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Conserved domains on  [gi|692318524|ref|WP_032129323|]
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MULTISPECIES: lytic transglycosylase domain-containing protein [Stenotrophomonas]

Protein Classification

lytic transglycosylase domain-containing protein( domain architecture ID 13298820)

lytic transglycosylase domain-containing protein similar to lytic transglycosylase which catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
 108-239 1.93e-45

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: 153.06  E-value: 1.93e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318524 108 LRKANLPTEFALIPFVESGYRPNARNGSGPTGLWQFIATTARNHRVPMANGYDGRLSAVDSTQAAVRYLKTLHGMFgGDW 187
Cdd:cd16894    1 LLKEGLPEELKYLALVESGFNPDAVSSAGAAGLWQFMPATAREYGLRVDSWVDERRDPEKSTRAAARYLKDLYKRF-GDW 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 692318524 188 RLATMAYNAGEYRVLQSMRKAGMNaqNAKPAALPGLSPVTHAYVEKLHALAC 239
Cdd:cd16894   80 LLALAAYNAGEGRVRRAIKRAGTD--KWEDYYRLYLPAETRRYVPKFLAAKI 129
mltD super family cl32574
membrane-bound lytic murein transglycosylase D; Provisional
 103-397 4.51e-40

membrane-bound lytic murein transglycosylase D; Provisional


The actual alignment was detected with superfamily member PRK10783:

Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 147.96  E-value: 4.51e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318524 103 YVVEELRKANLPTEFALIPFVESGYRPNARNGSGPTGLWQFIATTARNHRVPMANGYDGRLSAVDSTQAAVRYLKTLHGM 182
Cdd:PRK10783 107 WIVGQIKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQTRWYDARRDVVASTTAALDMMQRLNKM 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318524 183 FGGDWRLATMAYNAGEYRVLQSMRKagmNAQNAKPAALPGLS-PV-THAYVEKLHALACVLEDVE---------DQPRVM 251
Cdd:PRK10783 187 FDGDWLLTVAAYNSGEGRVMKAIKA---NKAKGKPTDFWSLSlPReTKIYVPKMLALSDILKNSKrygvrlpttDESRAL 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318524 252 ASLDRTVPVlkdhtlpagtSVQQWAAQRALDPARIARLNPALAAGNRA-SGTTRVLAPVSAANATVTEAATTLVAStapv 330
Cdd:PRK10783 264 ARVDLGQQI----------ELAQAAEMAGMSLTKLKTFNAGYKRSTTApSGPHYIMVPKKHADQLRESLASGEIAA---- 329

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 692318524 331 atttptpqVAKTVAAIADRPRSRRHTVRDGESAWTIARRYGMPVKALLSLNGLSGSSvLKPGAVLRV 397
Cdd:PRK10783 330 --------VQSTLVADNTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSK-LKVGQTLTI 387
 
Name Accession Description Interval E-value
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
 108-239 1.93e-45

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: 153.06  E-value: 1.93e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318524 108 LRKANLPTEFALIPFVESGYRPNARNGSGPTGLWQFIATTARNHRVPMANGYDGRLSAVDSTQAAVRYLKTLHGMFgGDW 187
Cdd:cd16894    1 LLKEGLPEELKYLALVESGFNPDAVSSAGAAGLWQFMPATAREYGLRVDSWVDERRDPEKSTRAAARYLKDLYKRF-GDW 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 692318524 188 RLATMAYNAGEYRVLQSMRKAGMNaqNAKPAALPGLSPVTHAYVEKLHALAC 239
Cdd:cd16894   80 LLALAAYNAGEGRVRRAIKRAGTD--KWEDYYRLYLPAETRRYVPKFLAAKI 129
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 103-397 4.51e-40

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 147.96  E-value: 4.51e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318524 103 YVVEELRKANLPTEFALIPFVESGYRPNARNGSGPTGLWQFIATTARNHRVPMANGYDGRLSAVDSTQAAVRYLKTLHGM 182
Cdd:PRK10783 107 WIVGQIKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQTRWYDARRDVVASTTAALDMMQRLNKM 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318524 183 FGGDWRLATMAYNAGEYRVLQSMRKagmNAQNAKPAALPGLS-PV-THAYVEKLHALACVLEDVE---------DQPRVM 251
Cdd:PRK10783 187 FDGDWLLTVAAYNSGEGRVMKAIKA---NKAKGKPTDFWSLSlPReTKIYVPKMLALSDILKNSKrygvrlpttDESRAL 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318524 252 ASLDRTVPVlkdhtlpagtSVQQWAAQRALDPARIARLNPALAAGNRA-SGTTRVLAPVSAANATVTEAATTLVAStapv 330
Cdd:PRK10783 264 ARVDLGQQI----------ELAQAAEMAGMSLTKLKTFNAGYKRSTTApSGPHYIMVPKKHADQLRESLASGEIAA---- 329

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 692318524 331 atttptpqVAKTVAAIADRPRSRRHTVRDGESAWTIARRYGMPVKALLSLNGLSGSSvLKPGAVLRV 397
Cdd:PRK10783 330 --------VQSTLVADNTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSK-LKVGQTLTI 387
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 1-233 6.46e-24

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: 99.30  E-value: 6.46e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318524   1 MMRRSLPLALGLALGLAGTAGAQSLGAGISQNLTAAAALPLDPSALPAPSVRNGQEIFTSFRDGLAEPSCDAEATSPRWQ 80
Cdd:COG0741    4 AAAAAAALALAASAAAALALALLAAAAAAAALAAAAAALAAAAAAAAGAAAAAASAAAGGPALAAALAAADALAAFAAIA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318524  81 KQFAHAPSRLANQDDDALVLFGYVVEELRKANLPTEFAL-IPFVESGYRPNARNGSGPTGLWQFIATTAR--NHRVPMAN 157
Cdd:COG0741   84 ALAAELLALAALLLRRPLPYLPLIEEAAKKYGVDPALVLaLIRQESAFNPNAVSPAGARGLMQLMPATARrlGLKLGLGP 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 692318524 158 GYDGRLSAVDSTQAAVRYLKTLHGMFGGDWRLATMAYNAGEYRVLQSMRKAGmnaqNAKPAALPglSPVTHAYVEK 233
Cdd:COG0741  164 SPDDLFDPETNIRAGAAYLRELLDRFDGDLVLALAAYNAGPGRVRRWLRRNG----DRDGEIIP--YAETRNYVKK 233
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 107-209 1.22e-23

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: 94.68  E-value: 1.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318524  107 ELRKANLPTEFALIPFVESGYRPNARNGSGPTGLWQFIATTARNHRVPMANGYDGRLSAVDSTQAAVRYLKTLHGMFGGD 186
Cdd:pfam01464   5 AQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLRVNPGVDDLFDPEKNIKAGTKYLKELYKQYGGD 84

                          90       100
                  ....*....|....*....|...
gi 692318524  187 WRLATMAYNAGEYRVLQSMRKAG 209
Cdd:pfam01464  85 LWLALAAYNAGPGRVRKWIKNAG 107
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
248-397 8.60e-13

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 65.89  E-value: 8.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318524 248 PRVMASLDRTVPVLKDHTLPAGTSVQQWAAQRALDPARIARLNPALAAGNRASGTTRVLAPVSAANATVTEAATTLVAST 327
Cdd:COG1388    6 LSANAALLAAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAAR 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318524 328 APVATTTPTPQVAKTVAAiADRPRSRRHTVRDGESAWTIARRYGMPVKALLSLNGLSgSSVLKPGAVLRV 397
Cdd:COG1388   86 YTVKSGDTLSGIARRYGA-AAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLS-SDTIRPGQKLKI 153
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 353-397 3.99e-12

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: 60.19  E-value: 3.99e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 692318524 353 RRHTVRDGESAWTIARRYGMPVKALLSLNGLSGSSVLKPGAVLRV 397
Cdd:cd00118    1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 355-397 8.82e-11

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: 56.64  E-value: 8.82e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 692318524  355 HTVRDGESAWTIARRYGMPVKALLSLNGLSgSSVLKPGAVLRV 397
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLS-SPNLYVGQKLKI 42
LysM smart00257
Lysin motif;
355-397 9.14e-11

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 56.69  E-value: 9.14e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 692318524   355 HTVRDGESAWTIARRYGMPVKALLSLNGLSGSSVLKPGAVLRV 397
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
PRK11619 PRK11619
lytic murein transglycosylase; Provisional
 124-201 1.33e-05

lytic murein transglycosylase; Provisional


Pssm-ID: 183236 [Multi-domain]  Cd Length: 644  Bit Score: 47.36  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318524 124 ESGYRPNARNGSGPTGLWQFIATTARnHRVPMAN--GYDGR---LSAVDSTQAAVRYLKTLHGMFGGDWRLATMAYNAGE 198
Cdd:PRK11619 504 ESAWNPKARSPVGASGLMQIMPGTAT-HTVKMFSipGYSSSsqlLDPETNINIGTSYLEYVYQQFGNNRILASAAYNAGP 582


                 ...
gi 692318524 199 YRV 201
Cdd:PRK11619 583 GRV 585
 
Name Accession Description Interval E-value
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
 108-239 1.93e-45

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: 153.06  E-value: 1.93e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318524 108 LRKANLPTEFALIPFVESGYRPNARNGSGPTGLWQFIATTARNHRVPMANGYDGRLSAVDSTQAAVRYLKTLHGMFgGDW 187
Cdd:cd16894    1 LLKEGLPEELKYLALVESGFNPDAVSSAGAAGLWQFMPATAREYGLRVDSWVDERRDPEKSTRAAARYLKDLYKRF-GDW 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 692318524 188 RLATMAYNAGEYRVLQSMRKAGMNaqNAKPAALPGLSPVTHAYVEKLHALAC 239
Cdd:cd16894   80 LLALAAYNAGEGRVRRAIKRAGTD--KWEDYYRLYLPAETRRYVPKFLAAKI 129
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 103-397 4.51e-40

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 147.96  E-value: 4.51e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318524 103 YVVEELRKANLPTEFALIPFVESGYRPNARNGSGPTGLWQFIATTARNHRVPMANGYDGRLSAVDSTQAAVRYLKTLHGM 182
Cdd:PRK10783 107 WIVGQIKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQTRWYDARRDVVASTTAALDMMQRLNKM 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318524 183 FGGDWRLATMAYNAGEYRVLQSMRKagmNAQNAKPAALPGLS-PV-THAYVEKLHALACVLEDVE---------DQPRVM 251
Cdd:PRK10783 187 FDGDWLLTVAAYNSGEGRVMKAIKA---NKAKGKPTDFWSLSlPReTKIYVPKMLALSDILKNSKrygvrlpttDESRAL 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318524 252 ASLDRTVPVlkdhtlpagtSVQQWAAQRALDPARIARLNPALAAGNRA-SGTTRVLAPVSAANATVTEAATTLVAStapv 330
Cdd:PRK10783 264 ARVDLGQQI----------ELAQAAEMAGMSLTKLKTFNAGYKRSTTApSGPHYIMVPKKHADQLRESLASGEIAA---- 329

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 692318524 331 atttptpqVAKTVAAIADRPRSRRHTVRDGESAWTIARRYGMPVKALLSLNGLSGSSvLKPGAVLRV 397
Cdd:PRK10783 330 --------VQSTLVADNTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSK-LKVGQTLTI 387
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 1-233 6.46e-24

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: 99.30  E-value: 6.46e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318524   1 MMRRSLPLALGLALGLAGTAGAQSLGAGISQNLTAAAALPLDPSALPAPSVRNGQEIFTSFRDGLAEPSCDAEATSPRWQ 80
Cdd:COG0741    4 AAAAAAALALAASAAAALALALLAAAAAAAALAAAAAALAAAAAAAAGAAAAAASAAAGGPALAAALAAADALAAFAAIA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318524  81 KQFAHAPSRLANQDDDALVLFGYVVEELRKANLPTEFAL-IPFVESGYRPNARNGSGPTGLWQFIATTAR--NHRVPMAN 157
Cdd:COG0741   84 ALAAELLALAALLLRRPLPYLPLIEEAAKKYGVDPALVLaLIRQESAFNPNAVSPAGARGLMQLMPATARrlGLKLGLGP 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 692318524 158 GYDGRLSAVDSTQAAVRYLKTLHGMFGGDWRLATMAYNAGEYRVLQSMRKAGmnaqNAKPAALPglSPVTHAYVEK 233
Cdd:COG0741  164 SPDDLFDPETNIRAGAAYLRELLDRFDGDLVLALAAYNAGPGRVRRWLRRNG----DRDGEIIP--YAETRNYVKK 233
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 107-209 1.22e-23

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: 94.68  E-value: 1.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318524  107 ELRKANLPTEFALIPFVESGYRPNARNGSGPTGLWQFIATTARNHRVPMANGYDGRLSAVDSTQAAVRYLKTLHGMFGGD 186
Cdd:pfam01464   5 AQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLRVNPGVDDLFDPEKNIKAGTKYLKELYKQYGGD 84

                          90       100
                  ....*....|....*....|...
gi 692318524  187 WRLATMAYNAGEYRVLQSMRKAG 209
Cdd:pfam01464  85 LWLALAAYNAGPGRVRKWIKNAG 107
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
 100-214 2.30e-21

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


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 95.13  E-value: 2.30e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318524 100 LFGYVVEELRKANLPTE-FALIPFVESGYRPNARNGSGPTGLWQFIATTARNHRVpmangyDGRLSAVDSTQAAVRYLKT 178
Cdd:COG4623  264 YDPLFEKYAEEYGLDWRlLAALAYQESHWNPRARSPTGARGLMQLMPATAKELGV------DDRLDPEQSIRAGAKYLRW 337

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 692318524 179 LHGMFG------GDWRLATMAYNAGEYRVLQSMRKAGMNAQN 214
Cdd:COG4623  338 LYDRFPeaidepDRWWFALAAYNAGPGHVQDARRLAKKQGLD 379
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
 123-201 1.44e-13

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: 66.47  E-value: 1.44e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 692318524 123 VESGYRPNARNGSGPTGLWQFIATTARNhrvPMANGYDGRLSAVDSTQAAVRYLKTLHGMFGGDWRLATMAYNAGEYRV 201
Cdd:cd00254   10 VESGFNPRAVSPAGARGLMQLMPGTARD---LGRRGVDDLFDPEENIRAGARYLRELLDRFGGDLELALAAYNAGPGAV 85
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
248-397 8.60e-13

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 65.89  E-value: 8.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318524 248 PRVMASLDRTVPVLKDHTLPAGTSVQQWAAQRALDPARIARLNPALAAGNRASGTTRVLAPVSAANATVTEAATTLVAST 327
Cdd:COG1388    6 LSANAALLAAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAAR 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318524 328 APVATTTPTPQVAKTVAAiADRPRSRRHTVRDGESAWTIARRYGMPVKALLSLNGLSgSSVLKPGAVLRV 397
Cdd:COG1388   86 YTVKSGDTLSGIARRYGA-AAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLS-SDTIRPGQKLKI 153
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 353-397 3.99e-12

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: 60.19  E-value: 3.99e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 692318524 353 RRHTVRDGESAWTIARRYGMPVKALLSLNGLSGSSVLKPGAVLRV 397
Cdd:cd00118    1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 355-397 8.82e-11

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: 56.64  E-value: 8.82e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 692318524  355 HTVRDGESAWTIARRYGMPVKALLSLNGLSgSSVLKPGAVLRV 397
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLS-SPNLYVGQKLKI 42
LysM smart00257
Lysin motif;
355-397 9.14e-11

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 56.69  E-value: 9.14e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 692318524   355 HTVRDGESAWTIARRYGMPVKALLSLNGLSGSSVLKPGAVLRV 397
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
LT_Slt70-like cd16896
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ...
 117-233 4.94e-10

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: 57.52  E-value: 4.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318524 117 FALIpFVESGYRPNARNGSGPTGLWQFIATTAR--NHRVPMANGYDGRL-SAVDSTQAAVRYLKTLHGMFGGDWRLATMA 193
Cdd:cd16896   23 AAVI-KVESNFNPNAVSSKGAIGLMQIMPETAEwiAEKLGLEDFSEDDLyDPETNIRLGTWYLSYLLKEFDGNLVLALAA 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 692318524 194 YNAGEYRVLQSMRKAGMNAQNAKPAALPglSPVTHAYVEK 233
Cdd:cd16896  102 YNAGPGNVDKWLKDGGWSGDGKTLDQIP--FPETRHYVKK 139
Slt70-like cd13401
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ...
 124-201 4.27e-09

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: 54.79  E-value: 4.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318524 124 ESGYRPNARNGSGPTGLWQFIATTAR--NHRVPMANGYDGRLS-AVDSTQAAVRYLKTLHGMFGGDWRLATMAYNAGEYR 200
Cdd:cd13401   31 ESAFDPDAVSPAGALGLMQLMPATAKdvAKKLGLPYYSPRDLFdPEYNIRLGSAYLAELLDRFDGNPVLALAAYNAGPGR 110


                 .
gi 692318524 201 V 201
Cdd:cd13401  111 V 111
Slt35-like cd13399
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ...
 114-199 6.65e-08

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: 50.38  E-value: 6.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318524 114 PTEFALIPFVESGYRPNA-RNGSGPTGLWQFIATTARNHRVPmANGyDGR---LSAVDSTQAAVRYLKT----LHGMFGG 185
Cdd:cd13399    5 PGILAAILGVESGFGPNAgGSPAGAQGIAQFMPSTWKAYGVD-GNG-DGKadpFNPEDAIASAANYLCRhgwdLNAFLGE 82

                         90
                 ....*....|....
gi 692318524 186 DWRLATMAYNAGEY 199
Cdd:cd13399   83 DNFLALAAYNAGPG 96
MLTF-like cd13403
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily ...
 124-208 7.80e-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: 51.38  E-value: 7.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318524 124 ESGYRPNARNGSGPTGLWQFIATTARnhrvpmANGYDGRLSAVDSTQAAVRYLKTLHGMFGGD------WRLATMAYNAG 197
Cdd:cd13403   22 ESRFNPNARSPAGARGLMQLMPSTAR------ELGVNDRLDPEQNIHAGAKYLRYLRDRFPPDidepdrLKFALAAYNAG 95

                         90
                 ....*....|.
gi 692318524 198 EYRVLQSMRKA 208
Cdd:cd13403   96 PGHVRDARRLA 106
Lyz-like cd00442
lysozyme-like domains; This family contains several members, including soluble lytic ...
 118-175 1.11e-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: 42.78  E-value: 1.11e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318524 118 ALIPFVESGYRPNAR--NGSGPTGLWQFIATTARNHRVpmaNGYDGRLSAVDSTQAAVRY 175
Cdd:cd00442    3 AAIIGQESGGNKPANagSGSGAAGLFQFMPGTWKAYGK---NSSSDLNDPEASIEAAAKY 59
PRK11619 PRK11619
lytic murein transglycosylase; Provisional
 124-201 1.33e-05

lytic murein transglycosylase; Provisional


Pssm-ID: 183236 [Multi-domain]  Cd Length: 644  Bit Score: 47.36  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318524 124 ESGYRPNARNGSGPTGLWQFIATTARnHRVPMAN--GYDGR---LSAVDSTQAAVRYLKTLHGMFGGDWRLATMAYNAGE 198
Cdd:PRK11619 504 ESAWNPKARSPVGASGLMQIMPGTAT-HTVKMFSipGYSSSsqlLDPETNINIGTSYLEYVYQQFGNNRILASAAYNAGP 582


                 ...
gi 692318524 199 YRV 201
Cdd:PRK11619 583 GRV 585
PHA00368 PHA00368
internal virion protein D
 122-200 2.36e-05

internal virion protein D


Pssm-ID: 222785 [Multi-domain]  Cd Length: 1315  Bit Score: 46.70  E-value: 2.36e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 692318524  122 FVESGYRPNARNGSGPTGLWQFIATTARNhrVPMANGYDGRLSAVDSTQAAVRYLKTLHGMFGGDWRLATMAYNAGEYR 200
Cdd:PHA00368   34 WDESRFNPTAKSPTGPKGLMQFTKATAKA--LGLIVDDDDRLDPELAIDAGARYLADLVGKYDGDELKAALAYNQGEGR 110
LT_TF-like cd13402
lytic transglycosylase-like domain of tail fiber-like proteins and similar domains; These tail ...
 124-177 1.99e-04

lytic transglycosylase-like domain of tail fiber-like proteins and similar domains; These tail fiber-like proteins are multi-domain proteins that include a lytic transglycosylase (LT) domain. Members of the LT family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, and the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL). 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: 381605 [Multi-domain]  Cd Length: 117  Bit Score: 40.64  E-value: 1.99e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 692318524 124 ESGYRP--------NARNGSGPTGLWQFIATTARNHRVPmanGYDGRLSAVDSTQAAVRYLK 177
Cdd:cd13402   11 ESGGNPnainnwdsNAKAGHPSKGLMQVIPPTFAAYAPP---GHGNILNPLDNILAAINYAK 69
PRK13914 PRK13914
invasion associated endopeptidase;
298-388 2.00e-04

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 43.25  E-value: 2.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318524 298 RASGTTRVLAPvsaANATVTEAATTLVASTAPVatttptpQVAKTVAAIADRPRSRRHTVRDGESAWTIARRYGMPVKAL 377
Cdd:PRK13914 155 KKETTTQQAAP---AAETKTEVKQTTQATTPAP-------KVAETKETPVVDQNATTHAVKSGDTIWALSVKYGVSVQDI 224

                         90
                 ....*....|.
gi 692318524 378 LSLNGLSGSSV 388
Cdd:PRK13914 225 MSWNNLSSSSI 235
SLT COG3953
SLT domain protein [Mobilome: prophages, transposons];
124-193 7.17e-04

SLT domain protein [Mobilome: prophages, transposons];


Pssm-ID: 443153 [Multi-domain]  Cd Length: 325  Bit Score: 41.24  E-value: 7.17e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 692318524 124 ESGYRP--------NARNGSGPTGLWQFIATTARNHRVPmanGYDGRLSAVDSTQAAVRYLKTLHGMFGGDWRLATMA 193
Cdd:COG3953  243 ESGGNPnainlwdsNAAAGTPSKGLMQVIPPTFNAYKLP---GHGNIYNPVDNILAGINYAKSRYGSSDNVPGLASLG 317
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 252-397 8.76e-04

Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion transport and metabolism];


Pssm-ID: 441258 [Multi-domain]  Cd Length: 163  Bit Score: 39.60  E-value: 8.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318524 252 ASLDRTVPVLKDHTLPAGTSVQQWAAQRALDPARIARLNPALAAGNRASGTTRVLAPVSAANATVTEAATTLVASTAPVA 331
Cdd:COG1652    8 AALAALLPAVSAAAATVLALAAAAALAVVAGLGAAVGAGGALAAALPLAAGLAAAVAAAAAAAVLIAPVAVMRAGAAAKL 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 692318524 332 TTTPTPQVAKTVAAIADRP-RSRRHTVRDGESAWTIARR-YGMPVK--ALLSLN--GLSGSSVLKPGAVLRV 397
Cdd:COG1652   88 SPAVTVAEEAAAPSAELAPdAPKTYTVKPGDTLWGIAKRfYGDPARwpEIAEANrdQIKNPDLIYPGQVLRI 159
 
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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