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Conserved domains on  [gi|1789780199|gb|QHB23689|]
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peptidase M23 [Mediterraneibacter gnavus ATCC 29149]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CwlT-like cd16891
CwlT-like N-terminal lysozyme domain and similar domains; CwlT is a bifunctional cell wall ...
 285-432 3.64e-58

CwlT-like N-terminal lysozyme domain and similar domains; CwlT is a bifunctional cell wall hydrolase containing an N-terminal lysozyme domain and a C-terminal NlpC/P60 endopeptidase domain (gamma-d-D-glutamyl-L-diamino acid endopeptidase), and has been implicated in the spread of transposons. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).


:

Pssm-ID: 381612 [Multi-domain]  Cd Length: 151  Bit Score: 191.66  E-value: 3.64e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789780199 285 YRPAVERAAAKYGMSDYVDLILAVMMQESGGRGLDVMQAAEGGFNTryphvPNGITDPEYSIECGIQELKYALDKAGCTG 364
Cdd:cd16891     1 YRPLVEKEAKKYGIPEYVPLILAIIMQESGGKGPDIMQSSESAGLP-----PNTITDPEESIEQGVKYFADVLKKAKGKG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789780199 365 ptdlDRIKLALQGYNYGSAYIDWAMERDGGYTKENAIAYSDMMCAR-------------PSWPYDrYGDKEYVEHVLRYY 431
Cdd:cd16891    76 ----VDIWTAVQAYNFGGGYIDYVAKNGGKYTLELAKAYSREVVAPslgnytgsalyngGYLYYN-YGDFFYVELVMRYL 150


                  .
gi 1789780199 432 Q 432
Cdd:cd16891   151 A 151
Peptidase_C39_like super family cl00296
Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The ...
 469-588 3.71e-20

Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is not conserved in all sub-families.


The actual alignment was detected with superfamily member cd02549:

Pssm-ID: 469710 [Multi-domain]  Cd Length: 141  Bit Score: 87.08  E-value: 3.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789780199 469 GCGPTSFAMIASYLTGTTITPIDAISWCGNSYYKPGVGTYWS--YFQAASDHfgCGAVTQTSDPNQVLQALSEGHPVISS 546
Cdd:cd02549     6 GCGPTSLAMVLSYLGVKVTKPQLAAEGNTYDFAKDGYGTYPKpiVSAAARKY--GLVVRPLTGLLALLRQLAAGHPVIVS 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1789780199 547 QRAGLF-TSGGHFIVLRGVTAGGKVLVNDPNDSSSKNYINREF 588
Cdd:cd02549    84 VNLGVSiTPSGHAMVVIGYDRKGNVYVNDPGGGRRLVVSFDEF 126
 
Name Accession Description Interval E-value
CwlT-like cd16891
CwlT-like N-terminal lysozyme domain and similar domains; CwlT is a bifunctional cell wall ...
 285-432 3.64e-58

CwlT-like N-terminal lysozyme domain and similar domains; CwlT is a bifunctional cell wall hydrolase containing an N-terminal lysozyme domain and a C-terminal NlpC/P60 endopeptidase domain (gamma-d-D-glutamyl-L-diamino acid endopeptidase), and has been implicated in the spread of transposons. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).


Pssm-ID: 381612 [Multi-domain]  Cd Length: 151  Bit Score: 191.66  E-value: 3.64e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789780199 285 YRPAVERAAAKYGMSDYVDLILAVMMQESGGRGLDVMQAAEGGFNTryphvPNGITDPEYSIECGIQELKYALDKAGCTG 364
Cdd:cd16891     1 YRPLVEKEAKKYGIPEYVPLILAIIMQESGGKGPDIMQSSESAGLP-----PNTITDPEESIEQGVKYFADVLKKAKGKG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789780199 365 ptdlDRIKLALQGYNYGSAYIDWAMERDGGYTKENAIAYSDMMCAR-------------PSWPYDrYGDKEYVEHVLRYY 431
Cdd:cd16891    76 ----VDIWTAVQAYNFGGGYIDYVAKNGGKYTLELAKAYSREVVAPslgnytgsalyngGYLYYN-YGDFFYVELVMRYL 150


                  .
gi 1789780199 432 Q 432
Cdd:cd16891   151 A 151
Lysozyme_like pfam13702
Lysozyme-like;
279-431 2.75e-51

Lysozyme-like;


Pssm-ID: 433415 [Multi-domain]  Cd Length: 165  Bit Score: 174.07  E-value: 2.75e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789780199 279 SDEVLSYRPAVERAAAKYGMSDYVDLILAVMMQESGGRGLDVMQAAEGGFNTryphvPNGITDPEYSIECGIQELKYALD 358
Cdd:pfam13702   1 SEEVLAYQPMVEKEAKEQGIPEYVPLILAIIYQESKGKGGDVMQSSESLGGP-----PNTITDPEESIKQGVKYLAENLE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789780199 359 KAGCTGPtdldRIKLALQGYNYGSAYIDWAMERDGGYTKENAIAYSDMMCARPS---------------------WPYDR 417
Cdd:pfam13702  76 KAKKKGV----DLWTAVQAYNFGKGYIDYVAENGGKHTEELAKQYSKEVVAPSLgnttgekytysnpvaieynggWLYAN 151

                         170
                  ....*....|....
gi 1789780199 418 YGDKEYVEHVLRYY 431
Cdd:pfam13702 152 YGNIFYAEHVKQYY 165
Peptidase_C39A cd02549
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
 469-588 3.71e-20

A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family of proteins with a single peptidase domain, which are lacking the nucleotide-binding transporter signature or have different domain architectures.


Pssm-ID: 239109 [Multi-domain]  Cd Length: 141  Bit Score: 87.08  E-value: 3.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789780199 469 GCGPTSFAMIASYLTGTTITPIDAISWCGNSYYKPGVGTYWS--YFQAASDHfgCGAVTQTSDPNQVLQALSEGHPVISS 546
Cdd:cd02549     6 GCGPTSLAMVLSYLGVKVTKPQLAAEGNTYDFAKDGYGTYPKpiVSAAARKY--GLVVRPLTGLLALLRQLAAGHPVIVS 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1789780199 547 QRAGLF-TSGGHFIVLRGVTAGGKVLVNDPNDSSSKNYINREF 588
Cdd:cd02549    84 VNLGVSiTPSGHAMVVIGYDRKGNVYVNDPGGGRRLVVSFDEF 126
Peptidase_C39_2 pfam13529
Peptidase_C39 like family;
446-575 1.54e-17

Peptidase_C39 like family;


Pssm-ID: 379241 [Multi-domain]  Cd Length: 139  Bit Score: 79.41  E-value: 1.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789780199 446 QIPHYLQTDYGNipygggsiasSGCGPTSFAMIASYLtGTTITPIDAISW-------------CGNSYYKPGVGTYWSYF 512
Cdd:pfam13529   1 DVPYYNQLDELP----------NGCGPTSLAMVLSYL-GITVTQDELAKEigtnpdgnpntgfVGNPYDKSGYGVYNPPI 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789780199 513 QAASDHFGCGAVTQT-SDPNQVLQALSEGHPVISSQRAGL-----FTSGGHFIVLRGVTAGGK-VLVNDP 575
Cdd:pfam13529  70 VALAEKYGLKVTDITgSSFDEVIRLLDAGIPVVVSTTTFGplnyyFTSSGHLVVIVGYDDKGDyVYVNDP 139
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 254-433 8.51e-13

Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin domain) [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440504 [Multi-domain]  Cd Length: 244  Bit Score: 68.48  E-value: 8.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789780199 254 AKNYAENLTAFFGTASSGIVAAINLSDEVLSYRPAVERAAAKYGMSDyvDLILAVMMQESGG----------RGLdvMQ- 322
Cdd:COG0741    72 AADALAAFAAIAALAAELLALAALLLRRPLPYLPLIEEAAKKYGVDP--ALVLALIRQESAFnpnavspagaRGL--MQl 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789780199 323 ----AAEGGFNTRYPHVPNGITDPEYSIECGIQELKYALDKAGctgptdlDRIKLALQGYNYGSAYIDWAMERDGGYTKE 398
Cdd:COG0741   148 mpatARRLGLKLGLGPSPDDLFDPETNIRAGAAYLRELLDRFD-------GDLVLALAAYNAGPGRVRRWLRRNGDRDGE 220

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1789780199 399 NaIAYSDMmcarpswpydrygdKEYVEHVLRYYQI 433
Cdd:COG0741   221 I-IPYAET--------------RNYVKKVLANYAI 240
 
Name Accession Description Interval E-value
CwlT-like cd16891
CwlT-like N-terminal lysozyme domain and similar domains; CwlT is a bifunctional cell wall ...
 285-432 3.64e-58

CwlT-like N-terminal lysozyme domain and similar domains; CwlT is a bifunctional cell wall hydrolase containing an N-terminal lysozyme domain and a C-terminal NlpC/P60 endopeptidase domain (gamma-d-D-glutamyl-L-diamino acid endopeptidase), and has been implicated in the spread of transposons. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).


Pssm-ID: 381612 [Multi-domain]  Cd Length: 151  Bit Score: 191.66  E-value: 3.64e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789780199 285 YRPAVERAAAKYGMSDYVDLILAVMMQESGGRGLDVMQAAEGGFNTryphvPNGITDPEYSIECGIQELKYALDKAGCTG 364
Cdd:cd16891     1 YRPLVEKEAKKYGIPEYVPLILAIIMQESGGKGPDIMQSSESAGLP-----PNTITDPEESIEQGVKYFADVLKKAKGKG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789780199 365 ptdlDRIKLALQGYNYGSAYIDWAMERDGGYTKENAIAYSDMMCAR-------------PSWPYDrYGDKEYVEHVLRYY 431
Cdd:cd16891    76 ----VDIWTAVQAYNFGGGYIDYVAKNGGKYTLELAKAYSREVVAPslgnytgsalyngGYLYYN-YGDFFYVELVMRYL 150


                  .
gi 1789780199 432 Q 432
Cdd:cd16891   151 A 151
Lysozyme_like pfam13702
Lysozyme-like;
279-431 2.75e-51

Lysozyme-like;


Pssm-ID: 433415 [Multi-domain]  Cd Length: 165  Bit Score: 174.07  E-value: 2.75e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789780199 279 SDEVLSYRPAVERAAAKYGMSDYVDLILAVMMQESGGRGLDVMQAAEGGFNTryphvPNGITDPEYSIECGIQELKYALD 358
Cdd:pfam13702   1 SEEVLAYQPMVEKEAKEQGIPEYVPLILAIIYQESKGKGGDVMQSSESLGGP-----PNTITDPEESIKQGVKYLAENLE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789780199 359 KAGCTGPtdldRIKLALQGYNYGSAYIDWAMERDGGYTKENAIAYSDMMCARPS---------------------WPYDR 417
Cdd:pfam13702  76 KAKKKGV----DLWTAVQAYNFGKGYIDYVAENGGKHTEELAKQYSKEVVAPSLgnttgekytysnpvaieynggWLYAN 151

                         170
                  ....*....|....
gi 1789780199 418 YGDKEYVEHVLRYY 431
Cdd:pfam13702 152 YGNIFYAEHVKQYY 165
Peptidase_C39A cd02549
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
 469-588 3.71e-20

A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family of proteins with a single peptidase domain, which are lacking the nucleotide-binding transporter signature or have different domain architectures.


Pssm-ID: 239109 [Multi-domain]  Cd Length: 141  Bit Score: 87.08  E-value: 3.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789780199 469 GCGPTSFAMIASYLTGTTITPIDAISWCGNSYYKPGVGTYWS--YFQAASDHfgCGAVTQTSDPNQVLQALSEGHPVISS 546
Cdd:cd02549     6 GCGPTSLAMVLSYLGVKVTKPQLAAEGNTYDFAKDGYGTYPKpiVSAAARKY--GLVVRPLTGLLALLRQLAAGHPVIVS 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1789780199 547 QRAGLF-TSGGHFIVLRGVTAGGKVLVNDPNDSSSKNYINREF 588
Cdd:cd02549    84 VNLGVSiTPSGHAMVVIGYDRKGNVYVNDPGGGRRLVVSFDEF 126
Peptidase_C39_2 pfam13529
Peptidase_C39 like family;
446-575 1.54e-17

Peptidase_C39 like family;


Pssm-ID: 379241 [Multi-domain]  Cd Length: 139  Bit Score: 79.41  E-value: 1.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789780199 446 QIPHYLQTDYGNipygggsiasSGCGPTSFAMIASYLtGTTITPIDAISW-------------CGNSYYKPGVGTYWSYF 512
Cdd:pfam13529   1 DVPYYNQLDELP----------NGCGPTSLAMVLSYL-GITVTQDELAKEigtnpdgnpntgfVGNPYDKSGYGVYNPPI 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789780199 513 QAASDHFGCGAVTQT-SDPNQVLQALSEGHPVISSQRAGL-----FTSGGHFIVLRGVTAGGK-VLVNDP 575
Cdd:pfam13529  70 VALAEKYGLKVTDITgSSFDEVIRLLDAGIPVVVSTTTFGplnyyFTSSGHLVVIVGYDDKGDyVYVNDP 139
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 254-433 8.51e-13

Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin domain) [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440504 [Multi-domain]  Cd Length: 244  Bit Score: 68.48  E-value: 8.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789780199 254 AKNYAENLTAFFGTASSGIVAAINLSDEVLSYRPAVERAAAKYGMSDyvDLILAVMMQESGG----------RGLdvMQ- 322
Cdd:COG0741    72 AADALAAFAAIAALAAELLALAALLLRRPLPYLPLIEEAAKKYGVDP--ALVLALIRQESAFnpnavspagaRGL--MQl 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789780199 323 ----AAEGGFNTRYPHVPNGITDPEYSIECGIQELKYALDKAGctgptdlDRIKLALQGYNYGSAYIDWAMERDGGYTKE 398
Cdd:COG0741   148 mpatARRLGLKLGLGPSPDDLFDPETNIRAGAAYLRELLDRFD-------GDLVLALAAYNAGPGRVRRWLRRNGDRDGE 220

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1789780199 399 NaIAYSDMmcarpswpydrygdKEYVEHVLRYYQI 433
Cdd:COG0741   221 I-IPYAET--------------RNYVKKVLANYAI 240
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
 264-433 2.99e-11

Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 65.85  E-value: 2.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789780199 264 FFGTASSGIVAAINLSDEVLS-YRPAVERAAAKYGMsDYvDLILAVMMQES----------GGRGLdvMQ-----AAEGG 327
Cdd:COG4623   242 YFGHVKRDTRAFLRRIEGRLPpYDPLFEKYAEEYGL-DW-RLLAALAYQEShwnprarsptGARGL--MQlmpatAKELG 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789780199 328 FNTRYphvpngitDPEYSIECGIQELKYALDKAGcTGPTDLDRIKLALQGYNYGSAYIDWAM---ERDGGYT------KE 398
Cdd:COG4623   318 VDDRL--------DPEQSIRAGAKYLRWLYDRFP-EAIDEPDRWWFALAAYNAGPGHVQDARrlaKKQGLDPdrwfdvEK 388

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1789780199 399 NAIAYSDMMCARPSWPYDrygdkeYVEHVLRYYQI 433
Cdd:COG4623   389 SQPKYYDTGYARGRETVN------YVPNIRAYYDI 417
Peptidase_C70 pfam12385
Papain-like cysteine protease AvrRpt2; This is a family of cysteine proteases, found in ...
 457-581 8.02e-10

Papain-like cysteine protease AvrRpt2; This is a family of cysteine proteases, found in actinobacteria, protobacteria and firmicutes. Papain-like cysteine proteases play a crucial role in plant-pathogen/pest interactions. On entering the host they act on non-self substrates, thereby manipulating the host to evade proteolysis. AvrRpt2 from Pseudomonas syringae pv. tomato DC3000 triggers resistance to P. syringae-2-dependent defence responses, including hypersensitive cell death, by cleaving the Arabidopsis RIN4 protein which is monitored by the cognate resistance protein RPS2.


Pssm-ID: 403550 [Multi-domain]  Cd Length: 143  Bit Score: 57.47  E-value: 8.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789780199 457 NIPYGGGSiASSGCGPTSFAMIASYLTGTTITP--IDAISWcgnSYYKPGVGTYWSYFQAASDHFGCGAV---TQTSDPN 531
Cdd:pfam12385   6 DVPYNVQQ-AAMGCWAASASMIAGYRGQKPIDPseIAALVP---GWSQYDTGLNGPEDIALAEKWGLGNVpepPQSYSID 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1789780199 532 QVLQALSEGHPVISSQR-AGLFtsGGHFIVLRGVTA-GGKVLVNDPNDSSSK 581
Cdd:pfam12385  82 ALVKLLRAYGPLWCAIAwPGGF--VGHAIVLTGIDEdGTPVYYHDPWSGPRR 131
MLTF-like cd13403
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily ...
 289-433 3.51e-08

membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily includes membrane-bound lytic murein transglycosylase F (MltF, murein lyase F) that degrades murein glycan strands. It is responsible for catalyzing the release of 1,6-anhydromuropeptides from peptidoglycan. Lytic transglycosylase catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc) as do goose-type lysozymes. However, in addition, it also makes a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.


Pssm-ID: 381606 [Multi-domain]  Cd Length: 161  Bit Score: 53.31  E-value: 3.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789780199 289 VERAAAKYGMsDYVdLILAVMMQES----------GGRGLdvMQ-----AAEGGFNTRYphvpngitDPEYSIECGIQEL 353
Cdd:cd13403     1 FKKYAEKYGF-DWR-LLAAQAYQESrfnpnarspaGARGL--MQlmpstARELGVNDRL--------DPEQNIHAGAKYL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789780199 354 KYaLDKAGCTGPTDLDRIKLALQGYNYGSAYIDWAM---ERDGG------YTKENAIAYSDmmcaRPSWPYDRYGDK--- 421
Cdd:cd13403    69 RY-LRDRFPPDIDEPDRLKFALAAYNAGPGHVRDARrlaKKYGLnpnvwfDNVEVLPLLKS----PYYDPVVKYGYArgr 143

                         170
                  ....*....|....*
gi 1789780199 422 ---EYVEHVLRYYQI 433
Cdd:cd13403   144 etvNYVRNIRKYYDA 158
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
 303-432 2.51e-07

lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble membrane-bound LTs in bacteria and LTs in bacteriophage lambda. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.


Pssm-ID: 381594 [Multi-domain]  Cd Length: 111  Bit Score: 49.52  E-value: 2.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789780199 303 DLILAVMMQESGG----------RGLdvMQ-----AAE-GGFNTRYPHvpngitDPEYSIECGIQELKYALDKAGctgpt 366
Cdd:cd00254     2 ALVLAVIRVESGFnpravspagaRGL--MQlmpgtARDlGRRGVDDLF------DPEENIRAGARYLRELLDRFG----- 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1789780199 367 dlDRIKLALQGYNYGSAYIDWAMERDGGYTKENaiaysdmmcarpswpydrygdKEYVEHVLRYYQ 432
Cdd:cd00254    69 --GDLELALAAYNAGPGAVDRWGGGEVPPYKET---------------------RNYVQRVLAYYQ 111
LT_Slt70-like cd16896
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ...
 283-433 5.69e-07

uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized lytic transglycosylase (LT) with a conserved sequence pattern suggesting similarity to the Slt70, a 70kda soluble lytic transglycosylase which also has an N-terminal U-shaped U-domain and a linker L-domain. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.


Pssm-ID: 381617 [Multi-domain]  Cd Length: 146  Bit Score: 49.43  E-value: 5.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789780199 283 LSYRPAVERAAAKYGMSDYvdLILAVMMQES----------GGRGLdvMQ---------AAEGGFNtryPHVPNGITDPE 343
Cdd:cd16896     2 LKYREYIEKYAKEYGVDPL--LVAAVIKVESnfnpnavsskGAIGL--MQimpetaewiAEKLGLE---DFSEDDLYDPE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789780199 344 YSIECGIQELKYALDKAGctgptdlDRIKLALQGYNYGSAYID-WAmeRDGGYTKE----NAIAYSDMmcarpswpydry 418
Cdd:cd16896    75 TNIRLGTWYLSYLLKEFD-------GNLVLALAAYNAGPGNVDkWL--KDGGWSGDgktlDQIPFPET------------ 133

                         170
                  ....*....|....*
gi 1789780199 419 gdKEYVEHVLRYYQI 433
Cdd:cd16896   134 --RHYVKKVLKNYKI 146
Slt70-like cd13401
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ...
 285-433 7.06e-06

70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the 70kda soluble lytic transglycosylase (LT)-like proteins, which also have an N-terminal U-shaped U-domain and a linker L-domain. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda.


Pssm-ID: 381604 [Multi-domain]  Cd Length: 152  Bit Score: 46.32  E-value: 7.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789780199 285 YRPAVERAAAKYGMSDYvdLILAVMMQES----------GGRGLdvMQ-----AAE--GGFNTRYPHvPNGITDPEYSIE 347
Cdd:cd13401     6 YRDLVERAAKKNGLDPA--LVYAIIRQESafdpdavspaGALGL--MQlmpatAKDvaKKLGLPYYS-PRDLFDPEYNIR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789780199 348 CGIQELKYALDKAGctgptdlDRIKLALQGYNYGSAYID-WAMERDGGYTKEnaiaysdmmcarpsW----PYD--Rygd 420
Cdd:cd13401    81 LGSAYLAELLDRFD-------GNPVLALAAYNAGPGRVRrWLKRRGDLDPDL--------------WietiPFSetR--- 136

                         170
                  ....*....|...
gi 1789780199 421 kEYVEHVLRYYQI 433
Cdd:cd13401   137 -NYVKRVLENYVV 148
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 292-381 4.85e-03

Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found in phages, type II, type III and type IV secretion systems.


Pssm-ID: 396169 [Multi-domain]  Cd Length: 114  Bit Score: 37.29  E-value: 4.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789780199 292 AAAKYGMSdyVDLILAVMMQESGG----------RGL-DVMQAAEGGFNTRYPHVPNGITDPEYSIECGIQELKYALDKA 360
Cdd:pfam01464   4 AAQKYGVD--PSLLLAIAQQESGFnpkavsksgaVGLmQIMPSTAKRLGLRVNPGVDDLFDPEKNIKAGTKYLKELYKQY 81

                          90       100
                  ....*....|....*....|.
gi 1789780199 361 GctgptdlDRIKLALQGYNYG 381
Cdd:pfam01464  82 G-------GDLWLALAAYNAG 95
 
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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