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Conserved domains on  [gi|2705749730|ref|WP_338044642|]
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lytic transglycosylase domain-containing protein [Moraxella lincolnii]

Protein Classification

lytic transglycosylase domain-containing protein( domain architecture ID 11432856)

lytic transglycosylase domain-containing protein similar to Bacillus subtilis bifunctional muramidase/lytic transglycosylase CwlQ that cleaves the beta-1,4-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine (MurNAc-GlcNAc) in peptidoglycan, producing both N-acetylmuramic acid and 1,6-anhydro-N-acetylmuramic acid

Gene Ontology:  GO:0016787|GO:0000270|GO:0008933|GO:0071555
PubMed:  8765311|7479697|9723170

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 63-218 1.27e-56

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: 182.12  E-value: 1.27e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2705749730  63 DSQVRNLTNNTSASHYGQSVASRSANRNAYDALIRSSAARHGVDPALMKAMMHTESAFNPNARSPVGAQGLMQLMPATAR 142
Cdd:COG0741    74 DALAAFAAIAALAAELLALAALLLRRPLPYLPLIEEAAKKYGVDPALVLALIRQESAFNPNAVSPAGARGLMQLMPATAR 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2705749730 143 RF--------SVNNTWSPAENIEGAAKYIAWLMRRFNNNVEFAIAGYNAGEGNVDKY--------GGIPPFRETRNYVKS 206
Cdd:COG0741   154 RLglklglgpSPDDLFDPETNIRAGAAYLRELLDRFDGDLVLALAAYNAGPGRVRRWlrrngdrdGEIIPYAETRNYVKK 233

                         170
                  ....*....|..
gi 2705749730 207 VLsRYHGLYKHD 218
Cdd:COG0741   234 VL-ANYAIYRAG 244
 
Name Accession Description Interval E-value
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 63-218 1.27e-56

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: 182.12  E-value: 1.27e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2705749730  63 DSQVRNLTNNTSASHYGQSVASRSANRNAYDALIRSSAARHGVDPALMKAMMHTESAFNPNARSPVGAQGLMQLMPATAR 142
Cdd:COG0741    74 DALAAFAAIAALAAELLALAALLLRRPLPYLPLIEEAAKKYGVDPALVLALIRQESAFNPNAVSPAGARGLMQLMPATAR 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2705749730 143 RF--------SVNNTWSPAENIEGAAKYIAWLMRRFNNNVEFAIAGYNAGEGNVDKY--------GGIPPFRETRNYVKS 206
Cdd:COG0741   154 RLglklglgpSPDDLFDPETNIRAGAAYLRELLDRFDGDLVLALAAYNAGPGRVRRWlrrngdrdGEIIPYAETRNYVKK 233

                         170
                  ....*....|..
gi 2705749730 207 VLsRYHGLYKHD 218
Cdd:COG0741   234 VL-ANYAIYRAG 244
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
 107-211 3.47e-49

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: 158.53  E-value: 3.47e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2705749730 107 PALMKAMMHTESAFNPNARSPVGAQGLMQLMPATARRF---SVNNTWSPAENIEGAAKYIAWLMRRFNNNVEFAIAGYNA 183
Cdd:cd00254     1 PALVLAVIRVESGFNPRAVSPAGARGLMQLMPGTARDLgrrGVDDLFDPEENIRAGARYLRELLDRFGGDLELALAAYNA 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 2705749730 184 GEGNVDKYGG--IPPFRETRNYVKSVLSRY 211
Cdd:cd00254    81 GPGAVDRWGGgeVPPYKETRNYVQRVLAYY 110
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 96-203 6.13e-33

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: 117.02  E-value: 6.13e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2705749730  96 IRSSAARHGVDPALMKAMMHTESAFNPNARSPVGAQGLMQLMPATARRF------SVNNTWSPAENIEGAAKYIAWLMRR 169
Cdd:pfam01464   1 IIKAAQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLglrvnpGVDDLFDPEKNIKAGTKYLKELYKQ 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2705749730 170 FNNNVEFAIAGYNAGEGNVDKYGGIPPFRETRNY 203
Cdd:pfam01464  81 YGGDLWLALAAYNAGPGRVRKWIKNAGAKDKKLL 114
PRK11619 PRK11619
lytic murein transglycosylase; Provisional
 91-217 2.79e-25

lytic murein transglycosylase; Provisional


Pssm-ID: 183236 [Multi-domain]  Cd Length: 644  Bit Score: 105.14  E-value: 2.79e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2705749730  91 AYDALIRSSAARHGVDPALMKAMMHTESAFNPNARSPVGAQGLMQLMPATA----RRFSVNNTWS------PAENIEGAA 160
Cdd:PRK11619  478 AWNDEFRRYTSGKGIPQSYAMAIARQESAWNPKARSPVGASGLMQIMPGTAthtvKMFSIPGYSSssqlldPETNINIGT 557

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2705749730 161 KYIAWLMRRFNNNVEFAIAGYNAGEGNVDKYGG--------------IpPFRETRNYVKSVLSrYHGLYKH 217
Cdd:PRK11619  558 SYLEYVYQQFGNNRILASAAYNAGPGRVRTWLGnsagridavafvesI-PFSETRGYVKNVLA-YDAYYRY 626
 
Name Accession Description Interval E-value
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 63-218 1.27e-56

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: 182.12  E-value: 1.27e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2705749730  63 DSQVRNLTNNTSASHYGQSVASRSANRNAYDALIRSSAARHGVDPALMKAMMHTESAFNPNARSPVGAQGLMQLMPATAR 142
Cdd:COG0741    74 DALAAFAAIAALAAELLALAALLLRRPLPYLPLIEEAAKKYGVDPALVLALIRQESAFNPNAVSPAGARGLMQLMPATAR 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2705749730 143 RF--------SVNNTWSPAENIEGAAKYIAWLMRRFNNNVEFAIAGYNAGEGNVDKY--------GGIPPFRETRNYVKS 206
Cdd:COG0741   154 RLglklglgpSPDDLFDPETNIRAGAAYLRELLDRFDGDLVLALAAYNAGPGRVRRWlrrngdrdGEIIPYAETRNYVKK 233

                         170
                  ....*....|..
gi 2705749730 207 VLsRYHGLYKHD 218
Cdd:COG0741   234 VL-ANYAIYRAG 244
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
 107-211 3.47e-49

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: 158.53  E-value: 3.47e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2705749730 107 PALMKAMMHTESAFNPNARSPVGAQGLMQLMPATARRF---SVNNTWSPAENIEGAAKYIAWLMRRFNNNVEFAIAGYNA 183
Cdd:cd00254     1 PALVLAVIRVESGFNPRAVSPAGARGLMQLMPGTARDLgrrGVDDLFDPEENIRAGARYLRELLDRFGGDLELALAAYNA 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 2705749730 184 GEGNVDKYGG--IPPFRETRNYVKSVLSRY 211
Cdd:cd00254    81 GPGAVDRWGGgeVPPYKETRNYVQRVLAYY 110
Slt70-like cd13401
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ...
 91-212 2.03e-48

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: 158.02  E-value: 2.03e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2705749730  91 AYDALIRSSAARHGVDPALMKAMMHTESAFNPNARSPVGAQGLMQLMPATAR---------RFSVNNTWSPAENIEGAAK 161
Cdd:cd13401     5 PYRDLVERAAKKNGLDPALVYAIIRQESAFDPDAVSPAGALGLMQLMPATAKdvakklglpYYSPRDLFDPEYNIRLGSA 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2705749730 162 YIAWLMRRFNNNVEFAIAGYNAGEGNVDK----YGGIP--------PFRETRNYVKSVLSRYH 212
Cdd:cd13401    85 YLAELLDRFDGNPVLALAAYNAGPGRVRRwlkrRGDLDpdlwietiPFSETRNYVKRVLENYV 147
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
 92-217 2.78e-44

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


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 155.22  E-value: 2.78e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2705749730  92 YDALIRSSAARHGVDPALMKAMMHTESAFNPNARSPVGAQGLMQLMPATARRFSVNNTWSPAENIEGAAKYIAWLMRRFN 171
Cdd:COG4623   264 YDPLFEKYAEEYGLDWRLLAALAYQESHWNPRARSPTGARGLMQLMPATAKELGVDDRLDPEQSIRAGAKYLRWLYDRFP 343

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2705749730 172 NNVE------FAIAGYNAGEGNVD-------KYGGIPPF-------------------RETRNYVKSVLSRYHGLYKH 217
Cdd:COG4623   344 EAIDepdrwwFALAAYNAGPGHVQdarrlakKQGLDPDRwfdveksqpkyydtgyargRETVNYVPNIRAYYDIYKRL 421
LT_Slt70-like cd16896
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ...
 92-211 6.85e-43

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: 143.42  E-value: 6.85e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2705749730  92 YDALIRSSAARHGVDPALMKAMMHTESAFNPNARSPVGAQGLMQLMPATAR---------RFSVNNTWSPAENIEGAAKY 162
Cdd:cd16896     4 YREYIEKYAKEYGVDPLLVAAVIKVESNFNPNAVSSKGAIGLMQIMPETAEwiaeklgleDFSEDDLYDPETNIRLGTWY 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2705749730 163 IAWLMRRFNNNVEFAIAGYNAGEGNVDKY---GGIP---------PFRETRNYVKSVLSRY 211
Cdd:cd16896    84 LSYLLKEFDGNLVLALAAYNAGPGNVDKWlkdGGWSgdgktldqiPFPETRHYVKKVLKNY 144
MLTF-like cd13403
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily ...
 96-211 2.30e-36

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: 127.27  E-value: 2.30e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2705749730  96 IRSSAARHGVDPALMKAMMHTESAFNPNARSPVGAQGLMQLMPATARRFSVNNTWSPAENIEGAAKYIAWLMRRFNNNVE 175
Cdd:cd13403     1 FKKYAEKYGFDWRLLAAQAYQESRFNPNARSPAGARGLMQLMPSTARELGVNDRLDPEQNIHAGAKYLRYLRDRFPPDID 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2705749730 176 ------FAIAGYNAGEGNV-------DKYGGIP---------------PF------------RETRNYVKSVLSRY 211
Cdd:cd13403    81 epdrlkFALAAYNAGPGHVrdarrlaKKYGLNPnvwfdnvevlpllksPYydpvvkygyargRETVNYVRNIRKYY 156
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 96-203 6.13e-33

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: 117.02  E-value: 6.13e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2705749730  96 IRSSAARHGVDPALMKAMMHTESAFNPNARSPVGAQGLMQLMPATARRF------SVNNTWSPAENIEGAAKYIAWLMRR 169
Cdd:pfam01464   1 IIKAAQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLglrvnpGVDDLFDPEKNIKAGTKYLKELYKQ 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2705749730 170 FNNNVEFAIAGYNAGEGNVDKYGGIPPFRETRNY 203
Cdd:pfam01464  81 YGGDLWLALAAYNAGPGRVRKWIKNAGAKDKKLL 114
PRK11619 PRK11619
lytic murein transglycosylase; Provisional
 91-217 2.79e-25

lytic murein transglycosylase; Provisional


Pssm-ID: 183236 [Multi-domain]  Cd Length: 644  Bit Score: 105.14  E-value: 2.79e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2705749730  91 AYDALIRSSAARHGVDPALMKAMMHTESAFNPNARSPVGAQGLMQLMPATA----RRFSVNNTWS------PAENIEGAA 160
Cdd:PRK11619  478 AWNDEFRRYTSGKGIPQSYAMAIARQESAWNPKARSPVGASGLMQIMPGTAthtvKMFSIPGYSSssqlldPETNINIGT 557

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2705749730 161 KYIAWLMRRFNNNVEFAIAGYNAGEGNVDKYGG--------------IpPFRETRNYVKSVLSrYHGLYKH 217
Cdd:PRK11619  558 SYLEYVYQQFGNNRILASAAYNAGPGRVRTWLGnsagridavafvesI-PFSETRGYVKNVLA-YDAYYRY 626
LT_MltC_MltE cd16893
membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and ...
 94-212 5.04e-25

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: 97.63  E-value: 5.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2705749730  94 ALIRSSAARHGVDPALMKAMMHTESAFNPNARSPVGAQGLMQLMPATA------------RRFSVNNTWSPAENIE-GAA 160
Cdd:cd16893     1 PIVEKYAKKYGVDPALILAIIETESSFNPYAVSHSPAYGLMQIVPSTAgrdvyrllggkgGLPSKSYLFDPENNIDiGTA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2705749730 161 kYIAWLMRRFNNNVE-------FAIAGYNAGEGNVDKYGG------IP------------------PFRETRNYVKSVLS 209
Cdd:cd16893    81 -YLHILQNRYLKGIKnpksreyCAIAAYNGGAGNVLRTFSsdrkkaISkinrlspdevyqhltkklPAAETRNYLKKVLK 159


                  ...
gi 2705749730 210 RYH 212
Cdd:cd16893   160 AKK 162
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
 101-208 1.45e-23

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: 92.97  E-value: 1.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2705749730 101 ARHGVdPALMKAMMHTESAFNPNARSPVGAQGLMQLMPATARRFSVNNTW------SPAENIEGAAKYIAWLMRRFnNNV 174
Cdd:cd16894     2 LKEGL-PEELKYLALVESGFNPDAVSSAGAAGLWQFMPATAREYGLRVDSwvderrDPEKSTRAAARYLKDLYKRF-GDW 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2705749730 175 EFAIAGYNAGEGNVDKY--------------GGIPpfRETRNYVKSVL 208
Cdd:cd16894    80 LLALAAYNAGEGRVRRAikragtdkwedyyrLYLP--AETRRYVPKFL 125
Slt35-like cd13399
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ...
 103-187 4.40e-16

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: 72.34  E-value: 4.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2705749730 103 HGVDPALMKAMMHTESAFNPNA-RSPVGAQGLMQLMPATARRFSV-------NNTWSPAENIEGAAKY---IAWLMRRFN 171
Cdd:cd13399     1 YGVPPGILAAILGVESGFGPNAgGSPAGAQGIAQFMPSTWKAYGVdgngdgkADPFNPEDAIASAANYlcrHGWDLNAFL 80

                          90
                  ....*....|....*..
gi 2705749730 172 -NNVEFAIAGYNAGEGN 187
Cdd:cd13399    81 gEDNFLALAAYNAGPGA 97
PRK10859 PRK10859
membrane-bound lytic murein transglycosylase MltF;
92-188 5.11e-16

membrane-bound lytic murein transglycosylase MltF;


Pssm-ID: 236778 [Multi-domain]  Cd Length: 482  Bit Score: 77.61  E-value: 5.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2705749730  92 YDALIRSSAarHGVDPALMKAMMHTESAFNPNARSPVGAQGLMQLMPATARRFSVNNTWSPAENIEGAAKYIAWLMRRFN 171
Cdd:PRK10859  290 YQPLFEKYA--GELDWRLLAAIAYQESHWNPQATSPTGVRGLMMLTRNTAQSMGVTDRLDPEQSIRGGARYLQDLMERLP 367

                          90       100
                  ....*....|....*....|...
gi 2705749730 172 NNVE------FAIAGYNAGEGNV 188
Cdd:PRK10859  368 ESIPeperiwFALAAYNIGYGHM 390
PHA00368 PHA00368
internal virion protein D
 90-209 2.49e-14

internal virion protein D


Pssm-ID: 222785 [Multi-domain]  Cd Length: 1315  Bit Score: 72.89  E-value: 2.49e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2705749730   90 NAYDALIRSSAARHGVDPALMKAMMHTESAFNPNARSPVGAQGLMQLMPATAR----RFSVNNTWSPAENIEGAAKYIAW 165
Cdd:PHA00368     9 SEYDGLFQKAADAHGVSYDLLRKVGWDESRFNPTAKSPTGPKGLMQFTKATAKalglIVDDDDRLDPELAIDAGARYLAD 88

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2705749730  166 LMRRFNNNVEFAIAGYNAGEG--------NVDKYGGIPPFRETRNYVKSVLS 209
Cdd:PHA00368    89 LVGKYDGDELKAALAYNQGEGrlgapqleAYDKGDFASISEEGRNYLRNLLD 140
mltC PRK11671
membrane-bound lytic murein transglycosylase MltC;
92-188 1.02e-13

membrane-bound lytic murein transglycosylase MltC;


Pssm-ID: 183271 [Multi-domain]  Cd Length: 359  Bit Score: 70.47  E-value: 1.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2705749730  92 YDALIRSSAARHGVDPALMKAMMHTESAFNPNARSPVGAQGLMQLMPATARR--FSVNNTW---------SPAENIEGAA 160
Cdd:PRK11671  192 YLPMVRKASRKYGVDESLILAIMQTESSFNPYAVSRSDALGLMQVVQHTAGKdvFRMKGKSgqpsrsylfDPANNIDTGT 271

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2705749730 161 KYIAWLMRRF----NNNV--EFA-IAGYNAGEGNV 188
Cdd:PRK11671  272 AYLAILQNVYlggiTNPTsrRYAvITAYNGGAGSV 306
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 117-209 3.92e-09

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 57.05  E-value: 3.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2705749730 117 ESAFNPNARSPVGAQGLMQLMPATARRFSV-NNTWSPAENIEGAAKYIAWLM-----RRFNNNVEFAIAGYNAGEGNV-- 188
Cdd:PRK10783  128 ESAFDPHATSGANAAGIWQIIPSTGRNYGLkQTRWYDARRDVVASTTAALDMmqrlnKMFDGDWLLTVAAYNSGEGRVmk 207

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2705749730 189 ----DKYGGIP--------PfRETRNYVKSVLS 209
Cdd:PRK10783  208 aikaNKAKGKPtdfwslslP-RETKIYVPKMLA 239
Lyz-like cd00442
lysozyme-like domains; This family contains several members, including soluble lytic ...
 112-162 8.23e-07

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: 45.48  E-value: 8.23e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2705749730 112 AMMHTESAFNPNAR--SPVGAQGLMQLMPATAR---RFSVNNTWSPAENIEGAAKY 162
Cdd:cd00442     4 AIIGQESGGNKPANagSGSGAAGLFQFMPGTWKaygKNSSSDLNDPEASIEAAAKY 59
emtA PRK15470
membrane-bound lytic murein transglycosylase EmtA;
104-166 3.43e-06

membrane-bound lytic murein transglycosylase EmtA;


Pssm-ID: 185367 [Multi-domain]  Cd Length: 203  Bit Score: 46.88  E-value: 3.43e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2705749730 104 GVDPALMKAMMHTESAFNPNARSPVGAQGLMQLMPATA-----RRF------SVNNTWSPAENIEGAAKYIAWL 166
Cdd:PRK15470   51 GVDPQLITAIIAIESGGNPNAVSKSNAIGLMQLKASTSgrdvyRRMgwsgepTTSELKNPERNISMGAAYLNIL 124
GEWL cd01021
Goose egg-white lysozyme; Eukaryotic goose-type or G-type lysozyme (goose egg-white lysozyme; ...
 64-210 1.26e-05

Goose egg-white lysozyme; Eukaryotic goose-type or G-type lysozyme (goose egg-white lysozyme; GEWL) catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc). Mammals have two lysozymes. This family corresponds to human and mouse lysozyme G-like protein 2.


Pssm-ID: 381601 [Multi-domain]  Cd Length: 174  Bit Score: 44.51  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2705749730  64 SQVRNLTNNTSASHygqSVASRSANR-NAYDALIRSSAARHGVDPALMKAMMHTES----AFNPNARSPVG-AQGLMQLm 137
Cdd:cd01021    11 KQDGLLYGGVAASE---KMAETDLNRlNKYKDCIKQVGKKLCIDPALIAAIISRESragaALDKNGWGDHGnGFGLMQV- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2705749730 138 patARRF-SVNNTWSPAENIEGAAK----YIAWLMRRFNN-----NVEFAIAGYNAGEGNVDKYGGIPPFRETRNYVKSV 207
Cdd:cd01021    87 ---DKRYhPPKGAWDSEEHIEQATGilidFIKTVQRKHPSwspeqQLKGGIAAYNAGVGNVQSYAGMDIGTTGNDYSNDV 163


                  ...
gi 2705749730 208 LSR 210
Cdd:cd01021   164 IAR 166
LT_IagB-like cd13400
Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like ...
 103-211 2.50e-05

Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like protein, similar to Escherichia coli invasion protein IagB. IagB is encoded within a pathogenicity island in Salmonella enterica and has been shown to degrade polymeric peptidoglycan. IagB-like invasion proteins are implicated in the invasion of eukaryotic host cells by bacteria. 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. Members of this family resemble the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda.


Pssm-ID: 381603 [Multi-domain]  Cd Length: 109  Bit Score: 42.52  E-value: 2.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2705749730 103 HGVDPALMKAMMHTESAFNPNA--RSPVGAQ--GLMQL----MPATARRFSVNN--TWSPAENIEGAAKYIAWLMRRFNN 172
Cdd:cd13400     1 YGVPPRLLRAIAKVESGFNPNAinRNKNGSYdiGLMQInsiwLPELARYGITREelLNDPCTNIYVGAWILARNIKRYGN 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2705749730 173 NVEfAIAGYNAgegnvdkygGIPPFRetRNYVKSVLSRY 211
Cdd:cd13400    81 TWK-AVGAYNS---------GTPKKN--DKYARKVYRIY 107
LT_TF-like cd13402
lytic transglycosylase-like domain of tail fiber-like proteins and similar domains; These tail ...
 107-165 5.17e-03

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: 36.02  E-value: 5.17e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2705749730 107 PALMKAMMHtESAFNP--------NARSPVGAQGLMQLMPATARRFSV---NNTWSPAENIEGAAKYIAW 165
Cdd:cd13402     2 NALLRQIQT-ESGGNPnainnwdsNAKAGHPSKGLMQVIPPTFAAYAPpghGNILNPLDNILAAINYAKA 70
 
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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