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Conserved domains on  [gi|490365314|ref|WP_004244978|]
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MULTISPECIES: murein transglycosylase D [Proteus]

Protein Classification

murein transglycosylase D( domain architecture ID 11484940)

membrane-bound lytic murein transglycosylase D catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acetyl-D-glucosamine (GlcNAc)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 1-444 0e+00

membrane-bound lytic murein transglycosylase D; Provisional


:

Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 716.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314   1 MKTKVILFSILLLAGCQQSK---SIKPDLSAITPTSLGTSTSYQPQ---------YDIKTNLWGYVVSELKMDIPDNERI 68
Cdd:PRK10783   1 MKAKAILLASVLLVGCQSSKndaTVQQHAQSLSSAGQGEAGKYTSQarwmddgtsIAPDQDLWAFIGDELKMGIPENSRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314  69 SQQETYFLNNPKHIQTVALRAEPYMYWIIEEIEKRNLPMELALVPVVESAFNPHVTSSAKAAGLWQFVPVTANYYGLAQN 148
Cdd:PRK10783  81 REQKQKYLRNKSYLHDVTLRAEPYMYWIVGQIKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314 149 QWYDGRRDVVASTNAALDLLERLYIMFDSDWPLALAAYNAGEGRVMQAIKANESKNLPTDYWSLSLPKETMNYVPKILAL 228
Cdd:PRK10783 161 RWYDARRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGRVMKAIKANKAKGKPTDFWSLSLPRETKIYVPKMLAL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314 229 SKVIRDNEA-DITFPKSNyRDKSLAAIDIGEQITLSKVAELSQLPITTVKDYNPGYKRGITAPNGPHVILLPRNKLAQFQ 307
Cdd:PRK10783 241 SDILKNSKRyGVRLPTTD-ESRALARVDLGQQIELAQAAEMAGMSLTKLKTFNAGYKRSTTAPSGPHYIMVPKKHADQLR 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314 308 NAFADEAILKTIRLAVAKANqsIKQEGIYKVRSGDSFYAIARRYNMSVKELQRLNGLSAkSTLLVGQTLKIHNAGSVNNr 387
Cdd:PRK10783 320 ESLASGEIAAVQSTLVADNT--PLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRG-SKLKVGQTLTIGAGSSAQR- 395

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490365314 388 ptsKPTGASPSYYKVRQGDSYYSIARRHNINLKQLMSWNADIK-MLKPGTQLTLYLKK 444
Cdd:PRK10783 396 ---LANNSDSITYRVRKGDSLSSIAKRHGVNIKDVMRWNSDTAkNLQPGDKLTLFVKN 450
 
Name Accession Description Interval E-value
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 1-444 0e+00

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 716.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314   1 MKTKVILFSILLLAGCQQSK---SIKPDLSAITPTSLGTSTSYQPQ---------YDIKTNLWGYVVSELKMDIPDNERI 68
Cdd:PRK10783   1 MKAKAILLASVLLVGCQSSKndaTVQQHAQSLSSAGQGEAGKYTSQarwmddgtsIAPDQDLWAFIGDELKMGIPENSRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314  69 SQQETYFLNNPKHIQTVALRAEPYMYWIIEEIEKRNLPMELALVPVVESAFNPHVTSSAKAAGLWQFVPVTANYYGLAQN 148
Cdd:PRK10783  81 REQKQKYLRNKSYLHDVTLRAEPYMYWIVGQIKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314 149 QWYDGRRDVVASTNAALDLLERLYIMFDSDWPLALAAYNAGEGRVMQAIKANESKNLPTDYWSLSLPKETMNYVPKILAL 228
Cdd:PRK10783 161 RWYDARRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGRVMKAIKANKAKGKPTDFWSLSLPRETKIYVPKMLAL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314 229 SKVIRDNEA-DITFPKSNyRDKSLAAIDIGEQITLSKVAELSQLPITTVKDYNPGYKRGITAPNGPHVILLPRNKLAQFQ 307
Cdd:PRK10783 241 SDILKNSKRyGVRLPTTD-ESRALARVDLGQQIELAQAAEMAGMSLTKLKTFNAGYKRSTTAPSGPHYIMVPKKHADQLR 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314 308 NAFADEAILKTIRLAVAKANqsIKQEGIYKVRSGDSFYAIARRYNMSVKELQRLNGLSAkSTLLVGQTLKIHNAGSVNNr 387
Cdd:PRK10783 320 ESLASGEIAAVQSTLVADNT--PLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRG-SKLKVGQTLTIGAGSSAQR- 395

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490365314 388 ptsKPTGASPSYYKVRQGDSYYSIARRHNINLKQLMSWNADIK-MLKPGTQLTLYLKK 444
Cdd:PRK10783 396 ---LANNSDSITYRVRKGDSLSSIAKRHGVNIKDVMRWNSDTAkNLQPGDKLTLFVKN 450
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
 100-229 2.41e-62

Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases (LT) catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc). Membrane-bound lytic murein transglycosylase D protein (MltD) family members may have one or more small LysM domains, which may contribute to peptidoglycan binding. Unlike the similar "goose-type" lysozymes, LTs 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, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).


Pssm-ID: 381615 [Multi-domain]  Cd Length: 129  Bit Score: 197.74  E-value: 2.41e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314 100 IEKRNLPMELALVPVVESAFNPHVTSSAKAAGLWQFVPVTANYYGLAQNQWYDGRRDVVASTNAALDLLERLYIMFDsDW 179
Cdd:cd16894    1 LLKEGLPEELKYLALVESGFNPDAVSSAGAAGLWQFMPATAREYGLRVDSWVDERRDPEKSTRAAARYLKDLYKRFG-DW 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 490365314 180 PLALAAYNAGEGRVMQAIKANESKNlPTDYWSLSLPKETMNYVPKILALS 229
Cdd:cd16894   80 LLALAAYNAGEGRVRRAIKRAGTDK-WEDYYRLYLPAETRRYVPKFLAAK 128
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 86-235 1.32e-39

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: 142.44  E-value: 1.32e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314  86 ALRAEPYMYWIIEEIEKRNLPMELAL-VPVVESAFNPHVTSSAKAAGLWQFVPVTANYYGLAQNQ--WYDGRRDVVASTN 162
Cdd:COG0741   97 LRRPLPYLPLIEEAAKKYGVDPALVLaLIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKLGLgpSPDDLFDPETNIR 176

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490365314 163 AALDLLERLYIMFDSDWPLALAAYNAGEGRVMQAIKANesknlPTDYWSlSLP-KETMNYVPKILALSKVIRDN 235
Cdd:COG0741  177 AGAAYLRELLDRFDGDLVLALAAYNAGPGRVRRWLRRN-----GDRDGE-IIPyAETRNYVKKVLANYAIYRAG 244
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 96-204 2.83e-30

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: 113.17  E-value: 2.83e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314   96 IIEEIEKRNL-PMELALVPVVESAFNPHVTSSAKAAGLWQFVPVTANYYGLAQNQWYDGRRDVVASTNAALDLLERLYIM 174
Cdd:pfam01464   1 IIKAAQKYGVdPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLRVNPGVDDLFDPEKNIKAGTKYLKELYKQ 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 490365314  175 FDSDWPLALAAYNAGEGRVMQAIKANESKN 204
Cdd:pfam01464  81 YGGDLWLALAAYNAGPGRVRKWIKNAGAKD 110
LysM smart00257
Lysin motif;
335-378 2.44e-12

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 60.92  E-value: 2.44e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 490365314   335 IYKVRSGDSFYAIARRYNMSVKELQRLNGLSAKSTLLVGQTLKI 378
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
 
Name Accession Description Interval E-value
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 1-444 0e+00

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 716.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314   1 MKTKVILFSILLLAGCQQSK---SIKPDLSAITPTSLGTSTSYQPQ---------YDIKTNLWGYVVSELKMDIPDNERI 68
Cdd:PRK10783   1 MKAKAILLASVLLVGCQSSKndaTVQQHAQSLSSAGQGEAGKYTSQarwmddgtsIAPDQDLWAFIGDELKMGIPENSRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314  69 SQQETYFLNNPKHIQTVALRAEPYMYWIIEEIEKRNLPMELALVPVVESAFNPHVTSSAKAAGLWQFVPVTANYYGLAQN 148
Cdd:PRK10783  81 REQKQKYLRNKSYLHDVTLRAEPYMYWIVGQIKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314 149 QWYDGRRDVVASTNAALDLLERLYIMFDSDWPLALAAYNAGEGRVMQAIKANESKNLPTDYWSLSLPKETMNYVPKILAL 228
Cdd:PRK10783 161 RWYDARRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGRVMKAIKANKAKGKPTDFWSLSLPRETKIYVPKMLAL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314 229 SKVIRDNEA-DITFPKSNyRDKSLAAIDIGEQITLSKVAELSQLPITTVKDYNPGYKRGITAPNGPHVILLPRNKLAQFQ 307
Cdd:PRK10783 241 SDILKNSKRyGVRLPTTD-ESRALARVDLGQQIELAQAAEMAGMSLTKLKTFNAGYKRSTTAPSGPHYIMVPKKHADQLR 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314 308 NAFADEAILKTIRLAVAKANqsIKQEGIYKVRSGDSFYAIARRYNMSVKELQRLNGLSAkSTLLVGQTLKIHNAGSVNNr 387
Cdd:PRK10783 320 ESLASGEIAAVQSTLVADNT--PLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRG-SKLKVGQTLTIGAGSSAQR- 395

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490365314 388 ptsKPTGASPSYYKVRQGDSYYSIARRHNINLKQLMSWNADIK-MLKPGTQLTLYLKK 444
Cdd:PRK10783 396 ---LANNSDSITYRVRKGDSLSSIAKRHGVNIKDVMRWNSDTAkNLQPGDKLTLFVKN 450
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
 100-229 2.41e-62

Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases (LT) catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc). Membrane-bound lytic murein transglycosylase D protein (MltD) family members may have one or more small LysM domains, which may contribute to peptidoglycan binding. Unlike the similar "goose-type" lysozymes, LTs 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, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).


Pssm-ID: 381615 [Multi-domain]  Cd Length: 129  Bit Score: 197.74  E-value: 2.41e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314 100 IEKRNLPMELALVPVVESAFNPHVTSSAKAAGLWQFVPVTANYYGLAQNQWYDGRRDVVASTNAALDLLERLYIMFDsDW 179
Cdd:cd16894    1 LLKEGLPEELKYLALVESGFNPDAVSSAGAAGLWQFMPATAREYGLRVDSWVDERRDPEKSTRAAARYLKDLYKRFG-DW 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 490365314 180 PLALAAYNAGEGRVMQAIKANESKNlPTDYWSLSLPKETMNYVPKILALS 229
Cdd:cd16894   80 LLALAAYNAGEGRVRRAIKRAGTDK-WEDYYRLYLPAETRRYVPKFLAAK 128
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 86-235 1.32e-39

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: 142.44  E-value: 1.32e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314  86 ALRAEPYMYWIIEEIEKRNLPMELAL-VPVVESAFNPHVTSSAKAAGLWQFVPVTANYYGLAQNQ--WYDGRRDVVASTN 162
Cdd:COG0741   97 LRRPLPYLPLIEEAAKKYGVDPALVLaLIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKLGLgpSPDDLFDPETNIR 176

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490365314 163 AALDLLERLYIMFDSDWPLALAAYNAGEGRVMQAIKANesknlPTDYWSlSLP-KETMNYVPKILALSKVIRDN 235
Cdd:COG0741  177 AGAAYLRELLDRFDGDLVLALAAYNAGPGRVRRWLRRN-----GDRDGE-IIPyAETRNYVKKVLANYAIYRAG 244
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
 71-227 9.45e-36

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


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 136.73  E-value: 9.45e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314  71 QETYFLNNPKHIQTVAL----RAEPYMYWIIEEIEKRNLPME-LALVPVVESAFNPHVTSSAKAAGLWQFVPVTANYYGL 145
Cdd:COG4623  239 YERYFGHVKRDTRAFLRriegRLPPYDPLFEKYAEEYGLDWRlLAALAYQESHWNPRARSPTGARGLMQLMPATAKELGV 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314 146 aqnqwyDGRRDVVASTNAALDLLERLYIMFDS------DWPLALAAYNAGEGRVMQAIKANESKNLPTDYWSLS------ 213
Cdd:COG4623  319 ------DDRLDPEQSIRAGAKYLRWLYDRFPEaidepdRWWFALAAYNAGPGHVQDARRLAKKQGLDPDRWFDVeksqpk 392

                        170       180
                 ....*....|....*....|.
gi 490365314 214 -------LPKETMNYVPKILA 227
Cdd:COG4623  393 yydtgyaRGRETVNYVPNIRA 413
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 96-204 2.83e-30

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: 113.17  E-value: 2.83e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314   96 IIEEIEKRNL-PMELALVPVVESAFNPHVTSSAKAAGLWQFVPVTANYYGLAQNQWYDGRRDVVASTNAALDLLERLYIM 174
Cdd:pfam01464   1 IIKAAQKYGVdPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLRVNPGVDDLFDPEKNIKAGTKYLKELYKQ 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 490365314  175 FDSDWPLALAAYNAGEGRVMQAIKANESKN 204
Cdd:pfam01464  81 YGGDLWLALAAYNAGPGRVRKWIKNAGAKD 110
Slt70-like cd13401
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ...
 91-227 2.95e-20

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: 86.76  E-value: 2.95e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314  91 PYMYWIIEEIEKRNLPMELALVpVV--ESAFNPHVTSSAKAAGLWQFVPVTANYYGLAQNQWYDGRRDV-VASTNAAL-- 165
Cdd:cd13401    5 PYRDLVERAAKKNGLDPALVYA-IIrqESAFDPDAVSPAGALGLMQLMPATAKDVAKKLGLPYYSPRDLfDPEYNIRLgs 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490365314 166 ----DLLERlyimFDSDWPLALAAYNAGEGRVMQAIKANEskNLPTDYWSLSLP-KETMNYVPKILA 227
Cdd:cd13401   84 aylaELLDR----FDGNPVLALAAYNAGPGRVRRWLKRRG--DLDPDLWIETIPfSETRNYVKRVLE 144
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
 115-227 1.57e-19

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: 83.42  E-value: 1.57e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314 115 VESAFNPHVTSSAKAAGLWQFVPVTANYYGLAQNqwyDGRRDVVASTNAALDLLERLYIMFDSDWPLALAAYNAGEGRVM 194
Cdd:cd00254   10 VESGFNPRAVSPAGARGLMQLMPGTARDLGRRGV---DDLFDPEENIRAGARYLRELLDRFGGDLELALAAYNAGPGAVD 86

                         90       100       110
                 ....*....|....*....|....*....|...
gi 490365314 195 qaiKANESKNLPtdywslslPKETMNYVPKILA 227
Cdd:cd00254   87 ---RWGGGEVPP--------YKETRNYVQRVLA 108
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
250-378 3.45e-15

LysM repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 72.82  E-value: 3.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314 250 SLAAIDIGEQITLSKVAELSQLPITTVKDYNPGYKRGITAPNGPHVILLPRNKLAQFQNAFADEAILKTIRLAVAKANQS 329
Cdd:COG1388   12 LLAAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKSG 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490365314 330 IKQEGI--------------YKVRSGDSFYAIARRYNMSVKELQRLNGLSAkSTLLVGQTLKI 378
Cdd:COG1388   92 DTLSGIarrygaaaapspvtYTVKKGDTLWSIARRYGVSVEELKRWNGLSS-DTIRPGQKLKI 153
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
335-440 4.64e-13

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 70.88  E-value: 4.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314 335 IYKVRSGDSFYAIARRYNMSVKELQRLNGLSAkSTLLVGQTLKIHNAGSVNNRPTSKPTGASPS-----YYKVRQGDSYY 409
Cdd:PRK06347 481 VYTVAKGDSLWRIANNNKVTIANLKSWNNLKS-DFIYPGQKLKVSAGSTTNNTNTAKPSTNKPSnstvkTYTVKKGDSLW 559

                         90       100       110
                 ....*....|....*....|....*....|..
gi 490365314 410 SIARRHNINLKQLMSWNA-DIKMLKPGTQLTL 440
Cdd:PRK06347 560 AISRQYKTTVDNIKAWNKlTSNMIHVGQKLTI 591
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 335-378 4.83e-13

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 63.27  E-value: 4.83e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 490365314 335 IYKVRSGDSFYAIARRYNMSVKELQRLNGLSAKSTLLVGQTLKI 378
Cdd:cd00118    2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 336-378 2.20e-12

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 61.26  E-value: 2.20e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 490365314  336 YKVRSGDSFYAIARRYNMSVKELQRLNGLSAkSTLLVGQTLKI 378
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSS-PNLYVGQKLKI 42
LysM smart00257
Lysin motif;
335-378 2.44e-12

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 60.92  E-value: 2.44e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 490365314   335 IYKVRSGDSFYAIARRYNMSVKELQRLNGLSAKSTLLVGQTLKI 378
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
MLTF-like cd13403
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily ...
 116-227 9.19e-12

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: 62.94  E-value: 9.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314 116 ESAFNPHVTSSAKAAGLWQFVPVTANYYGLAQnqwydgRRDVVASTNAALDLLERLYIMFDSDWP------LALAAYNAG 189
Cdd:cd13403   22 ESRFNPNARSPAGARGLMQLMPSTARELGVND------RLDPEQNIHAGAKYLRYLRDRFPPDIDepdrlkFALAAYNAG 95

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490365314 190 EGRVMQAIKANESKNLPTDYWS--------LSLPK-------------ETMNYVPKILA 227
Cdd:cd13403   96 PGHVRDARRLAKKYGLNPNVWFdnvevlplLKSPYydpvvkygyargrETVNYVRNIRK 154
LT_Slt70-like cd16896
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ...
 115-226 2.33e-11

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: 61.37  E-value: 2.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314 115 VESAFNPHVTSSAKAAGLWQFVPVTANY----YGLaQNQWYDGRRDvvASTNAALDL--LERLYIMFDSDWPLALAAYNA 188
Cdd:cd16896   28 VESNFNPNAVSSKGAIGLMQIMPETAEWiaekLGL-EDFSEDDLYD--PETNIRLGTwyLSYLLKEFDGNLVLALAAYNA 104

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 490365314 189 GEGRVMQAIKanESKNLPTDYWSLSLP-KETMNYVPKIL 226
Cdd:cd16896  105 GPGNVDKWLK--DGGWSGDGKTLDQIPfPETRHYVKKVL 141
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
335-426 4.21e-11

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 64.72  E-value: 4.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314 335 IYKVRSGDSFYAIARRYNMSVKELQRLNGLSAkSTLLVGQTLKIHNAGSVNNRPTSKP-TGASPS-----------YYKV 402
Cdd:PRK06347 332 IYTVVKGDSLWRIANNHKVTVANLKAWNNLKS-DFIYPGQKLKVSAGSTTSDTNTSKPsTGTSTSkpstgtstnakVYTV 410

                         90       100
                 ....*....|....*....|....
gi 490365314 403 RQGDSYYSIARRHNINLKQLMSWN 426
Cdd:PRK06347 411 VKGDSLWRIANNNKVTIANLKSWN 434
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
335-426 4.56e-11

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 64.72  E-value: 4.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314 335 IYKVRSGDSFYAIARRYNMSVKELQRLNGLSAkSTLLVGQTLKIhNAGSVNNRPTSKP------------TGASPSYYKV 402
Cdd:PRK06347 407 VYTVVKGDSLWRIANNNKVTIANLKSWNNLKS-DFIYPGQKLKV-SAGSTSNTNTSKPstntntskpstnTNTNAKVYTV 484

                         90       100
                 ....*....|....*....|....
gi 490365314 403 RQGDSYYSIARRHNINLKQLMSWN 426
Cdd:PRK06347 485 AKGDSLWRIANNNKVTIANLKSWN 508
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 399-440 2.61e-09

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 52.49  E-value: 2.61e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 490365314 399 YYKVRQGDSYYSIARRHNINLKQLMSWNADIK--MLKPGTQLTL 440
Cdd:cd00118    2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLINpdCIYPGQKLKI 45
LysM smart00257
Lysin motif;
399-440 3.85e-09

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 52.06  E-value: 3.85e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 490365314   399 YYKVRQGDSYYSIARRHNINLKQLMSWNADIK--MLKPGTQLTL 440
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDpdNLQVGQKLKI 44
Slt35-like cd13399
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ...
 115-191 4.07e-09

Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic transglycosylase Slt35 and Pseudomonas aeruginosa Sltb1. Lytic transglycosylase (LT) 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 to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this 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: 381602 [Multi-domain]  Cd Length: 108  Bit Score: 53.85  E-value: 4.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314 115 VESAFNPH-VTSSAKAAGLWQFVPVTANYYGLAQNQwyDGRRDVV----ASTNAALDLLER---LYIMFDSDWPLALAAY 186
Cdd:cd13399   14 VESGFGPNaGGSPAGAQGIAQFMPSTWKAYGVDGNG--DGKADPFnpedAIASAANYLCRHgwdLNAFLGEDNFLALAAY 91


                 ....*
gi 490365314 187 NAGEG 191
Cdd:cd13399   92 NAGPG 96
LT_MltC_MltE cd16893
membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and ...
 95-230 2.90e-08

membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and MltE are periplasmic, outer membrane attached lytic transglycosylases (LTs), which cleave beta-1,4-glycosidic bonds joining N-acetylmuramic acid and N-acetylglucosamine in the cell wall peptidoglycan, yielding 1,6-anhydromuropeptides. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda


Pssm-ID: 381614 [Multi-domain]  Cd Length: 162  Bit Score: 52.95  E-value: 2.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314  95 WIIEEIEKRNLPMELAL-VPVVESAFNPHVTSSAKAAGLWQFVPVTAnyyGLAQNQWYDGRRDVV-------ASTN---- 162
Cdd:cd16893    2 IVEKYAKKYGVDPALILaIIETESSFNPYAVSHSPAYGLMQIVPSTA---GRDVYRLLGGKGGLPsksylfdPENNidig 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314 163 -AALDLLE------------RLYimfdsdwpLALAAYNAGEGRVM--------QAIKANESKNLPTDYWSLS--LP-KET 218
Cdd:cd16893   79 tAYLHILQnrylkgiknpksREY--------CAIAAYNGGAGNVLrtfssdrkKAISKINRLSPDEVYQHLTkkLPaAET 150

                        170
                 ....*....|..
gi 490365314 219 MNYVPKILALSK 230
Cdd:cd16893  151 RNYLKKVLKAKK 162
PHA00368 PHA00368
internal virion protein D
 115-324 3.74e-08

internal virion protein D


Pssm-ID: 222785 [Multi-domain]  Cd Length: 1315  Bit Score: 55.94  E-value: 3.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314  115 VESAFNPHVTSSAKAAGLWQFVPVTANYYGLAQNQwyDGRRDVVASTNAALDLLERLYIMFDSDWPLALAAYNAGEGRvm 194
Cdd:PHA00368   35 DESRFNPTAKSPTGPKGLMQFTKATAKALGLIVDD--DDRLDPELAIDAGARYLADLVGKYDGDELKAALAYNQGEGR-- 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314  195 qaIKANESKNLPTDYWSlSLPKETMNYVPKILALSKVIRDNEADiTFPKSNYRDKSLAAIDIGEQITlSKVAELSQLPIT 274
Cdd:PHA00368  111 --LGAPQLEAYDKGDFA-SISEEGRNYLRNLLDVAKSPKSGDLE-SFGGITPKAKGIPAEAAFEGIG-KKGKVGTELPES 185

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314  275 TVKDY--------NPGYKRGITAPNGPhvILLPRNKLAQFQNaFAD--EAILKTIRLAVA 324
Cdd:PHA00368  186 HGFSVegkeqeapNVPFAKDFWEATGE--TLDEANSRSTFFG-FGDatEAELSNSVLGVA 242
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 400-440 5.27e-08

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 48.93  E-value: 5.27e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 490365314  400 YKVRQGDSYYSIARRHNINLKQLMSWNaDIK--MLKPGTQLTL 440
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELN-GLSspNLYVGQKLKI 42
PRK11619 PRK11619
lytic murein transglycosylase; Provisional
 116-227 4.71e-07

lytic murein transglycosylase; Provisional


Pssm-ID: 183236 [Multi-domain]  Cd Length: 644  Bit Score: 51.99  E-value: 4.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314 116 ESAFNPHVTSSAKAAGLWQFVPVTANY----YGLA----QNQWYDGRRDVVASTNaaldLLERLYIMFDSDWPLALAAYN 187
Cdd:PRK11619 504 ESAWNPKARSPVGASGLMQIMPGTATHtvkmFSIPgyssSSQLLDPETNINIGTS----YLEYVYQQFGNNRILASAAYN 579

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 490365314 188 AGEGRVMQAIKaNESKNLPTDYWSLSLP-KETMNYVPKILA 227
Cdd:PRK11619 580 AGPGRVRTWLG-NSAGRIDAVAFVESIPfSETRGYVKNVLA 619
PHA00658 PHA00658
putative lysin
 123-224 8.39e-07

putative lysin


Pssm-ID: 106967 [Multi-domain]  Cd Length: 720  Bit Score: 51.36  E-value: 8.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314 123 VTSSAKAAGLWQFVPVTA-NYYGLAQNQWYDGRRDVVASTNAALDL--LERLYIMFDSDWPLALAAYNAGEGRVMQAIKA 199
Cdd:PHA00658 324 LTSPKGAVGIAQVMPDTApEAAKLAGLPWDENRYRNDAAYNRALGMayFQKQLRDFGGDLPKAYAAYNAGPGALQSALKD 403

                         90       100
                 ....*....|....*....|....*
gi 490365314 200 NESKNlptdyWSLSLPKETMNYVPK 224
Cdd:PHA00658 404 AKDGN-----WLALLPKETQDYVVK 423
Lyz-like cd00442
lysozyme-like domains; This family contains several members, including soluble lytic ...
 108-165 9.36e-05

lysozyme-like domains; This family contains several members, including soluble lytic transglycosylases (SLT), goose egg-white lysozymes (GEWL), hen egg-white lysozymes (HEWL), chitinases, bacteriophage lambda lysozymes, endolysins, autolysins, chitosanases, and pesticin. Typical members are involved in the hydrolysis of beta-1,4- linked polysaccharides.


Pssm-ID: 381596 [Multi-domain]  Cd Length: 59  Bit Score: 40.09  E-value: 9.36e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365314 108 ELALVPVVESAFNPH--VTSSAKAAGLWQFVPVTANYYGLAQnqwYDGRRDVVASTNAAL 165
Cdd:cd00442    1 VLAAIIGQESGGNKPanAGSGSGAAGLFQFMPGTWKAYGKNS---SSDLNDPEASIEAAA 57
OapA COG3061
Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell ...
 336-378 4.09e-04

Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442295 [Multi-domain]  Cd Length: 425  Bit Score: 42.35  E-value: 4.09e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 490365314 336 YKVRSGDSFYAIARRYNMSVKELQRL--NGLSAK--STLLVGQTLKI 378
Cdd:COG3061   72 YTVQSGDTLSQIFRRLGLSASDLYALlaAEGDAKplSRLKPGQELRF 118
 
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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