytic quality control of these misfolded proteins by undergoing self-degradation and collaborating with FtsH, a membrane-bound and ATP-dependent protease, to eliminate them. HtpX, a zinc metalloprotease with an active site motif HEXXH, has an FtsH-like topology, and is capable of introducing endoproteolytic cleavages into SecY (also an FtsH substrate). However, HtpX does not have an ATPase activity and will only act against cytoplasmic regions of a target membrane protein. Thus, HtpX and FtsH have overlapping and/or complementary functions, which are especially important at high temperature; in E. coli and Xylella fastidiosa, HtpX is heat-inducible, while in Streptococcus gordonii it is not.


Pssm-ID: 320695 [Multi-domain]  Cd Length: 266  Bit Score: 45.56  E-value: 3.87e-05
                         10        20
                 ....*....|....*....|....*..
gi 636808205 267 VTPALLGSLNDEELAAVILHEIGHVKH 293
Cdd:cd07336   99 VTTGILRLLDKDELEGVLAHELAHIKN 125
M48B_HtpX_like cd07327
HtpX-like membrane-bound metallopeptidase; This family contains peptidase M48 subfamily B, ...
 264-297 3.90e-05

HtpX-like membrane-bound metallopeptidase; This family contains peptidase M48 subfamily B, also known as HtpX, which consists of proteins smaller than Ste24p, with homology restricted to the C-terminal half of Ste24p. HtpX, an integral membrane (IM) metallopeptidase, is widespread in bacteria and archaea, and plays a central role in protein quality control by preventing the accumulation of misfolded proteins in the membrane. Its expression is controlled by the Cpx stress response system, which senses abnormal membrane proteins. HtpX participates in the proteolytic quality control of these misfolded proteins by undergoing self-degradation and eliminating them by collaborating with FtsH, a membrane-bound and ATP-dependent protease. HtpX contains the zinc binding motif (HEXXH), has an FtsH-like topology, and is capable of introducing endoproteolytic cleavages into SecY (also an FtsH substrate). However, HtpX does not have an ATPase activity and will only act against cytoplasmic regions of a target membrane protein. Thus, HtpX and FtsH have overlapping and/or complementary functions, which are especially important at high temperature; in E. coli and Xylella fastidiosa, HtpX is heat-inducible, while in Streptococcus gordonii it is not. Mutation studies of HtpX-like M48 metalloprotease from Leptospira interrogans (LA4131) has been shown to result in altered expression of a subset of metal toxicity and stress response genes.


Pssm-ID: 320686 [Multi-domain]  Cd Length: 183  Bit Score: 44.55  E-value: 3.90e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 636808205 264 YILVTPALLGSLNDEELAAVILHEIGHVKHWHML 297
Cdd:cd07327   65 AVAVTTGLLQLLNEDELEAVLAHELSHIKNRDVL 98
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
482-589 6.87e-05

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 44.52  E-value: 6.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 482 DPENADLHVVAGDFHYASQNFIQAIAAYESAIGINSNHVHALNNLAWLLatcpvTEIQDPGRALNLAGRAVGLAPQSPFV 561
Cdd:COG4785   69 LPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAY-----LLLGDYDAALEDFDRALELDPDYAYA 143

                         90       100
                 ....*....|....*....|....*...
gi 636808205 562 QDTYAEALFANHRVAEAVSAARKALELA 589
Cdd:COG4785  144 YLNRGIALYYLGRYELAIADLEKALELD 171
M48B_HtpX_like cd07337
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ...
 262-376 8.36e-05

Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of peptidase M48 subfamily B includes uncharacterized HtpX homologs and consists of proteins smaller than Ste24p, with homology restricted to the C-terminal half of Ste24p. HtpX expression is controlled by the Cpx stress response system, which senses abnormal membrane proteins. HtpX participates in the proteolytic quality control of these misfolded proteins by undergoing self-degradation and collaborating with FtsH, a membrane-bound and ATP-dependent protease, to eliminate them. HtpX, a zinc metalloprotease with an active site motif HEXXH, has an FtsH-like topology, and is capable of introducing endoproteolytic cleavages into SecY (also an FtsH substrate). However, HtpX does not have an ATPase activity and will only act against cytoplasmic regions of a target membrane protein. Thus, HtpX and FtsH have overlapping and/or complementary functions, which are especially important at high temperature; in E. coli and Xylella fastidiosa, HtpX is heat-inducible, while in Streptococcus gordonii it is not.


Pssm-ID: 320696 [Multi-domain]  Cd Length: 203  Bit Score: 43.84  E-value: 8.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 262 FRYILVTPALLGSLNDEELAAVILHEIGHVKHWHMLYYLVFFagfiacnavlydplMLLVLAgatyfpePVFSgidisqv 341
Cdd:cd07337   76 RNTICVTKGLLDLLDYEELKGILAHELGHLSHKDTDYLLLIF--------------VLLLLA-------AIWT------- 127

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 636808205 342 hsvLMGAILICFFIVYFrfvFGFFMRNFERQADLY 376
Cdd:cd07337  128 ---KLGTLLIFVWIRLL---VMFSSRKAEYRADAF 156
M48B_Htpx_like cd07340
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ...
 265-309 9.49e-05

Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of peptidase M48 subfamily B includes uncharacterized HtpX homologs and consists of proteins smaller than Ste24p, with homology restricted to the C-terminal half of Ste24p. HtpX expression is controlled by the Cpx stress response system, which senses abnormal membrane proteins. HtpX participates in the proteolytic quality control of these misfolded proteins by undergoing self-degradation and collaborating with FtsH, a membrane-bound and ATP-dependent protease, to eliminate them. HtpX, a zinc metalloprotease with an active site motif HEXXH, has an FtsH-like topology, and is capable of introducing endoproteolytic cleavages into SecY (also an FtsH substrate). However, HtpX does not have an ATPase activity and will only act against cytoplasmic regions of a target membrane protein. Thus, HtpX and FtsH have overlapping and/or complementary functions, which are especially important at high temperature; in E. coli and Xylella fastidiosa, HtpX is heat-inducible, while in Streptococcus gordonii it is not.


Pssm-ID: 320699 [Multi-domain]  Cd Length: 246  Bit Score: 44.41  E-value: 9.49e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 636808205 265 ILVTPALLGSLNDEELAAVILHEIGHVKHWHMLY--YLVFFAGFIAC 309
Cdd:cd07340   71 IAVTTGLLEKLNRDELEGVIAHELSHIKNYDIRLmtIAVVLVGIIAL 117
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 479-594 1.10e-04

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 45.46  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205  479 LKMDPENADLHVVAGDFHYASQNFIQAIAAYESAIGINSNHVHALNNLAWLLAtcpvtEIQDPGRALNLAGRAVGLAPQS 558
Cdd:TIGR02917 628 LALQPDSALALLLLADAYAVMKNYAKAITSLKRALELKPDNTEAQIGLAQLLL-----AAKRTESAKKIAKSLQKQHPKA 702

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 636808205  559 PFVQDTYAEALFANHRVAEAVSAARKALELARDRQN 594
Cdd:TIGR02917 703 ALGFELEGDLYLRQKDYPAAIQAYRKALKRAPSSQN 738
M48C_Oma1-like cd07324
Oma1 peptidase-like, integral membrane metallopeptidase; This family contains peptidase M48 ...
 264-297 1.12e-04

Oma1 peptidase-like, integral membrane metallopeptidase; This family contains peptidase M48 subfamily C (also known as Oma1 peptidase or mitochondrial metalloendopeptidase OMA1), including similar peptidases containing tetratricopeptide (TPR) repeats, as well as uncharacterized proteins such as E. coli bepA (formerly yfgC), ycaL and loiP (formerly yggG), considered to be putative metallopeptidases. Oma1 peptidase is part of the quality control system in the inner membrane of mitochondria, with its catalytic site facing the matrix space. It cleaves and thereby promotes the turnover of mistranslated or misfolded membrane proteins. Oma1 can cleave the misfolded multi-pass membrane protein Oxa1, thus exerting a function similar to the ATP-dependent m-AAA protease for quality control of inner membrane proteins. It has been proposed that in the absence of m-AAA protease, proteolysis of Oxa1 is mediated by Oma1 in an ATP-independent manner. Homologs of Oma1 are present in higher eukaryotes, eubacteria and archaebacteria, suggesting that Oma1 is the founding member of a conserved family of membrane-embedded metallopeptidases, all containing the zinc metalloprotease motif (HEXXH). M48 peptidases proteolytically remove the C-terminal three residues of farnesylated proteins.


Pssm-ID: 320683 [Multi-domain]  Cd Length: 142  Bit Score: 42.55  E-value: 1.12e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 636808205 264 YILVTPALLGSLNDE-ELAAVILHEIGHVKHWHML 297
Cdd:cd07324   39 YIFVTTGLLLLLESEdELAAVLAHEIGHVTLRHIA 73
COG4784 COG4784
Putative Zn-dependent protease [General function prediction only];
264-291 1.39e-04

Putative Zn-dependent protease [General function prediction only];


Pssm-ID: 443814 [Multi-domain]  Cd Length: 488  Bit Score: 44.88  E-value: 1.39e-04
                         10        20
                 ....*....|....*....|....*....
gi 636808205 264 YILVTPALLGSLNDE-ELAAVILHEIGHV 291
Cdd:COG4784  108 YVYVTRGLLALANDEaELAAVLGHEIGHV 136
M56_BlaR1_MecR1_like cd07341
Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; ...
 195-301 2.41e-04

Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; This family contains peptidase M56, which includes zinc metalloprotease domain in MecR1 as well as BlaR1. MecR1 is a transmembrane beta-lactam sensor/signal transducer protein that regulates the expression of an altered penicillin-binding protein PBP2a, which resists inactivation by beta-lactam antibiotics, in methicillin-resistant Staphylococcus aureus (MRSA). BlaR1 regulates the inducible expression of a class A beta-lactamase that hydrolytically destroys certain ?-lactam antibiotics in MRSA. Both, MecR1 and BlaR1, are transmembrane proteins that consist of four transmembrane helices, a cytoplasmic zinc protease domain, and the soluble C-terminal extracellular sensor domain, and are highly similar in sequence and function. The signal for protein expression is transmitted by site-specific proteolytic cleavage of both the transducer, which auto-activates, and the repressor, which is inactivated, unblocking gene transcription. All members contain the zinc metalloprotease motif (HEXXH). Homologs of this peptidase domain are also found in a number of other bacterial genome sequences, most of which are as yet uncharacterized.


Pssm-ID: 320700 [Multi-domain]  Cd Length: 187  Bit Score: 42.32  E-value: 2.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 195 VFMAGIAVFGPVFIKTIWQCRPM---EKGPGRSRIEAVCHMAGLRYAD-ILIWDLFAGSMItagvmglVGKFRYILVTPA 270
Cdd:cd07341    1 IWLAGALLLLLRLLRGLLRLRRLrrrAEPVPDSLLLELARRLGLRRSVrLSVSALVASPMV-------VGLFRPVILLPE 73

                         90       100       110
                 ....*....|....*....|....*....|.
gi 636808205 271 LLGSLNDEELAAVILHEIGHVKHWHMLYYLV 301
Cdd:cd07341   74 GLLEGSPEELRAILLHELAHIRRRDLLVNLL 104
M48C_loiP_like cd07334
Peptidase M48C Ste24p loiP-like, integral membrane protein; This subfamily contains peptidase ...
 271-295 3.25e-04

Peptidase M48C Ste24p loiP-like, integral membrane protein; This subfamily contains peptidase M48 Ste24p protease loiP (formerly yggG)-like family are mostly uncharacterized proteins that include E. coli loiP and ycaLG, considered to be putative metallopeptidases, containing a zinc-binding motif, HEXXH, and a COOH-terminal ER retrieval signal (KKXX). They proteolytically remove the C-terminal three residues of farnesylated proteins. They are integral membrane proteins associated with the endoplasmic reticulum and golgi, binding one zinc ion per subunit. In eukaryotes, Ste24p is required for the first NH2-terminal proteolytic processing event within the a-factor precursor, which takes place after COOH-terminal CAAX modification (C is cysteine; A is usually aliphatic; X is one of several amino acids) is complete. Mutation studies have shown that the HEXXH protease motif, which is extracellular but adjacent to a transmembrane domain and therefore close to the membrane surface, is critical for Ste24p activity. LoiP has been shown to be a metallopeptidase that cleaves its targets preferentially between Phe-Phe residues. It is upregulated when bacteria are subjected to media of low osmolarity, thus yggG was named LoiP (low osmolarity induced protease). Proper membrane localization of LoiP may depend on YfgC, another putative metalloprotease in this subfamily.


Pssm-ID: 320693 [Multi-domain]  Cd Length: 215  Bit Score: 42.19  E-value: 3.25e-04
                         10        20
                 ....*....|....*....|....*
gi 636808205 271 LLGSLNDEELAAVILHEIGHVKHWH 295
Cdd:cd07334   85 LMDMMTDDELLGVIGHEIGHVKLGH 109
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 473-597 3.37e-04

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 43.92  E-value: 3.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205  473 RLVLEQ-LKMDPENAD-LHVVAgDFHYASQNFIQAIAAYESAIGINSNHVHALNNLAWLLAtcpvtEIQDPGRALNLAGR 550
Cdd:TIGR02917 485 REAFEKaLSIEPDFFPaAANLA-RIDIQEGNPDDAIQRFEKVLTIDPKNLRAILALAGLYL-----RTGNEEEAVAWLEK 558

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 636808205  551 AVGLAPQ--SPFVQdtYAEALFANHRVAEAVSAARKALELARDRQNYYQ 597
Cdd:TIGR02917 559 AAELNPQeiEPALA--LAQYYLGKGQLKKALAILNEAADAAPDSPEAWL 605
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 479-598 4.61e-04

mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 273380 [Multi-domain]  Cd Length: 615  Bit Score: 43.05  E-value: 4.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205  479 LKMDPENADLHVVAGDFHYASQNFIQAIAAYESAIGINSNHVHALNNLAwllatCPVTEIQDPGRALNLAGRAVGLAPQS 558
Cdd:TIGR00990 392 LKLNSEDPDIYYHRAQLHFIKGEFAQAGKDYQKSIDLDPDFIFSHIQLG-----VTQYKEGSIASSMATFRRCKKNFPEA 466

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 636808205  559 PFVQDTYAEALFANHRVAEAVSAARKALELARDRQNYYQN 598
Cdd:TIGR00990 467 PDVYNYYGELLLDQNKFDEAIEKFDTAIELEKETKPMYMN 506
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 540-598 6.68e-04

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 40.71  E-value: 6.68e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 636808205 540 DPGRALNLAGRAVGLAPQSPFVQDTYAEALFANHRVAEAVSAARKALELARDRQNYYQN 598
Cdd:COG5010   69 DFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSN 127
M48C_bepA_like cd07333
Peptidase M48C Ste24p bepA-like, integral membrane protein; This family contains peptidase ...
 264-294 1.16e-03

Peptidase M48C Ste24p bepA-like, integral membrane protein; This family contains peptidase M48C Ste24p protease bepA (formerly yfgC)-like proteins considered to be putative metallopeptidases, containing a zinc-binding motif, HEXXH, and a COOH-terminal ER retrieval signal (KKXX). They proteolytically remove the C-terminal three residues of farnesylated proteins. They are integral membrane proteins associated with the endoplasmic reticulum and golgi, binding one zinc ion per subunit. In eukaryotes, Ste24p is required for the first NH2-terminal proteolytic processing event within the a-factor precursor, which takes place after COOH-terminal CAAX modification (C is cysteine; A is usually aliphatic; X is one of several amino acids) is complete. Mutation studies have shown that the HEXXH protease motif, which is extracellular but adjacent to a transmembrane domain and therefore close to the membrane surface, is critical for Ste24p activity. Several members of this family also contain tetratricopeptide (TPR) repeat motifs, which are involved in a variety of functions including protein-protein interactions. BepA has been shown to possess protease activity and is responsible for the degradation of incorrectly folded LptD, an essential outer-membrane protein (OMP) involved in OM transport and assembly of lipopolysaccharide. Overexpression of the bepA protease causes abnormal biofilm architecture.


Pssm-ID: 320692 [Multi-domain]  Cd Length: 174  Bit Score: 40.17  E-value: 1.16e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 636808205 264 YILVTPALLGSLNDE-ELAAVILHEIGHV--KHW 294
Cdd:cd07333   66 YIYVNTGLILAADNEaELAGVLAHEIGHVvaRHI 99
PRK03982 PRK03982
heat shock protein HtpX; Provisional
 267-293 2.04e-03

heat shock protein HtpX; Provisional


Pssm-ID: 235186 [Multi-domain]  Cd Length: 288  Bit Score: 40.37  E-value: 2.04e-03
                         10        20
                 ....*....|....*....|....*..
gi 636808205 267 VTPALLGSLNDEELAAVILHEIGHVKH 293
Cdd:PRK03982 112 VTEGILNLLNEDELEGVIAHELTHIKN 138
PRK03001 PRK03001
zinc metalloprotease HtpX;
267-308 3.40e-03

zinc metalloprotease HtpX;


Pssm-ID: 179524 [Multi-domain]  Cd Length: 283  Bit Score: 39.62  E-value: 3.40e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 636808205 267 VTPALLGSLNDEELAAVILHEIGHVKHWHMLYYLV--FFAGFIA 308
Cdd:PRK03001 111 ATTGILRVLSEREIRGVMAHELAHVKHRDILISTIsaTMAGAIS 154
PRK02870 PRK02870
heat shock protein HtpX; Provisional
 265-409 3.57e-03

heat shock protein HtpX; Provisional


Pssm-ID: 235081 [Multi-domain]  Cd Length: 336  Bit Score: 40.09  E-value: 3.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 265 ILVTPALLGSLNDEELAAVILHEIGHVKHWHMLYYLvffagfiaCNAVLYDpLMLLVLAGATYFpepvFSGIDISQVHSV 344
Cdd:PRK02870 158 VAITTGLLEKLDRDELQAVMAHELSHIRHGDIRLTL--------CVGVLSN-IMLIVADFLFYS----FMGNRRNSGANR 224

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 345 LMGAILICFFIV-YFRFVFGFFM-RNFERQAD---LYLFRffpNAFPLIRTFYKIGAISRQDMERPNWHH 409
Cdd:PRK02870 225 ARMIILILRYVLpILTVLLMLFLsRTREYMADagaVELMR---DNEPMARALQKISNDHAQNDEQYAYKH 291
PRK01265 PRK01265
heat shock protein HtpX; Provisional
 191-293 4.07e-03

heat shock protein HtpX; Provisional


Pssm-ID: 234931 [Multi-domain]  Cd Length: 324  Bit Score: 39.73  E-value: 4.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 191 IIIMVFMAGIA--VFGPVFIKTIWQCR---PMEKGPGR--SRIEAVCHMAGLRYADILIWDL-----FAGSMITAGvmgl 258
Cdd:PRK01265  47 ILIFVFFLNIIqwLFGPYMINAAYRTVevtPTDPVYGWlySIVAEVAKYNGIRVPKVYIADVpfpnaFAYGSPIAG---- 122

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 636808205 259 vgkfRYILVTPALLGSLNDEELAAVILHEIGHVKH 293
Cdd:PRK01265 123 ----KRIAITLPLLKILNRDEIKAVAGHELGHLKH 153
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 484-606 5.47e-03

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 39.59  E-value: 5.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 484 ENADLHVVAGDFHYASQNFIQAIAAYESAIGINSNHVHALNNLAWLLAtcpvtEIQDPGRALNLAGRAVGLAPQSPFVQD 563
Cdd:COG3914   42 GLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQ-----ALGRYEEALALYRRALALNPDNAEALF 116

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 636808205 564 TYAEALFANHRVAEAVSAARKALELARDRQNYYQNQVRRFQRH 606
Cdd:COG3914  117 NLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRL 159
M48B_HtpX_like cd07335
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This family contains ...
 265-308 5.65e-03

Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This family contains peptidase M48 subfamily B, also known as HtpX, which consists of proteins smaller than Ste24p, with homology restricted to the C-terminal half of Ste24p. HtpX, an integral membrane (IM) metallopeptidase, is widespread in bacteria and archaea, and plays a central role in protein quality control by preventing the accumulation of misfolded proteins in the membrane. Its expression is controlled by the Cpx stress response system, which senses abnormal membrane proteins. HtpX participates in the proteolytic quality control of these misfolded proteins by undergoing self-degradation and eliminating them by collaborating with FtsH, a membrane-bound and ATP-dependent protease. HtpX contains the zinc binding motif (HEXXH), has an FtsH-like topology, and is capable of introducing endoproteolytic cleavages into SecY (also an FtsH substrate). However, HtpX does not have an ATPase activity and will only act against cytoplasmic regions of a target membrane protein. Thus, HtpX and FtsH have overlapping and/or complementary functions, which are especially important at high temperature; in E. coli and Xylella fastidiosa, HtpX is heat-inducible, while in Streptococcus gordonii it is not. Mutation studies of HtpX-like M48 metalloprotease from Leptospira interrogans (LA4131) has been shown to result in altered expression of a subset of metal toxicity and stress response genes.


Pssm-ID: 320694 [Multi-domain]  Cd Length: 240  Bit Score: 38.72  E-value: 5.65e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 636808205 265 ILVTPALLGSLNDEELAAVILHEIGHVKHWHML----------YYLVFFAGFIA 308
Cdd:cd07335   76 VAVSTGLLDNMSEDEVEAVLAHEISHIANGDMVtmtllqgvvnTFVIFLSRIIA 129
HemYx COG3071
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to ...
 476-556 7.59e-03

Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to protoporphyrinogen oxidase HemY) [Function unknown];


Pssm-ID: 442305 [Multi-domain]  Cd Length: 323  Bit Score: 38.74  E-value: 7.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 476 LEQ-LKMDPENADLHVVAGDFHYASQNFIQAIAAYESAIGINSN-HVHALnnLAWLLAtcpvtEIQDPGRALNLAGRAVG 553
Cdd:COG3071  247 AEKwLKKHPNDPDLLLALGRLCLRNQLWGKAREYLEAALALRPSaEAYAE--LARLLE-----QLGDPEEAAEHYRKALA 319


                 ...
gi 636808205 554 LAP 556
Cdd:COG3071  320 LAL 322
M48_Ste24p_like cd07328
M48 Ste24 endopeptidase-like, integral membrane metallopeptidase; This family contains ...
 226-304 8.61e-03

M48 Ste24 endopeptidase-like, integral membrane metallopeptidase; This family contains peptidase M48-like proteins that are as yet uncharacterized, but probably function as intracellular, membrane-associated zinc metalloproteases; they all contain the HEXXH Zn-binding motif, which is critical for Ste24p activity. They likely remove the C-terminal three residues of farnesylated proteins proteolytically and are possibly associated with the endoplasmic reticulum and golgi.


Pssm-ID: 320687 [Multi-domain]  Cd Length: 160  Bit Score: 37.53  E-value: 8.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636808205 226 IEAVCHMAGLRYAD-ILIWDLFAGSMITAGVmgLVGKFRYILVTPALLGSLNDEELAAVILHEIGHVKHWHMLYYLVFFA 304
Cdd:cd07328   32 VDELAAALGAPPPDeVVLTADVNASVTELGL--LLGRRGLLTLGLPLLAALSPEELRAVLAHELGHFANGDTRLGAWILS 109
PRK01345 PRK01345
heat shock protein HtpX; Provisional
 267-293 9.44e-03

heat shock protein HtpX; Provisional


Pssm-ID: 234944 [Multi-domain]  Cd Length: 317  Bit Score: 38.46  E-value: 9.44e-03
                         10        20
                 ....*....|....*....|....*..
gi 636808205 267 VTPALLGSLNDEELAAVILHEIGHVKH 293
Cdd:PRK01345 111 ATTGLLQRLSPEEVAGVMAHELAHVKN 137
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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