NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1201930635|ref|WP_087614203|]
View 

MULTISPECIES: ubiquitin-like domain-containing protein [Bacillus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
YabE COG3583
Uncharacterized conserved protein YabE, contains G5 and tandem DUF348 domains [Function ...
 119-428 1.22e-72

Uncharacterized conserved protein YabE, contains G5 and tandem DUF348 domains [Function unknown];


:

Pssm-ID: 442802 [Multi-domain]  Cd Length: 335  Bit Score: 231.68  E-value: 1.22e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201930635 119 VVYEAAKPVKLTINGEEKTLWSTAKTVGALLDEQDVDVKEQDQIDPAIDTDISK----EMKINIEPAFQVTVNDAGKQKK 194
Cdd:COG3583    26 AYAAAKKTVTLDVDGEERTVTTFAGTVGEVLEEAGITVGEHDVVSPALDTPLTDgdtgELTITVKRAKPVTVVVDGKTRT 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201930635 195 IWTTSTTVADFLKQQKMNIKDEDKIKPALDAKLTKGkADITITRIEKVTDVVEEKIAFDVKKQEDASLEKGKEKVVQKGK 274
Cdd:COG3583   106 VTTTATTVGEALAEAGITLGEDDRVSPALDAPLTDG-MTITVTRVTTKTVTEEEPIPFETVRKEDPSLPKGETKVVQEGV 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201930635 275 EGKLKKHFEVVKENGKEVSRELVKEETAEQSKDKVIAVGTKQsSPKFETVSASGDSKTVVSRSNESTGKVMTVSSTAYTA 354
Cdd:COG3583   185 PGVKEVTYRVTYENGKEVSREVVSEKVTKEPVDEVVAVGTKP-RPAPAPVPAGSGSGGGGSSTGSGGYGGLAASSATTAA 263

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1201930635 355 SCSGCSGHTATGVNlkNNPNAKVIAVDPNVIPLGSKVHVEGYGYAIAADTGSAIKGNKIDVFFPEKSSAYRWGN 428
Cdd:COG3583   264 SGGGTGAPGGGGAA--RPTAGAVAGVVVVGGGGGGGPGGGGGGGAAAGGGGGGGGGGAIDGAEGGSSAAAGGGR 335
DUF348 pfam03990
G5-linked-Ubiquitin-like domain; This domain normally occurs as tandem repeats; however it is ...
 70-108 5.52e-09

G5-linked-Ubiquitin-like domain; This domain normally occurs as tandem repeats; however it is found as a single copy in the S. cerevisiae DNA-binding nuclear protein YCR593. This protein is involved in sporulation part of the SET3C complex, which is required to repress early/middle sporulation genes during meiosis. The bacterial proteins are likely to be involved in a cell wall function as they are found in conjunction with the pfam07501 domain, which is involved in various cell surface processes. This domain is also present in the resuscitation-promoting factors RpfB from Mycobacterium tuberculosis and Rpf2 from Corynebacterium glutamicum. These are factors that stimulate resuscitation of dormant cells. This domain has a beta grasp fold. Structural description of this domain revealed a structural conservation between these domains and ubiquitin, hence it is termed UBL-G5.


:

Pssm-ID: 461121 [Multi-domain]  Cd Length: 41  Bit Score: 51.65  E-value: 5.52e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1201930635  70 VSVSINGKKKHIRTHANTVGDLLETLDIKTRDEDKITPA 108
Cdd:pfam03990   1 VTLTVDGKERTVTTTAGTVGDLLEEAGITLGEHDKVSPS 39
 
Name Accession Description Interval E-value
YabE COG3583
Uncharacterized conserved protein YabE, contains G5 and tandem DUF348 domains [Function ...
 119-428 1.22e-72

Uncharacterized conserved protein YabE, contains G5 and tandem DUF348 domains [Function unknown];


Pssm-ID: 442802 [Multi-domain]  Cd Length: 335  Bit Score: 231.68  E-value: 1.22e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201930635 119 VVYEAAKPVKLTINGEEKTLWSTAKTVGALLDEQDVDVKEQDQIDPAIDTDISK----EMKINIEPAFQVTVNDAGKQKK 194
Cdd:COG3583    26 AYAAAKKTVTLDVDGEERTVTTFAGTVGEVLEEAGITVGEHDVVSPALDTPLTDgdtgELTITVKRAKPVTVVVDGKTRT 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201930635 195 IWTTSTTVADFLKQQKMNIKDEDKIKPALDAKLTKGkADITITRIEKVTDVVEEKIAFDVKKQEDASLEKGKEKVVQKGK 274
Cdd:COG3583   106 VTTTATTVGEALAEAGITLGEDDRVSPALDAPLTDG-MTITVTRVTTKTVTEEEPIPFETVRKEDPSLPKGETKVVQEGV 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201930635 275 EGKLKKHFEVVKENGKEVSRELVKEETAEQSKDKVIAVGTKQsSPKFETVSASGDSKTVVSRSNESTGKVMTVSSTAYTA 354
Cdd:COG3583   185 PGVKEVTYRVTYENGKEVSREVVSEKVTKEPVDEVVAVGTKP-RPAPAPVPAGSGSGGGGSSTGSGGYGGLAASSATTAA 263

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1201930635 355 SCSGCSGHTATGVNlkNNPNAKVIAVDPNVIPLGSKVHVEGYGYAIAADTGSAIKGNKIDVFFPEKSSAYRWGN 428
Cdd:COG3583   264 SGGGTGAPGGGGAA--RPTAGAVAGVVVVGGGGGGGPGGGGGGGAAAGGGGGGGGGGAIDGAEGGSSAAAGGGR 335
DPBB_YuiC-like cd22786
double-psi beta-barrel fold of YuiC subfamily proteins; The YuiC subfamily includes a group of ...
 342-437 6.35e-44

double-psi beta-barrel fold of YuiC subfamily proteins; The YuiC subfamily includes a group of conserved double-psi beta-barrel (DPBB) fold proteins, such as Bacillus subtilis protein YuiC, cell wall shaping protein YabE, cell wall-binding protein YocH, as well as Clostridium tetani phosphatase-associated protein PapQ. YuiC is a Firmicute stationary phase survival (Sps) protein that closely resembles the Barwin-like endoglucanase beta barrel of MltA. It is a double-psi beta-barrel (DPBB) fold that consists of two interlocked "psi-structure" motifs related by a pseudo-2-fold axis and may be involved in substrate binding and catalysis.


Pssm-ID: 439263 [Multi-domain]  Cd Length: 96  Bit Score: 148.52  E-value: 6.35e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201930635 342 GKVMTVSSTAYTASCS---GCSGHTATGVNLKNnpnAKVIAVDPNVIPLGSKVHVEGYGYAIAADTGSAIKGNKIDVFFP 418
Cdd:cd22786     1 SKKITVEATAYSPCSSsggGCYGITASGTPLKR---KGTIAVDPSVIPLGTKVYIPGYGYAVVADTGGAIKGNRIDLYFP 77

                          90
                  ....*....|....*....
gi 1201930635 419 EKSSAYRWGNKTVKIKILN 437
Cdd:cd22786    78 THEEAINWGRKTVEVYVLK 96
wall_bind_EntB NF040676
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ...
 60-436 1.81e-33

cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.


Pssm-ID: 468642 [Multi-domain]  Cd Length: 476  Bit Score: 131.06  E-value: 1.81e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201930635  60 YAAHELTKQSVSVSINgkKKHIRTHANTVGDLLETLdiktRDEDKITPAKQTK----------ITADMDVVYEAAK-PVK 128
Cdd:NF040676   75 FVSSEFTKDVYHVTAN--LLNVRTEANTESEILGRL----KKDDVIESTHQVKdgwlqfeykgKTAYANVSFLSSTaPTE 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201930635 129 LTINGEEKTLWSTAKTVGALLDEQDVDV-------KEQDQIDPAIDTDISKEMKINIEPAFQVTVNDAgKQKKIWTTSTT 201
Cdd:NF040676  149 KKADEKTKQVAKVQKSVKAKEEAKTQKVakakettKAQEIVKPKEEVKVQEVVKPKEEPKVQEIVKPK-EEVKVQEEVKP 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201930635 202 VADFLKQQKMNIKDEDKIKPALDAK-------LTKGKADITITRIEKVTDvvEEKIAFDVKKQEDASLE-----KGKEKV 269
Cdd:NF040676  228 KEEEKVQEIVKPKEEAKVQEEVKVKeeakvqeIAKAKEEAKAQEIAKAKE--EAKAQEIAKAKEEAKAQeiakaKEEEKA 305

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201930635 270 VQKGKEGKLKKHFEVVKENGKEVSRELVKEEtaEQSKDKVIAVGTKQSSPKFETVSASGDSKTVVSRSN-ESTGKVMTVS 348
Cdd:NF040676  306 QEIAKAKEEAKAREIAKAKEEEKAREIAKAK--EEAKAREIAKAKEEAKAREIAKAKEEERAKEASKNNiQSAKRELTVV 383

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201930635 349 STAYTASCS-----GCSGHTATGVNLKNNPNAKVIAVDPNVIPLGSKVHVEGYGYAIAADTGSAIKGNKIDVFFPEKSSA 423
Cdd:NF040676  384 ATAYTADPSengtyGGRVLTAMGHDLTANPNMRIIAVDPKVIPLGSKVWVEGYGEAIAGDTGSAIKGNRIDVLMGSKSKA 463

                         410
                  ....*....|...
gi 1201930635 424 YRWGNKTVKIKIL 436
Cdd:NF040676  464 MNWGRQTVKVKIL 476
3D pfam06725
3D domain; This short presumed domain contains three conserved aspartate residues, hence the ...
 376-437 7.56e-24

3D domain; This short presumed domain contains three conserved aspartate residues, hence the name 3D. It has been shown to be part of the catalytic double psi beta barrel domain of MltA.


Pssm-ID: 399598 [Multi-domain]  Cd Length: 72  Bit Score: 94.19  E-value: 7.56e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1201930635 376 KVIAVDPNVIPLGSKVHVEG-------YGYAIAADTGSAIKGNKIDVFFPEKSSAY-RWG--NKTVKIKILN 437
Cdd:pfam06725   1 RSIAVDPSVIPLGTPVYVEGplggkpvYRLAIAQDTGGAIKGNRIDLYFGTGDEAGnLAGlyRKTGRVYILL 72
DUF348 pfam03990
G5-linked-Ubiquitin-like domain; This domain normally occurs as tandem repeats; however it is ...
 70-108 5.52e-09

G5-linked-Ubiquitin-like domain; This domain normally occurs as tandem repeats; however it is found as a single copy in the S. cerevisiae DNA-binding nuclear protein YCR593. This protein is involved in sporulation part of the SET3C complex, which is required to repress early/middle sporulation genes during meiosis. The bacterial proteins are likely to be involved in a cell wall function as they are found in conjunction with the pfam07501 domain, which is involved in various cell surface processes. This domain is also present in the resuscitation-promoting factors RpfB from Mycobacterium tuberculosis and Rpf2 from Corynebacterium glutamicum. These are factors that stimulate resuscitation of dormant cells. This domain has a beta grasp fold. Structural description of this domain revealed a structural conservation between these domains and ubiquitin, hence it is termed UBL-G5.


Pssm-ID: 461121 [Multi-domain]  Cd Length: 41  Bit Score: 51.65  E-value: 5.52e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1201930635  70 VSVSINGKKKHIRTHANTVGDLLETLDIKTRDEDKITPA 108
Cdd:pfam03990   1 VTLTVDGKERTVTTTAGTVGDLLEEAGITLGEHDKVSPS 39
 
Name Accession Description Interval E-value
YabE COG3583
Uncharacterized conserved protein YabE, contains G5 and tandem DUF348 domains [Function ...
 119-428 1.22e-72

Uncharacterized conserved protein YabE, contains G5 and tandem DUF348 domains [Function unknown];


Pssm-ID: 442802 [Multi-domain]  Cd Length: 335  Bit Score: 231.68  E-value: 1.22e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201930635 119 VVYEAAKPVKLTINGEEKTLWSTAKTVGALLDEQDVDVKEQDQIDPAIDTDISK----EMKINIEPAFQVTVNDAGKQKK 194
Cdd:COG3583    26 AYAAAKKTVTLDVDGEERTVTTFAGTVGEVLEEAGITVGEHDVVSPALDTPLTDgdtgELTITVKRAKPVTVVVDGKTRT 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201930635 195 IWTTSTTVADFLKQQKMNIKDEDKIKPALDAKLTKGkADITITRIEKVTDVVEEKIAFDVKKQEDASLEKGKEKVVQKGK 274
Cdd:COG3583   106 VTTTATTVGEALAEAGITLGEDDRVSPALDAPLTDG-MTITVTRVTTKTVTEEEPIPFETVRKEDPSLPKGETKVVQEGV 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201930635 275 EGKLKKHFEVVKENGKEVSRELVKEETAEQSKDKVIAVGTKQsSPKFETVSASGDSKTVVSRSNESTGKVMTVSSTAYTA 354
Cdd:COG3583   185 PGVKEVTYRVTYENGKEVSREVVSEKVTKEPVDEVVAVGTKP-RPAPAPVPAGSGSGGGGSSTGSGGYGGLAASSATTAA 263

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1201930635 355 SCSGCSGHTATGVNlkNNPNAKVIAVDPNVIPLGSKVHVEGYGYAIAADTGSAIKGNKIDVFFPEKSSAYRWGN 428
Cdd:COG3583   264 SGGGTGAPGGGGAA--RPTAGAVAGVVVVGGGGGGGPGGGGGGGAAAGGGGGGGGGGAIDGAEGGSSAAAGGGR 335
COG3584 COG3584
3D (Asp-Asp-Asp) domain, usually in lytic transglycosylases [Function unknown]; 3D ...
 346-437 1.71e-44

3D (Asp-Asp-Asp) domain, usually in lytic transglycosylases [Function unknown]; 3D (Asp-Asp-Asp) domain, usually in lytic transglycosylases is part of the Pathway/BioSystem: 3D


Pssm-ID: 442803 [Multi-domain]  Cd Length: 92  Bit Score: 149.87  E-value: 1.71e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201930635 346 TVSSTAYTA---SCSGCSGHTATGVNLKNNpnaKVIAVDPNVIPLGSKVHVEGYGYAIAADTGSAIKGNKIDVFFPEKSS 422
Cdd:COG3584     1 TVTATAYTAgpeCTGKGGGITASGTRLRPG---GVIAVDPDVIPLGTKVYIEGYGYAVAEDTGGAIKGNRIDIYMPSVSE 77

                          90
                  ....*....|....*
gi 1201930635 423 AYRWGNKTVKIKILN 437
Cdd:COG3584    78 ALNWGRRTVTVYILE 92
DPBB_YuiC-like cd22786
double-psi beta-barrel fold of YuiC subfamily proteins; The YuiC subfamily includes a group of ...
 342-437 6.35e-44

double-psi beta-barrel fold of YuiC subfamily proteins; The YuiC subfamily includes a group of conserved double-psi beta-barrel (DPBB) fold proteins, such as Bacillus subtilis protein YuiC, cell wall shaping protein YabE, cell wall-binding protein YocH, as well as Clostridium tetani phosphatase-associated protein PapQ. YuiC is a Firmicute stationary phase survival (Sps) protein that closely resembles the Barwin-like endoglucanase beta barrel of MltA. It is a double-psi beta-barrel (DPBB) fold that consists of two interlocked "psi-structure" motifs related by a pseudo-2-fold axis and may be involved in substrate binding and catalysis.


Pssm-ID: 439263 [Multi-domain]  Cd Length: 96  Bit Score: 148.52  E-value: 6.35e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201930635 342 GKVMTVSSTAYTASCS---GCSGHTATGVNLKNnpnAKVIAVDPNVIPLGSKVHVEGYGYAIAADTGSAIKGNKIDVFFP 418
Cdd:cd22786     1 SKKITVEATAYSPCSSsggGCYGITASGTPLKR---KGTIAVDPSVIPLGTKVYIPGYGYAVVADTGGAIKGNRIDLYFP 77

                          90
                  ....*....|....*....
gi 1201930635 419 EKSSAYRWGNKTVKIKILN 437
Cdd:cd22786    78 THEEAINWGRKTVEVYVLK 96
3D_containing_proteins cd14667
Non-mltA associated 3D domain containing proteins, named for 3 conserved aspartate residues; ...
 347-436 1.10e-35

Non-mltA associated 3D domain containing proteins, named for 3 conserved aspartate residues; This family contains the 3D domain, named for its 3 conserved aspartates, including similar uncharacterized proteins. These proteins contain the critical active site aspartate of mltA-like lytic transglycosylases where the 3D domain forms a larger domain with the N-terminal region. This domain is also found in conjunction with numerous other domains such as the Escherichia coli MltA, a membrane-bound lytic transglycosylase comprised of 2 domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, corresponding to the 3D domain and Domain B is inserted within the linear sequence of domain A. MltA is distinct from other bacterial LTs, which are similar to each other. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. PG chains (also known as murein), the major components of the bacterial cell wall, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), and lytic transglycosylases cleave this beta-1-4 bond.


Pssm-ID: 270620 [Multi-domain]  Cd Length: 90  Bit Score: 126.87  E-value: 1.10e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201930635 347 VSSTAYTASCSGCSGHTATGVNLKNNPNAKVIAVDPNVIPLGSKVHVEGYGYAIAADTGSAIKGNKIDVFFPEKSSAYRW 426
Cdd:cd14667     1 FTATAYTSCEGCCGGGPGGTASGGLPVGGGTIAVDPSVIPLGTKVYIEGYGVYVVEDTGGAIKGNRIDIYMDSHAEALAF 80

                          90
                  ....*....|
gi 1201930635 427 GNKTVKIKIL 436
Cdd:cd14667    81 GRRYVEVYIL 90
wall_bind_EntB NF040676
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ...
 60-436 1.81e-33

cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.


Pssm-ID: 468642 [Multi-domain]  Cd Length: 476  Bit Score: 131.06  E-value: 1.81e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201930635  60 YAAHELTKQSVSVSINgkKKHIRTHANTVGDLLETLdiktRDEDKITPAKQTK----------ITADMDVVYEAAK-PVK 128
Cdd:NF040676   75 FVSSEFTKDVYHVTAN--LLNVRTEANTESEILGRL----KKDDVIESTHQVKdgwlqfeykgKTAYANVSFLSSTaPTE 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201930635 129 LTINGEEKTLWSTAKTVGALLDEQDVDV-------KEQDQIDPAIDTDISKEMKINIEPAFQVTVNDAgKQKKIWTTSTT 201
Cdd:NF040676  149 KKADEKTKQVAKVQKSVKAKEEAKTQKVakakettKAQEIVKPKEEVKVQEVVKPKEEPKVQEIVKPK-EEVKVQEEVKP 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201930635 202 VADFLKQQKMNIKDEDKIKPALDAK-------LTKGKADITITRIEKVTDvvEEKIAFDVKKQEDASLE-----KGKEKV 269
Cdd:NF040676  228 KEEEKVQEIVKPKEEAKVQEEVKVKeeakvqeIAKAKEEAKAQEIAKAKE--EAKAQEIAKAKEEAKAQeiakaKEEEKA 305

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201930635 270 VQKGKEGKLKKHFEVVKENGKEVSRELVKEEtaEQSKDKVIAVGTKQSSPKFETVSASGDSKTVVSRSN-ESTGKVMTVS 348
Cdd:NF040676  306 QEIAKAKEEAKAREIAKAKEEEKAREIAKAK--EEAKAREIAKAKEEAKAREIAKAKEEERAKEASKNNiQSAKRELTVV 383

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201930635 349 STAYTASCS-----GCSGHTATGVNLKNNPNAKVIAVDPNVIPLGSKVHVEGYGYAIAADTGSAIKGNKIDVFFPEKSSA 423
Cdd:NF040676  384 ATAYTADPSengtyGGRVLTAMGHDLTANPNMRIIAVDPKVIPLGSKVWVEGYGEAIAGDTGSAIKGNRIDVLMGSKSKA 463

                         410
                  ....*....|...
gi 1201930635 424 YRWGNKTVKIKIL 436
Cdd:NF040676  464 MNWGRQTVKVKIL 476
DPBB_MltA_YuiC-like cd22784
double-psi beta-barrel fold of membrane-bound lytic murein transglycosylase A (MltA) and ...
 350-435 1.95e-24

double-psi beta-barrel fold of membrane-bound lytic murein transglycosylase A (MltA) and YuiC-like proteins; This family includes two subfamilies of conserved double-psi beta-barrel (DPBB) domain proteins, such as membrane-bound lytic murein transglycosylase A (MltA)-like proteins and YuiC-like proteins. MltA, also called murein hydrolase A, is a murein-degrading enzyme that may play a role in the recycling of muropeptides during cell elongation and/or cell division. It degrades murein glycan strands and insoluble, high-molecular weight murein sacculi. Bacterial lytic transglycosylases (LTs) are classified into 4 families: family 1 includes slt70 MltC-MltF, family 2 includes MltA, family 3 includes MltB, and family 4 includes proteins of bacteriophage origin. MltA is distinct from other bacterial LTs, which are similar in structure and sequence with a lysozyme-like fold. MltA is a kidney bean-shaped monomeric protein comprised of two domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, which corresponds to a double-psi beta-barrel (DPBB) fold. Domain B also has a beta-barrel fold topology, but it is inserted within the linear sequence of domain A. YuiC is a Firmicute stationary phase survival (Sps) protein that closely resembles the Barwin-like endoglucanase beta barrel of MltA. It is a DPBB fold that consists of two interlocked "psi-structure" motifs related by a pseudo-2-fold axis and may be involved in substrate binding and catalysis.


Pssm-ID: 439261 [Multi-domain]  Cd Length: 92  Bit Score: 96.56  E-value: 1.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201930635 350 TAYTA---SCSGCSGHTATGVNLKNNpnaKVIAVDPNVIPLGSKVHVEG---YGYAIAADTGSAIKGNKIDVFFPEKSSA 423
Cdd:cd22784     4 TAYTPdeeQTDGGPGITASGVTLRGY---GTVAVDRDLIPLGTKVKIEGpgsGGEYVVLDRGGAIKGNRIDIYFPSEKEA 80

                          90
                  ....*....|..
gi 1201930635 424 YRWGNKTVKIKI 435
Cdd:cd22784    81 KKFGRQKVTVTV 92
3D pfam06725
3D domain; This short presumed domain contains three conserved aspartate residues, hence the ...
 376-437 7.56e-24

3D domain; This short presumed domain contains three conserved aspartate residues, hence the name 3D. It has been shown to be part of the catalytic double psi beta barrel domain of MltA.


Pssm-ID: 399598 [Multi-domain]  Cd Length: 72  Bit Score: 94.19  E-value: 7.56e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1201930635 376 KVIAVDPNVIPLGSKVHVEG-------YGYAIAADTGSAIKGNKIDVFFPEKSSAY-RWG--NKTVKIKILN 437
Cdd:pfam06725   1 RSIAVDPSVIPLGTPVYVEGplggkpvYRLAIAQDTGGAIKGNRIDLYFGTGDEAGnLAGlyRKTGRVYILL 72
G5 pfam07501
G5 domain; This domain is found in a wide range of extracellular proteins. It is found ...
 241-315 2.71e-21

G5 domain; This domain is found in a wide range of extracellular proteins. It is found tandemly repeated in up to 8 copies. It is found in the N-terminus of peptidases belonging to the M26 family which cleave human IgA. The domain is also found in proteins involved in metabolism of bacterial cell walls suggesting this domain may have an adhesive function.


Pssm-ID: 462185 [Multi-domain]  Cd Length: 75  Bit Score: 87.22  E-value: 2.71e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1201930635 241 KVTDVVEEKIAFDVKKQEDASLEKGKEKVVQKGKEGKLKKHFEVVKENGKEVSRELVKEETAEQSKDKVIAVGTK 315
Cdd:pfam07501   1 EKTVTEEEEIPFETVTKEDPSLPKGEEKVVQEGKPGEKEVTYKVTYVNGKEVSREVVSEEVTKEPVDEVVAVGTK 75
3D_domain cd14486
3D domain, named for 3 conserved aspartate residues, is found in mltA-like lytic ...
 347-436 6.23e-20

3D domain, named for 3 conserved aspartate residues, is found in mltA-like lytic transglycosylases and numerous other contexts; This family contains the 3D domain, named for its 3 conserved aspartates. It is found in conjunction with numerous other domains such as MltA (membrane-bound lytic murein transglycosylase A). These aspartates are critical active site residues of mltA-like lytic transglycosylases. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. MltA has 2 domains, separated by a large groove, where the peptidoglycan strand binds. The C-terminus has a double-psi beta barrel fold within the 3D domain, which forms the larger A domain along with the N-terminal region of Mlts, but is also found in various other domain architectures. Peptigoglycan (also known as murein) chains, the primary structural component of bacterial cells walls, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc); lytic transglycosylases (LTs) cleave this beta-1-4 bond. Typically, LTs are exolytic, releasing Metabolite 1 (GlcNAc-anhMurNAc-L-Ala-D-Glu-m-Dap-D-Ala-D-Ala) from the ends of the PG strands. In contrast, membrane-bound lytic murein transglycosylase E (MltE) is endolytic , cleaving in the middle of PG strands, with further processing to Metabolite 1 accomplished by other LTs. In E. coli, there are six membrane- bound LTs: MltA-MltF and soluble Slt70. Slt35 is a soluble fragment cleaved from MltB. Bacterial LTs are classified in 4 families: Family 1 includes slt70 MltC-MltF, Family 2 includes MltA, Family 3 includes MltB, and family 4 of bacteriophage origin. While most LTs are related members of the lysozyme-like lytic transglycosylase family, MltA represents a distinct fold and sequence conservation.


Pssm-ID: 270619 [Multi-domain]  Cd Length: 104  Bit Score: 84.35  E-value: 6.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201930635 347 VSSTAYTAS-----------CSGCSGHTATGVNLKNnpnAKVIAVDPNVIPLGSKVHVEGY------GYAIAADTGSAIK 409
Cdd:cd14486     1 FQATGYTEWddgkrpsppdeFSFSFRLTASGRPPVP---YRTIAVDPSVIPLGSVVYIPELrglpndGVFVAEDTGGAIK 77

                          90       100
                  ....*....|....*....|....*..
gi 1201930635 410 GNKIDVFFPEKSSAYRWGNKTVKIKIL 436
Cdd:cd14486    78 GNHIDVYTGDGPDARSNALKTVTVYVV 104
DPBB_MltA-like cd22785
double-psi beta-barrel fold of membrane-bound lytic murein transglycosylase A (MltA) and ...
 361-423 1.19e-12

double-psi beta-barrel fold of membrane-bound lytic murein transglycosylase A (MltA) and similar proteins; MltA, also called murein hydrolase A, is a murein-degrading enzyme that may play a role in the recycling of muropeptides during cell elongation and/or cell division. It degrades murein glycan strands and insoluble, high-molecular weight murein sacculi. Bacterial lytic transglycosylases (LTs) are classified into 4 families: family 1 includes slt70 MltC-MltF, family 2 includes MltA, family 3 includes MltB, and family 4 includes proteins of bacteriophage origin. MltA is distinct from other bacterial LTs, which are similar in structure and sequence with a lysozyme-like fold. MltA is a kidney bean-shaped monomeric protein comprised of two domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, which corresponds to a double-psi beta-barrel (DPBB) fold. Domain B also has a beta-barrel fold topology, but it is inserted within the linear sequence of domain A. This model corresponds to the DPBB fold that consists of two interlocked "psi-structure" motifs related by a pseudo-2-fold axis. It is involved in substrate binding and catalysis.


Pssm-ID: 439262 [Multi-domain]  Cd Length: 97  Bit Score: 63.81  E-value: 1.19e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1201930635 361 GHTATGVNLKNNpnaKVIAVDPNVIPLGSKVHVEGY------------GYAIAADTGSAIKGNKIDVFFPEKSSA 423
Cdd:cd22785    10 PRGALGVPLTPF---RSVAVDPSVIPLGSVVYIPALdgvklpdgephdGLFIAQDTGGAIKGKHIDVFTGSGDEA 81
DUF348 pfam03990
G5-linked-Ubiquitin-like domain; This domain normally occurs as tandem repeats; however it is ...
 184-224 6.44e-11

G5-linked-Ubiquitin-like domain; This domain normally occurs as tandem repeats; however it is found as a single copy in the S. cerevisiae DNA-binding nuclear protein YCR593. This protein is involved in sporulation part of the SET3C complex, which is required to repress early/middle sporulation genes during meiosis. The bacterial proteins are likely to be involved in a cell wall function as they are found in conjunction with the pfam07501 domain, which is involved in various cell surface processes. This domain is also present in the resuscitation-promoting factors RpfB from Mycobacterium tuberculosis and Rpf2 from Corynebacterium glutamicum. These are factors that stimulate resuscitation of dormant cells. This domain has a beta grasp fold. Structural description of this domain revealed a structural conservation between these domains and ubiquitin, hence it is termed UBL-G5.


Pssm-ID: 461121 [Multi-domain]  Cd Length: 41  Bit Score: 57.04  E-value: 6.44e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1201930635 184 VTVNDAGKQKKIWTTSTTVADFLKQQKMNIKDEDKIKPALD 224
Cdd:pfam03990   1 VTLTVDGKERTVTTTAGTVGDLLEEAGITLGEHDKVSPSLD 41
DUF348 pfam03990
G5-linked-Ubiquitin-like domain; This domain normally occurs as tandem repeats; however it is ...
 127-167 5.07e-10

G5-linked-Ubiquitin-like domain; This domain normally occurs as tandem repeats; however it is found as a single copy in the S. cerevisiae DNA-binding nuclear protein YCR593. This protein is involved in sporulation part of the SET3C complex, which is required to repress early/middle sporulation genes during meiosis. The bacterial proteins are likely to be involved in a cell wall function as they are found in conjunction with the pfam07501 domain, which is involved in various cell surface processes. This domain is also present in the resuscitation-promoting factors RpfB from Mycobacterium tuberculosis and Rpf2 from Corynebacterium glutamicum. These are factors that stimulate resuscitation of dormant cells. This domain has a beta grasp fold. Structural description of this domain revealed a structural conservation between these domains and ubiquitin, hence it is termed UBL-G5.


Pssm-ID: 461121 [Multi-domain]  Cd Length: 41  Bit Score: 54.35  E-value: 5.07e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1201930635 127 VKLTINGEEKTLWSTAKTVGALLDEQDVDVKEQDQIDPAID 167
Cdd:pfam03990   1 VTLTVDGKERTVTTTAGTVGDLLEEAGITLGEHDKVSPSLD 41
DUF348 pfam03990
G5-linked-Ubiquitin-like domain; This domain normally occurs as tandem repeats; however it is ...
 70-108 5.52e-09

G5-linked-Ubiquitin-like domain; This domain normally occurs as tandem repeats; however it is found as a single copy in the S. cerevisiae DNA-binding nuclear protein YCR593. This protein is involved in sporulation part of the SET3C complex, which is required to repress early/middle sporulation genes during meiosis. The bacterial proteins are likely to be involved in a cell wall function as they are found in conjunction with the pfam07501 domain, which is involved in various cell surface processes. This domain is also present in the resuscitation-promoting factors RpfB from Mycobacterium tuberculosis and Rpf2 from Corynebacterium glutamicum. These are factors that stimulate resuscitation of dormant cells. This domain has a beta grasp fold. Structural description of this domain revealed a structural conservation between these domains and ubiquitin, hence it is termed UBL-G5.


Pssm-ID: 461121 [Multi-domain]  Cd Length: 41  Bit Score: 51.65  E-value: 5.52e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1201930635  70 VSVSINGKKKHIRTHANTVGDLLETLDIKTRDEDKITPA 108
Cdd:pfam03990   1 VTLTVDGKERTVTTTAGTVGDLLEEAGITLGEHDKVSPS 39
mltA_like_LT_A cd14485
Domain A of MltA and related lytic transglycosylase; domain A is interrupted by domain B; ...
 378-417 3.06e-06

Domain A of MltA and related lytic transglycosylase; domain A is interrupted by domain B; Escherichia coli MltA is a membrane-bound lytic transglycosylase comprised of two domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, which correspond to the 3D domain, named for 3 conserved aspartate residues. Domain B is inserted within the linear sequence of domain A. MltA is distinct from other bacterial lytic transglycosylases (LTs), which are similar to each other. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. PG chains (also known as murein), the major components of the bacterial cell wall, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), and lytic transglycosylases cleave this beta-1-4 bond. Typically, peptidoglycan lytic transglycosylases (LT) are exolytic, releasing Metabolite 1 (GlcNAc-anhMurNAc-L-Ala-D-Glu-m-Dap-D-Ala-D-Ala) from the ends of the PG strands. In contrast, MltE is endolytic , cleaving in the middle of PG strands, with further processing to Metabolite 1 accomplished by other LTs. In E. coli, there are six membrane-bound LTs: MltA-MltF and soluble Slt70. Slt35 is a soluble fragment cleaved from MltB. Bacterial LTs are classified in 4 families: Family 1 includes slt70 MltC-MltF, Family 2 includes MltA, Family 3 includes MltB, and Family 4 of bacteriophage origin. While most of the LT family members are similar in structure and sequence with a lysozyme-like fold, Family 2 (including mltA) is distinct.


Pssm-ID: 270618 [Multi-domain]  Cd Length: 159  Bit Score: 46.86  E-value: 3.06e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1201930635 378 IAVDPNVIPLGSKVHVEG------------YGYAIAADTGSAIKG-NKIDVFF 417
Cdd:cd14485    85 LAVDRSLIPLGAPVWLETplpdangggkplRRLVIAQDTGGAIKGpVRADLFW 137
MltA COG2821
Membrane-bound lytic murein transglycosylase [Cell wall/membrane/envelope biogenesis];
378-417 3.21e-05

Membrane-bound lytic murein transglycosylase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442069 [Multi-domain]  Cd Length: 388  Bit Score: 46.02  E-value: 3.21e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1201930635 378 IAVDPNVIPLGSKVHVEGYG------------YAIAADTGSAIKG-NKIDVFF 417
Cdd:COG2821   305 IAVDPSLIPLGAPVWLETTLpdanfsgkplrrLMIAQDTGGAIKGaVRADLFW 357
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH