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Conserved domains on  [gi|1671569799|gb|TMJ01823|]
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M50 family metallopeptidase [Terrabacteria group bacterium ANGP1]

Protein Classification

M50 family metallopeptidase( domain architecture ID 10145855)

M50 family metallopeptidase that cleaves transmembrane domains of substrate proteins, regulating intramembrane proteolysis (RIP) of diverse signal transduction mechanisms; belongs to the site-2 protease (S2P) class of zinc metalloproteases

EC:  3.4.24.-
Gene Ontology:  GO:0016020|GO:0008233|GO:0004222|GO:0046872|GO:0006508
MEROPS:  M50
PubMed:  16322567|16731018|24099006|27889944|24099002

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
S2P-M50 cd05709
Site-2 protease (S2P) class of zinc metalloproteases (MEROPS family M50) cleaves transmembrane ...
 26-214 1.11e-24

Site-2 protease (S2P) class of zinc metalloproteases (MEROPS family M50) cleaves transmembrane domains of substrate proteins, regulating intramembrane proteolysis (RIP) of diverse signal transduction mechanisms. Members of this family use proteolytic activity within the membrane to transfer information across membranes to integrate gene expression with physiologic stresses occurring in another cellular compartment. The domain core structure appears to contain at least three transmembrane helices with a catalytic zinc atom coordinated by three conserved residues contained within the consensus sequence HExxH, together with a conserved aspartate residue. The S2P/M50 family of RIP proteases is widely distributed; in eukaryotic cells, they regulate such processes as sterol and lipid metabolism, and endoplasmic reticulum (ER) stress responses. In sterol-depleted mammalian cells, a two-step proteolytic process releases the N-terminal domains of sterol regulatory element-binding proteins (SREBPs) from membranes of the ER. These domains translocate into the nucleus, where they activate genes of cholesterol and fatty acid biosynthesis. It is the second proteolytic step that is carried out by the SREBP Site-2 protease (S2P) which is present in this CD superfamily. Prokaryotic S2P/M50 homologs have been shown to regulate stress responses, sporulation, cell division, and cell differentiation. In Escherichia coli, the S2P homolog RseP is involved in the sigmaE pathway of extracytoplasmic stress responses, and in Bacillus subtilis, the S2P homolog SpoIVFB is involved in the pro-sigmaK pathway of spore formation. Some of the subfamilies within this hierarchy contain one or two PDZ domain insertions, with putative regulatory roles, such as the inhibition of substrate cleavage as seen by the RseP PDZ domain.


:

Pssm-ID: 100078 [Multi-domain]  Cd Length: 180  Bit Score: 96.15  E-value: 1.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671569799  26 LTALGVIGATVALHEGAHALVTARAGGKVKEIGIGFgppLFRLRVRHLPVVVRMLPLGGYAAVDPE-----QIPPRRRIP 100
Cdd:cd05709     1 LAFILALLISVTVHELGHALVARRLGVKVARFSGGF---TLNPLKHGDPYGIILIPLGGYAKPVGEnprafKKPRWQRLL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671569799 101 MLLAGPLANIAAGLLLMLAFrrhpveiptdgrrvgLTGFAGTLAALVRAAARGPGSIARLAGSMNVGLGLANLLPVYPLD 180
Cdd:cd05709    78 VALAGPLANLLLALLLLLLL---------------LLLGGLPPAPVGQAASSGLANLLAFLALINLNLAVFNLLPIPPLD 142

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1671569799 181 GGHVVMSILEERGVPRETRIRFARWTAALFIMLA 214
Cdd:cd05709   143 GGRILRALLEAIRGRVEERLEAYGFAILLGLLLL 176
 
Name Accession Description Interval E-value
S2P-M50 cd05709
Site-2 protease (S2P) class of zinc metalloproteases (MEROPS family M50) cleaves transmembrane ...
 26-214 1.11e-24

Site-2 protease (S2P) class of zinc metalloproteases (MEROPS family M50) cleaves transmembrane domains of substrate proteins, regulating intramembrane proteolysis (RIP) of diverse signal transduction mechanisms. Members of this family use proteolytic activity within the membrane to transfer information across membranes to integrate gene expression with physiologic stresses occurring in another cellular compartment. The domain core structure appears to contain at least three transmembrane helices with a catalytic zinc atom coordinated by three conserved residues contained within the consensus sequence HExxH, together with a conserved aspartate residue. The S2P/M50 family of RIP proteases is widely distributed; in eukaryotic cells, they regulate such processes as sterol and lipid metabolism, and endoplasmic reticulum (ER) stress responses. In sterol-depleted mammalian cells, a two-step proteolytic process releases the N-terminal domains of sterol regulatory element-binding proteins (SREBPs) from membranes of the ER. These domains translocate into the nucleus, where they activate genes of cholesterol and fatty acid biosynthesis. It is the second proteolytic step that is carried out by the SREBP Site-2 protease (S2P) which is present in this CD superfamily. Prokaryotic S2P/M50 homologs have been shown to regulate stress responses, sporulation, cell division, and cell differentiation. In Escherichia coli, the S2P homolog RseP is involved in the sigmaE pathway of extracytoplasmic stress responses, and in Bacillus subtilis, the S2P homolog SpoIVFB is involved in the pro-sigmaK pathway of spore formation. Some of the subfamilies within this hierarchy contain one or two PDZ domain insertions, with putative regulatory roles, such as the inhibition of substrate cleavage as seen by the RseP PDZ domain.


Pssm-ID: 100078 [Multi-domain]  Cd Length: 180  Bit Score: 96.15  E-value: 1.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671569799  26 LTALGVIGATVALHEGAHALVTARAGGKVKEIGIGFgppLFRLRVRHLPVVVRMLPLGGYAAVDPE-----QIPPRRRIP 100
Cdd:cd05709     1 LAFILALLISVTVHELGHALVARRLGVKVARFSGGF---TLNPLKHGDPYGIILIPLGGYAKPVGEnprafKKPRWQRLL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671569799 101 MLLAGPLANIAAGLLLMLAFrrhpveiptdgrrvgLTGFAGTLAALVRAAARGPGSIARLAGSMNVGLGLANLLPVYPLD 180
Cdd:cd05709    78 VALAGPLANLLLALLLLLLL---------------LLLGGLPPAPVGQAASSGLANLLAFLALINLNLAVFNLLPIPPLD 142

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1671569799 181 GGHVVMSILEERGVPRETRIRFARWTAALFIMLA 214
Cdd:cd05709   143 GGRILRALLEAIRGRVEERLEAYGFAILLGLLLL 176
SpoIVFB COG1994
Zn-dependent protease (includes sporulation protein SpoIVFB) [Posttranslational modification, ...
 21-214 6.36e-17

Zn-dependent protease (includes sporulation protein SpoIVFB) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441597  Cd Length: 175  Bit Score: 75.63  E-value: 6.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671569799  21 HWRHLLTALGVIGAtVALHEGAHALVTARAGGKVKEIgigfgpplfrlrvrhlpvvvRMLPL-GGYAAVDPEQIPPRRRI 99
Cdd:COG1994     8 HPSILIFALALFLS-VLLHELAHALVARRLGDPTAKI--------------------TLNPLkGGWAKINRNFRNPRDEA 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671569799 100 PMLLAGPLANIAAGLLLMLAFRrhpveiptdgrrvgltgfagtlaALVRAAARGPGSIARLAGSMNVGLGLANLLPVYPL 179
Cdd:COG1994    67 LVALAGPLANLLLALLFALLLR-----------------------LLPALGLGPLALLLGYLALINLVLAVFNLLPIPPL 123

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1671569799 180 DGGHVVMSILEERGVPRETRI-RFARWTAALFIMLA 214
Cdd:COG1994   124 DGGRILRALLPRRTARRATRLePYGFLILLLLIFLG 159
Peptidase_M50 pfam02163
Peptidase family M50;
27-214 5.37e-12

Peptidase family M50;


Pssm-ID: 426630 [Multi-domain]  Cd Length: 291  Bit Score: 64.05  E-value: 5.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671569799  27 TALGVIGATVALHEGAHALVTARAGGKVKEIGIGFgpplfrlrvrhlpVVVRMLPLGGYAAVDPE--QIPPRRRIPMLLA 104
Cdd:pfam02163   1 AFILALGILVVVHELGHFLVARRFGVKVERFSIGF-------------YRIALIPLGGYVKMADEfkSKSPWQRLAIALA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671569799 105 GPLANIAAGLLLMLAF-------RRHPVEIPT------------------------------------------------ 129
Cdd:pfam02163  68 GPLANFILAIILFAVLlflsgvpPPAPPVIGGvapgspaakaglkpgdvilsingkkitswqdlvealakspgkpitltv 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671569799 130 -----------------DGRRVG----------------------------LTGFAGTLAALVRAAARGPGSIAR----- 159
Cdd:pfam02163 148 erggqtltvtitpksseESKFIGigpvyvkygllealgfalektvnlvtltLKALGKLITGVSLKNLGGPIGIAGqaaea 227

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1671569799 160 -------LAGSMNVGLGLANLLPVYPLDGGHVVMSILEE-RGVPRETRIRFARWTAALFIMLA 214
Cdd:pfam02163 228 gliaflyFLALINLNLGIFNLLPVPPLDGGHILRALLEAiRGKPLSERAEEIALRVGLALLLL 290
TIGR00054 TIGR00054
RIP metalloprotease RseP; Members of this nearly universal bacterial protein family are ...
 26-109 7.75e-12

RIP metalloprotease RseP; Members of this nearly universal bacterial protein family are regulated intramembrane proteolysis (RIP) proteases. Older and synonymous gene symbols include yaeL in E. coli, mmpA in Caulobacter crescentus, etc. This family includes a region that hits the PDZ domain, found in a number of proteins targeted to the membrane by binding to a peptide ligand. The N-terminal region of this family contains a perfectly conserved motif HEXGH as found in a number of metalloproteinases, where the Glu is the active site and the His residues coordinate the metal cation. Membership in this family is determined by a match to the full length of the seed alignment; the model also detects fragments as well matches a number of members of the PEPTIDASE FAMILY S2C. The region of match appears not to overlap the active site domain. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 272878 [Multi-domain]  Cd Length: 419  Bit Score: 64.07  E-value: 7.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671569799  26 LTALGVIGATVALHEGAHALVTARAGGKVKEIGIGFGPPLFRLRVRHLPVVVRMLPLGGY---AAVDPE----------- 91
Cdd:TIGR00054   6 LASILALAVLIFVHELGHFLAARLCGIKVERFSIGFGPKILKFKKNGTEYAISLIPLGGYvkmKGLDKEmevkppetdgd 85

                          90       100
                  ....*....|....*....|.
gi 1671569799  92 ---QIPPRRRIPMLLAGPLAN 109
Cdd:TIGR00054  86 lfnNKSVFQKAIIIFAGPLAN 106
PRK10779 PRK10779
sigma E protease regulator RseP;
26-109 2.91e-06

sigma E protease regulator RseP;


Pssm-ID: 182723 [Multi-domain]  Cd Length: 449  Bit Score: 47.37  E-value: 2.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671569799  26 LTALGVIgatVALHEGAHALVTARAGGKVKEIGIGFGPPLFRLRVRH-LPVVVRMLPLGGYAAVDPEQI----PPRR--- 97
Cdd:PRK10779   11 IVALGVL---ITVHEFGHFWVARRCGVRVERFSIGFGKALWRRTDRQgTEYVIALIPLGGYVKMLDERVepvaPELRhha 87

                          90       100
                  ....*....|....*....|
gi 1671569799  98 --------RIPMLLAGPLAN 109
Cdd:PRK10779   88 fnnktvgqRAAIIAAGPIAN 107
 
Name Accession Description Interval E-value
S2P-M50 cd05709
Site-2 protease (S2P) class of zinc metalloproteases (MEROPS family M50) cleaves transmembrane ...
 26-214 1.11e-24

Site-2 protease (S2P) class of zinc metalloproteases (MEROPS family M50) cleaves transmembrane domains of substrate proteins, regulating intramembrane proteolysis (RIP) of diverse signal transduction mechanisms. Members of this family use proteolytic activity within the membrane to transfer information across membranes to integrate gene expression with physiologic stresses occurring in another cellular compartment. The domain core structure appears to contain at least three transmembrane helices with a catalytic zinc atom coordinated by three conserved residues contained within the consensus sequence HExxH, together with a conserved aspartate residue. The S2P/M50 family of RIP proteases is widely distributed; in eukaryotic cells, they regulate such processes as sterol and lipid metabolism, and endoplasmic reticulum (ER) stress responses. In sterol-depleted mammalian cells, a two-step proteolytic process releases the N-terminal domains of sterol regulatory element-binding proteins (SREBPs) from membranes of the ER. These domains translocate into the nucleus, where they activate genes of cholesterol and fatty acid biosynthesis. It is the second proteolytic step that is carried out by the SREBP Site-2 protease (S2P) which is present in this CD superfamily. Prokaryotic S2P/M50 homologs have been shown to regulate stress responses, sporulation, cell division, and cell differentiation. In Escherichia coli, the S2P homolog RseP is involved in the sigmaE pathway of extracytoplasmic stress responses, and in Bacillus subtilis, the S2P homolog SpoIVFB is involved in the pro-sigmaK pathway of spore formation. Some of the subfamilies within this hierarchy contain one or two PDZ domain insertions, with putative regulatory roles, such as the inhibition of substrate cleavage as seen by the RseP PDZ domain.


Pssm-ID: 100078 [Multi-domain]  Cd Length: 180  Bit Score: 96.15  E-value: 1.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671569799  26 LTALGVIGATVALHEGAHALVTARAGGKVKEIGIGFgppLFRLRVRHLPVVVRMLPLGGYAAVDPE-----QIPPRRRIP 100
Cdd:cd05709     1 LAFILALLISVTVHELGHALVARRLGVKVARFSGGF---TLNPLKHGDPYGIILIPLGGYAKPVGEnprafKKPRWQRLL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671569799 101 MLLAGPLANIAAGLLLMLAFrrhpveiptdgrrvgLTGFAGTLAALVRAAARGPGSIARLAGSMNVGLGLANLLPVYPLD 180
Cdd:cd05709    78 VALAGPLANLLLALLLLLLL---------------LLLGGLPPAPVGQAASSGLANLLAFLALINLNLAVFNLLPIPPLD 142

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1671569799 181 GGHVVMSILEERGVPRETRIRFARWTAALFIMLA 214
Cdd:cd05709   143 GGRILRALLEAIRGRVEERLEAYGFAILLGLLLL 176
S2P-M50_PDZ_RseP-like cd06163
RseP-like Site-2 proteases (S2P), zinc metalloproteases (MEROPS family M50A), cleave ...
 25-224 3.61e-24

RseP-like Site-2 proteases (S2P), zinc metalloproteases (MEROPS family M50A), cleave transmembrane domains of substrate proteins, regulating intramembrane proteolysis (RIP) of diverse signal transduction mechanisms. In Escherichia coli, the S2P homolog RseP is involved in the sigmaE pathway of extracytoplasmic stress responses. Also included in this group are such homologs as Bacillus subtilis YluC, Mycobacterium tuberculosis Rv2869c S2P, and Bordetella bronchiseptica HurP. Rv2869c S2P appears to have a role in the regulation of prokaryotic lipid biosynthesis and membrane composition and YluC of Bacillus has a role in transducing membrane stress. This group includes bacterial and eukaryotic S2P/M50s homologs with either one or two PDZ domains present. PDZ domains are believed to have a regulatory role. The RseP PDZ domain is required for the inhibitory reaction that prevents cleavage of its substrate, RseA.


Pssm-ID: 100084 [Multi-domain]  Cd Length: 182  Bit Score: 94.79  E-value: 3.61e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671569799  25 LLTALGVIGATVALHEGAHALVTARAGGKVKEIGIGFGPPLFRLRVRHLPVVVRMLPLGGY---------AAVDPEQ--- 92
Cdd:cd06163     1 ILAFILVLGILIFVHELGHFLVAKLFGVKVEEFSIGFGPKLFSFKKGETEYSISAIPLGGYvkmlgedpeEEADPEDdpr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671569799  93 ----IPPRRRIPMLLAGPLANIAAGLLLMLAfrrhpveiptdgrrvgltgfagtlaalvraaargpgsIARLAGSMNVGL 168
Cdd:cd06163    81 sfnsKPVWQRILIVFAGPLANFLLAIVLFAV-------------------------------------LLSFLALLSINL 123

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1671569799 169 GLANLLPVYPLDGGHVVMSILE---ERGVPRETRIRFARWTAALFIMLARAAMLGDLRR 224
Cdd:cd06163   124 GILNLLPIPALDGGHLLFLLIEairGRPLSEKVEEIIQTIGFALLLGLMLFVTFNDIVR 182
SpoIVFB COG1994
Zn-dependent protease (includes sporulation protein SpoIVFB) [Posttranslational modification, ...
 21-214 6.36e-17

Zn-dependent protease (includes sporulation protein SpoIVFB) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441597  Cd Length: 175  Bit Score: 75.63  E-value: 6.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671569799  21 HWRHLLTALGVIGAtVALHEGAHALVTARAGGKVKEIgigfgpplfrlrvrhlpvvvRMLPL-GGYAAVDPEQIPPRRRI 99
Cdd:COG1994     8 HPSILIFALALFLS-VLLHELAHALVARRLGDPTAKI--------------------TLNPLkGGWAKINRNFRNPRDEA 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671569799 100 PMLLAGPLANIAAGLLLMLAFRrhpveiptdgrrvgltgfagtlaALVRAAARGPGSIARLAGSMNVGLGLANLLPVYPL 179
Cdd:COG1994    67 LVALAGPLANLLLALLFALLLR-----------------------LLPALGLGPLALLLGYLALINLVLAVFNLLPIPPL 123

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1671569799 180 DGGHVVMSILEERGVPRETRI-RFARWTAALFIMLA 214
Cdd:COG1994   124 DGGRILRALLPRRTARRATRLePYGFLILLLLIFLG 159
S2P-M50_SpoIVFB cd06161
SpoIVFB Site-2 protease (S2P), a zinc metalloprotease (MEROPS family M50B), regulates ...
 15-211 5.95e-14

SpoIVFB Site-2 protease (S2P), a zinc metalloprotease (MEROPS family M50B), regulates intramembrane proteolysis (RIP), and is involved in the pro-sigmaK pathway of bacterial spore formation. SpoIVFB (sporulation protein, stage IV cell wall formation, F locus, promoter-distal B) is one of 4 proteins involved in endospore formation; the others are SpoIVFA (sporulation protein, stage IV cell wall formation, F locus, promoter-proximal A), BofA (bypass-of-forespore A), and SpoIVB (sporulation protein, stage IV cell wall formation, B locus). SpoIVFB is negatively regulated by SpoIVFA and BofA and activated by SpoIVB. It is thought that SpoIVFB, SpoIVFA, and BofA are located in the mother-cell membrane that surrounds the forespore and that SpoIVB is secreted from the forespore into the space between the two where it activates SpoIVFB.


Pssm-ID: 100082 [Multi-domain]  Cd Length: 208  Bit Score: 68.34  E-value: 5.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671569799  15 TNHGPRHWRHLLTALGVIGATVALHEGAHALVTARAGGKVKEIGIgfgpplfrlrvrhlpvvvrmLPLGGYAAVDPEQIP 94
Cdd:cd06161    20 PGVGPVAWLLGLLEALLLFLSVLLHELGHALVARRYGIRVRSITL--------------------LPFGGVAELEEEPET 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671569799  95 PRRRIPMLLAGPLANIAAGLLLMLAFRRHPVEIPtdgrrvgltgfagtlaalvraaargPGSIARLAGSMNVGLGLANLL 174
Cdd:cd06161    80 PKEEFVIALAGPLVSLLLAGLFYLLYLLLPGGGP-------------------------LSSLLEFLAQVNLILGLFNLL 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1671569799 175 PVYPLDGGHVVMSILEERGVPRE-TRI--RFARWTAALFI 211
Cdd:cd06161   135 PALPLDGGRVLRALLWRRTGYRRaTRIaaRIGQLFAILLV 174
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 25-120 7.23e-13

Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, protein turnover, chaperones, Transcription];


Pssm-ID: 440513 [Multi-domain]  Cd Length: 349  Bit Score: 67.03  E-value: 7.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671569799  25 LLTALGVIGATVALHEGAHaLVTARAGG-KVKEIGIGFGPPLFRLRVRHLPVVVRMLPLGGY---------AAVDPEQ-- 92
Cdd:COG0750     7 ILAFILVLGVLVFVHELGH-FLVARLFGvKVEEFSIGFGPKLFSKKRGETEYGIRAIPLGGYvkmagmdpeSEVAPEDdp 85

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1671569799  93 -----IPPRRRIPMLLAGPLANIAAGLLLMLAF 120
Cdd:COG0750    86 rafnsKPVWQRLIIVLAGPLANFLLAIVLFAVL 118
S2P-M50_SpoIVFB_CBS cd06164
SpoIVFB Site-2 protease (S2P), a zinc metalloprotease (MEROPS family M50B), regulates ...
 25-222 2.96e-12

SpoIVFB Site-2 protease (S2P), a zinc metalloprotease (MEROPS family M50B), regulates intramembrane proteolysis (RIP), and is involved in the pro-sigmaK pathway of bacterial spore formation. In this subgroup, SpoIVFB (sporulation protein, stage IV cell wall formation, F locus, promoter-distal B) contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain. SpoIVFB is one of 4 proteins involved in endospore formation; the others are SpoIVFA (sporulation protein, stage IV cell wall formation, F locus, promoter-proximal A), BofA (bypass-of-forespore A), and SpoIVB (sporulation protein, stage IV cell wall formation, B locus). SpoIVFB is negatively regulated by SpoIVFA and BofA and activated by SpoIVB. It is thought that SpoIVFB, SpoIVFA, and BofA are located in the mother-cell membrane that surrounds the forespore and that SpoIVB is secreted from the forespore into the space between the two where it activates SpoIVFB. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown.


Pssm-ID: 100085  Cd Length: 227  Bit Score: 63.71  E-value: 2.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671569799  25 LLTALGViGATVALHEGAHALVTARAGGKVKEIgigfgpplfrlrvrhlpvvvRMLPLGGYAAVDPEQIPPRRRIPMLLA 104
Cdd:cd06164    46 LAAALLL-FASVLLHELGHSLVARRYGIPVRSI--------------------TLFLFGGVARLEREPETPGQEFVIAIA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671569799 105 GPLANIAAGLLLMLAfrrhpveiptdgrrvgltgfagtLAALVRAAARGPGSIARLAGSMNVGLGLANLLPVYPLDGGHV 184
Cdd:cd06164   105 GPLVSLVLALLFLLL-----------------------SLALPGSGAGPLGVLLGYLALINLLLAVFNLLPAFPLDGGRV 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1671569799 185 VMSILEERGVPRETRIRFA----RWTAALFIMLARAAMLGDL 222
Cdd:cd06164   162 LRALLWRRTGDYLKATRIAawvgRGFAVLLIILGLLSLFLNL 203
Peptidase_M50 pfam02163
Peptidase family M50;
27-214 5.37e-12

Peptidase family M50;


Pssm-ID: 426630 [Multi-domain]  Cd Length: 291  Bit Score: 64.05  E-value: 5.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671569799  27 TALGVIGATVALHEGAHALVTARAGGKVKEIGIGFgpplfrlrvrhlpVVVRMLPLGGYAAVDPE--QIPPRRRIPMLLA 104
Cdd:pfam02163   1 AFILALGILVVVHELGHFLVARRFGVKVERFSIGF-------------YRIALIPLGGYVKMADEfkSKSPWQRLAIALA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671569799 105 GPLANIAAGLLLMLAF-------RRHPVEIPT------------------------------------------------ 129
Cdd:pfam02163  68 GPLANFILAIILFAVLlflsgvpPPAPPVIGGvapgspaakaglkpgdvilsingkkitswqdlvealakspgkpitltv 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671569799 130 -----------------DGRRVG----------------------------LTGFAGTLAALVRAAARGPGSIAR----- 159
Cdd:pfam02163 148 erggqtltvtitpksseESKFIGigpvyvkygllealgfalektvnlvtltLKALGKLITGVSLKNLGGPIGIAGqaaea 227

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1671569799 160 -------LAGSMNVGLGLANLLPVYPLDGGHVVMSILEE-RGVPRETRIRFARWTAALFIMLA 214
Cdd:pfam02163 228 gliaflyFLALINLNLGIFNLLPVPPLDGGHILRALLEAiRGKPLSERAEEIALRVGLALLLL 290
TIGR00054 TIGR00054
RIP metalloprotease RseP; Members of this nearly universal bacterial protein family are ...
 26-109 7.75e-12

RIP metalloprotease RseP; Members of this nearly universal bacterial protein family are regulated intramembrane proteolysis (RIP) proteases. Older and synonymous gene symbols include yaeL in E. coli, mmpA in Caulobacter crescentus, etc. This family includes a region that hits the PDZ domain, found in a number of proteins targeted to the membrane by binding to a peptide ligand. The N-terminal region of this family contains a perfectly conserved motif HEXGH as found in a number of metalloproteinases, where the Glu is the active site and the His residues coordinate the metal cation. Membership in this family is determined by a match to the full length of the seed alignment; the model also detects fragments as well matches a number of members of the PEPTIDASE FAMILY S2C. The region of match appears not to overlap the active site domain. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 272878 [Multi-domain]  Cd Length: 419  Bit Score: 64.07  E-value: 7.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671569799  26 LTALGVIGATVALHEGAHALVTARAGGKVKEIGIGFGPPLFRLRVRHLPVVVRMLPLGGY---AAVDPE----------- 91
Cdd:TIGR00054   6 LASILALAVLIFVHELGHFLAARLCGIKVERFSIGFGPKILKFKKNGTEYAISLIPLGGYvkmKGLDKEmevkppetdgd 85

                          90       100
                  ....*....|....*....|.
gi 1671569799  92 ---QIPPRRRIPMLLAGPLAN 109
Cdd:TIGR00054  86 lfnNKSVFQKAIIIFAGPLAN 106
S2P-M50_PDZ_Arch cd06159
Uncharacterized Archaeal homologs of Site-2 protease (S2P), zinc metalloproteases (MEROPS ...
 28-213 1.63e-09

Uncharacterized Archaeal homologs of Site-2 protease (S2P), zinc metalloproteases (MEROPS family M50) which cleave transmembrane domains of substrate proteins, regulating intramembrane proteolysis (RIP) of diverse signal transduction mechanisms. Members of the S2P/M50 family of RIP proteases use proteolytic activity within the membrane to transfer information across membranes to integrate gene expression with physiologic stresses occurring in another cellular compartment. In eukaryotic cells they regulate such processes as sterol and lipid metabolism, and endoplasmic reticulum stress responses. In prokaryotes they regulate such processes as sporulation, cell division, stress response, and cell differentiation. This group appears to be limited to Archaeal S2P/M50s homologs with additional putative N-terminal transmembrane spanning regions, relative to the core protein, and either one or two PDZ domains present.


Pssm-ID: 100080 [Multi-domain]  Cd Length: 263  Bit Score: 56.54  E-value: 1.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671569799  28 ALGVigaTVALHEGAHALVTARAGGKVKEIGIgfgppLFRLrvrhlpvvvrmLPLGGYAAVDPEQI---PPRRRIPMLLA 104
Cdd:cd06159   116 ALVV---GVVVHELSHGILARVEGIKVKSGGL-----LLLI-----------IPPGAFVEPDEEELnkaDRRIRLRIFAA 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671569799 105 GPLANIAAGLLLMLAFrrhpveiptdgrrvgltgfagtlaalvraaargpgsIARLAGSMNVGLGLANLLPVYPLDGGHV 184
Cdd:cd06159   177 GVTANFVVALIAFALF------------------------------------FLYWIFWINFLLGLFNCLPAIPLDGGHV 220

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1671569799 185 VMSILEERG--VPRETRIRFARWTAALFIML 213
Cdd:cd06159   221 FRDLLEALLrrFPSEKAERVVNAITYYLSSL 251
S2P-M50_like_1 cd06158
Uncharacterized homologs of Site-2 protease (S2P), zinc metalloproteases (MEROPS family M50) ...
 25-214 1.05e-07

Uncharacterized homologs of Site-2 protease (S2P), zinc metalloproteases (MEROPS family M50) which cleave transmembrane domains of substrate proteins, regulating intramembrane proteolysis (RIP) of diverse signal transduction mechanisms. Members of the S2P/M50 family of RIP proteases use proteolytic activity within the membrane to transfer information across membranes to integrate gene expression with physiologic stresses occurring in another cellular compartment. In eukaryotic cells they regulate such processes as sterol and lipid metabolism, and endoplasmic reticulum stress responses. In prokaryotes they regulate such processes as sporulation, cell division, stress response, and cell differentiation. This group includes bacterial, eukaryotic, and Archaeal S2P/M50s homologs with a minimal core protein and no PDZ domains.


Pssm-ID: 100079  Cd Length: 181  Bit Score: 50.24  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671569799  25 LLTALGVIGATVALHEGAHALVTARAGGK-VKEIGIGFGPPLfrlrvRH--------LPVVvrMLPLGGYA---AVDPEQ 92
Cdd:cd06158     1 ILIVIIAVLLAITLHEFAHAYVAYRLGDPtARRAGRLTLNPL-----AHidpigtiiLPLL--LPFLFGWAkpvPVNPRN 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671569799  93 IPPRRRIPML--LAGPLANIAAGLLLMLAFRrhpveiptdgrrvgLTGFAGTLAALVRAAargpgsIARLAGSMNVGLGL 170
Cdd:cd06158    74 FKNPRRGMLLvsLAGPLSNLLLALLFALLLR--------------LLPAFGGVVASFLFL------MLAYGVLINLVLAV 133

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1671569799 171 ANLLPVYPLDGGHVVMSILEERGvpRETRIRFARWTAALFIMLA 214
Cdd:cd06158   134 FNLLPIPPLDGSKILAALLPRRL--AEAYARLEPYGFLILLALL 175
PRK10779 PRK10779
sigma E protease regulator RseP;
26-109 2.91e-06

sigma E protease regulator RseP;


Pssm-ID: 182723 [Multi-domain]  Cd Length: 449  Bit Score: 47.37  E-value: 2.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671569799  26 LTALGVIgatVALHEGAHALVTARAGGKVKEIGIGFGPPLFRLRVRH-LPVVVRMLPLGGYAAVDPEQI----PPRR--- 97
Cdd:PRK10779   11 IVALGVL---ITVHEFGHFWVARRCGVRVERFSIGFGKALWRRTDRQgTEYVIALIPLGGYVKMLDERVepvaPELRhha 87

                          90       100
                  ....*....|....*....|
gi 1671569799  98 --------RIPMLLAGPLAN 109
Cdd:PRK10779   88 fnnktvgqRAAIIAAGPIAN 107
TIGR00054 TIGR00054
RIP metalloprotease RseP; Members of this nearly universal bacterial protein family are ...
 153-225 5.65e-04

RIP metalloprotease RseP; Members of this nearly universal bacterial protein family are regulated intramembrane proteolysis (RIP) proteases. Older and synonymous gene symbols include yaeL in E. coli, mmpA in Caulobacter crescentus, etc. This family includes a region that hits the PDZ domain, found in a number of proteins targeted to the membrane by binding to a peptide ligand. The N-terminal region of this family contains a perfectly conserved motif HEXGH as found in a number of metalloproteinases, where the Glu is the active site and the His residues coordinate the metal cation. Membership in this family is determined by a match to the full length of the seed alignment; the model also detects fragments as well matches a number of members of the PEPTIDASE FAMILY S2C. The region of match appears not to overlap the active site domain. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 272878 [Multi-domain]  Cd Length: 419  Bit Score: 40.57  E-value: 5.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671569799 153 GPGSIARLAGS---------------MNVGLGLANLLPVYPLDGGHVVMSILEE-RGVPRETRIRFARWT--AALFIMLA 214
Cdd:TIGR00054 329 GPVGIVKGAGSsansgivyllqfgafLSINLGIMNLLPIPALDGGQLLFLFIEAiRGKPLPEKVQAFVYRigVAFLLFLM 408

                          90
                  ....*....|.
gi 1671569799 215 RAAMLGDLRRL 225
Cdd:TIGR00054 409 GLGLFNDLLRL 419
 
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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