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Conserved domains on  [gi|1905965604|ref|WP_188745051|]
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lytic transglycosylase domain-containing protein [Roseovarius pacificus]

Protein Classification

lytic transglycosylase domain-containing protein( domain architecture ID 10083321)

lytic transglycosylase domain-containing protein similar to exolysins that catalyze the cleavage of the host peptidoglycans during virus entry

EC:  4.2.2.n1
Gene Ontology:  GO:0016798
PubMed:  8203016|8692991|7712284

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
 156-263 1.14e-37

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: 131.57  E-value: 1.14e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905965604 156 RALLQALIWQESRFTIGARSPVGAFGLTQIMPGTASDLG-INPEYYDSPYLQVHGGARYLATQLNTFDGNIINALAAYNA 234
Cdd:cd00254     1 PALVLAVIRVESGFNPRAVSPAGARGLMQLMPGTARDLGrRGVDDLFDPEENIRAGARYLRELLDRFGGDLELALAAYNA 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1905965604 235 GPGRVFEYGG--VPPFRETQHYVQVIPERYN 263
Cdd:cd00254    81 GPGAVDRWGGgeVPPYKETRNYVQRVLAYYQ 111
 
Name Accession Description Interval E-value
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
 156-263 1.14e-37

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: 131.57  E-value: 1.14e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905965604 156 RALLQALIWQESRFTIGARSPVGAFGLTQIMPGTASDLG-INPEYYDSPYLQVHGGARYLATQLNTFDGNIINALAAYNA 234
Cdd:cd00254     1 PALVLAVIRVESGFNPRAVSPAGARGLMQLMPGTARDLGrRGVDDLFDPEENIRAGARYLRELLDRFGGDLELALAAYNA 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1905965604 235 GPGRVFEYGG--VPPFRETQHYVQVIPERYN 263
Cdd:cd00254    81 GPGAVDRWGGgeVPPYKETRNYVQRVLAYYQ 111
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 147-265 2.65e-32

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: 121.64  E-value: 2.65e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905965604 147 RAGLSPvqwrALLQALIWQESRFTIGARSPVGAFGLTQIMPGTASDLGINPEYYDS------PYLQVHGGARYLATQLNT 220
Cdd:COG0741   113 KYGVDP----ALVLALIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKLGLGPSpddlfdPETNIRAGAAYLRELLDR 188

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1905965604 221 FDGNIINALAAYNAGPGRV--------FEYGGVPPFRETQHYVQVIPERYNLY 265
Cdd:COG0741   189 FDGDLVLALAAYNAGPGRVrrwlrrngDRDGEIIPYAETRNYVKKVLANYAIY 241
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 158-254 1.01e-22

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: 91.98  E-value: 1.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905965604 158 LLQALIWQESRFTIGARSPVGAFGLTQIMPGTASDLG--INPEYYDS--PYLQVHGGARYLATQLNTFDGNIINALAAYN 233
Cdd:pfam01464  14 LLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGlrVNPGVDDLfdPEKNIKAGTKYLKELYKQYGGDLWLALAAYN 93

                          90       100
                  ....*....|....*....|.
gi 1905965604 234 AGPGRVFEYGGVPPFRETQHY 254
Cdd:pfam01464  94 AGPGRVRKWIKNAGAKDKKLL 114
PRK11619 PRK11619
lytic murein transglycosylase; Provisional
 165-256 1.00e-13

lytic murein transglycosylase; Provisional


Pssm-ID: 183236 [Multi-domain]  Cd Length: 644  Bit Score: 72.40  E-value: 1.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905965604 165 QESRFTIGARSPVGAFGLTQIMPGTASD----LGInPEYYDS-----PYLQVHGGARYLATQLNTFDGNIINALAAYNAG 235
Cdd:PRK11619  503 QESAWNPKARSPVGASGLMQIMPGTATHtvkmFSI-PGYSSSsqlldPETNINIGTSYLEYVYQQFGNNRILASAAYNAG 581

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1905965604 236 PGRVFEYGGVP-------------PFRETQHYVQ 256
Cdd:PRK11619  582 PGRVRTWLGNSagridavafvesiPFSETRGYVK 615
 
Name Accession Description Interval E-value
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
 156-263 1.14e-37

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: 131.57  E-value: 1.14e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905965604 156 RALLQALIWQESRFTIGARSPVGAFGLTQIMPGTASDLG-INPEYYDSPYLQVHGGARYLATQLNTFDGNIINALAAYNA 234
Cdd:cd00254     1 PALVLAVIRVESGFNPRAVSPAGARGLMQLMPGTARDLGrRGVDDLFDPEENIRAGARYLRELLDRFGGDLELALAAYNA 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1905965604 235 GPGRVFEYGG--VPPFRETQHYVQVIPERYN 263
Cdd:cd00254    81 GPGAVDRWGGgeVPPYKETRNYVQRVLAYYQ 111
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 147-265 2.65e-32

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: 121.64  E-value: 2.65e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905965604 147 RAGLSPvqwrALLQALIWQESRFTIGARSPVGAFGLTQIMPGTASDLGINPEYYDS------PYLQVHGGARYLATQLNT 220
Cdd:COG0741   113 KYGVDP----ALVLALIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKLGLGPSpddlfdPETNIRAGAAYLRELLDR 188

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1905965604 221 FDGNIINALAAYNAGPGRV--------FEYGGVPPFRETQHYVQVIPERYNLY 265
Cdd:COG0741   189 FDGDLVLALAAYNAGPGRVrrwlrrngDRDGEIIPYAETRNYVKKVLANYAIY 241
Slt70-like cd13401
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ...
 147-268 5.64e-30

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: 112.57  E-value: 5.64e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905965604 147 RAGLSPvqwrALLQALIWQESRFTIGARSPVGAFGLTQIMPGTASDLG--INPEYYDS-----PYLQVHGGARYLATQLN 219
Cdd:cd13401    16 KNGLDP----ALVYAIIRQESAFDPDAVSPAGALGLMQLMPATAKDVAkkLGLPYYSPrdlfdPEYNIRLGSAYLAELLD 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1905965604 220 TFDGNIINALAAYNAGPGRVF----EYGGVP--------PFRETQHYVQVIPERYNLYLSR 268
Cdd:cd13401    92 RFDGNPVLALAAYNAGPGRVRrwlkRRGDLDpdlwietiPFSETRNYVKRVLENYVVYRAL 152
LT_Slt70-like cd16896
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ...
 129-256 1.96e-24

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: 97.58  E-value: 1.96e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905965604 129 EQLIIRVAQETsgfagvgraGLSPvqwrALLQALIWQESRFTIGARSPVGAFGLTQIMPGTA-------SDLGINPEYYD 201
Cdd:cd16896     5 REYIEKYAKEY---------GVDP----LLVAAVIKVESNFNPNAVSSKGAIGLMQIMPETAewiaeklGLEDFSEDDLY 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1905965604 202 SPYLQVHGGARYLATQLNTFDGNIINALAAYNAGPGRV--------FEYGGVP----PFRETQHYVQ 256
Cdd:cd16896    72 DPETNIRLGTWYLSYLLKEFDGNLVLALAAYNAGPGNVdkwlkdggWSGDGKTldqiPFPETRHYVK 138
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 158-254 1.01e-22

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: 91.98  E-value: 1.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905965604 158 LLQALIWQESRFTIGARSPVGAFGLTQIMPGTASDLG--INPEYYDS--PYLQVHGGARYLATQLNTFDGNIINALAAYN 233
Cdd:pfam01464  14 LLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGlrVNPGVDDLfdPEKNIKAGTKYLKELYKQYGGDLWLALAAYN 93

                          90       100
                  ....*....|....*....|.
gi 1905965604 234 AGPGRVFEYGGVPPFRETQHY 254
Cdd:pfam01464  94 AGPGRVRKWIKNAGAKDKKLL 114
MLTF-like cd13403
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily ...
 155-239 1.39e-22

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: 92.98  E-value: 1.39e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905965604 155 WRaLLQALIWQESRFTIGARSPVGAFGLTQIMPGTASDLGINPEYydSPYLQVHGGARYLAtQLNTFDGNIIN------- 227
Cdd:cd13403    12 WR-LLAAQAYQESRFNPNARSPAGARGLMQLMPSTARELGVNDRL--DPEQNIHAGAKYLR-YLRDRFPPDIDepdrlkf 87

                          90
                  ....*....|..
gi 1905965604 228 ALAAYNAGPGRV 239
Cdd:cd13403    88 ALAAYNAGPGHV 99
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
 155-265 1.13e-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: 95.90  E-value: 1.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905965604 155 WRaLLQALIWQESRFTIGARSPVGAFGLTQIMPGTASDLGINpEYYDsPYLQVHGGARYLATQLNTFDGNIIN------A 228
Cdd:COG4623   279 WR-LLAALAYQESHWNPRARSPTGARGLMQLMPATAKELGVD-DRLD-PEQSIRAGAKYLRWLYDRFPEAIDEpdrwwfA 355

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1905965604 229 LAAYNAGPGRVF-------EYGGVPPF-------------------RETQHYVQVIPERYNLY 265
Cdd:COG4623   356 LAAYNAGPGHVQdarrlakKQGLDPDRwfdveksqpkyydtgyargRETVNYVPNIRAYYDIY 418
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
 159-255 9.18e-16

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: 73.32  E-value: 9.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905965604 159 LQALIWQESRFTIGARSPVGAFGLTQIMPGTASDLGI-NPEYYD---SPYLQVHGGARYLAtQLNTFDGNIINALAAYNA 234
Cdd:cd16894    10 LKYLALVESGFNPDAVSSAGAAGLWQFMPATAREYGLrVDSWVDerrDPEKSTRAAARYLK-DLYKRFGDWLLALAAYNA 88

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1905965604 235 GPGRV--------------FEYGGVPpfRETQHYV 255
Cdd:cd16894    89 GEGRVrraikragtdkwedYYRLYLP--AETRRYV 121
PRK11619 PRK11619
lytic murein transglycosylase; Provisional
 165-256 1.00e-13

lytic murein transglycosylase; Provisional


Pssm-ID: 183236 [Multi-domain]  Cd Length: 644  Bit Score: 72.40  E-value: 1.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905965604 165 QESRFTIGARSPVGAFGLTQIMPGTASD----LGInPEYYDS-----PYLQVHGGARYLATQLNTFDGNIINALAAYNAG 235
Cdd:PRK11619  503 QESAWNPKARSPVGASGLMQIMPGTATHtvkmFSI-PGYSSSsqlldPETNINIGTSYLEYVYQQFGNNRILASAAYNAG 581

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1905965604 236 PGRVFEYGGVP-------------PFRETQHYVQ 256
Cdd:PRK11619  582 PGRVRTWLGNSagridavafvesiPFSETRGYVK 615
Slt35-like cd13399
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ...
 149-237 1.04e-11

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: 61.17  E-value: 1.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905965604 149 GLSPvqwrALLQALIWQESRF-TIGARSPVGAFGLTQIMPGTASDLGI-----------NPE---YYDSPYLQVHGGary 213
Cdd:cd13399     2 GVPP----GILAAILGVESGFgPNAGGSPAGAQGIAQFMPSTWKAYGVdgngdgkadpfNPEdaiASAANYLCRHGW--- 74

                          90       100
                  ....*....|....*....|....*
gi 1905965604 214 latQLNTFDGNII-NALAAYNAGPG 237
Cdd:cd13399    75 ---DLNAFLGEDNfLALAAYNAGPG 96
PHA00368 PHA00368
internal virion protein D
 158-238 1.82e-08

internal virion protein D


Pssm-ID: 222785 [Multi-domain]  Cd Length: 1315  Bit Score: 56.33  E-value: 1.82e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905965604  158 LLQALIWQESRFTIGARSPVGAFGLTQIMPGTASDLG--INPEYYDSPYLQVHGGARYLATQLNTFDGNIINALAAYNAG 235
Cdd:PHA00368    28 LLRKVGWDESRFNPTAKSPTGPKGLMQFTKATAKALGliVDDDDRLDPELAIDAGARYLADLVGKYDGDELKAALAYNQG 107


                   ...
gi 1905965604  236 PGR 238
Cdd:PHA00368   108 EGR 110
LT_MltC_MltE cd16893
membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and ...
 146-239 2.82e-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: 52.56  E-value: 2.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905965604 146 GRAGLSPvqwrALLQALIWQESRFTIGARSPVGAFGLTQIMPGTA----------SDLGINPEYYDSPYLQVHGGARYLA 215
Cdd:cd16893     8 KKYGVDP----ALILAIIETESSFNPYAVSHSPAYGLMQIVPSTAgrdvyrllggKGGLPSKSYLFDPENNIDIGTAYLH 83

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1905965604 216 TQLNTFDGNIIN-------ALAAYNAGPGRV 239
Cdd:cd16893    84 ILQNRYLKGIKNpksreycAIAAYNGGAGNV 114
PRK10859 PRK10859
membrane-bound lytic murein transglycosylase MltF;
155-239 3.20e-08

membrane-bound lytic murein transglycosylase MltF;


Pssm-ID: 236778 [Multi-domain]  Cd Length: 482  Bit Score: 55.27  E-value: 3.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905965604 155 WRaLLQALIWQESRFTIGARSPVGAFGLTQIMPGTASDLGI----NPEyydspylQ-VHGGARYLATQLNTFDGNI---- 225
Cdd:PRK10859  303 WR-LLAAIAYQESHWNPQATSPTGVRGLMMLTRNTAQSMGVtdrlDPE-------QsIRGGARYLQDLMERLPESIpepe 374

                          90
                  ....*....|....*.
gi 1905965604 226 -IN-ALAAYNAGPGRV 239
Cdd:PRK10859  375 rIWfALAAYNIGYGHM 390
PHA00658 PHA00658
putative lysin
 175-308 9.18e-07

putative lysin


Pssm-ID: 106967 [Multi-domain]  Cd Length: 720  Bit Score: 50.98  E-value: 9.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905965604 175 SPVGAFGLTQIMPGTASD------LGINPEYY--DSPYLQVHGGArYLATQLNTFDGNIINALAAYNAGPGRVFE----- 241
Cdd:PHA00658  326 SPKGAVGIAQVMPDTAPEaaklagLPWDENRYrnDAAYNRALGMA-YFQKQLRDFGGDLPKAYAAYNAGPGALQSalkda 404

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1905965604 242 ----YGGVPPfRETQHYVQVIPERYNLYLSR-----IGGIEALGTIDPALLANAN-LSMTGHGAAFYGNNSPAAIRQ 308
Cdd:PHA00658  405 kdgnWLALLP-KETQDYVVKNMQAYNAGQGRparptLADIEAQLQNDPRLAGNPErLKIARVEAERQFNMQTAALKQ 480
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 166-239 7.65e-05

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 44.73  E-value: 7.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905965604 166 ESRFTIGARSPVGAFGLTQIMPGTASDLGI-NPEYYDspylqvhgGARYLAT----------QLNT-FDGNIINALAAYN 233
Cdd:PRK10783  128 ESAFDPHATSGANAAGIWQIIPSTGRNYGLkQTRWYD--------ARRDVVAsttaaldmmqRLNKmFDGDWLLTVAAYN 199


                  ....*.
gi 1905965604 234 AGPGRV 239
Cdd:PRK10783  200 SGEGRV 205
PRK13722 PRK13722
lytic transglycosylase; Provisional
 158-235 1.09e-04

lytic transglycosylase; Provisional


Pssm-ID: 184274 [Multi-domain]  Cd Length: 169  Bit Score: 42.38  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905965604 158 LLQALIWQESRFTIGA--RSPVGAF--GLTQIMPGTASDL---GINPEYYDS-PYLQVHGGARYLATQLNTFdGNIINAL 229
Cdd:PRK13722   36 LLRAISWKESRYRVNAigINPVTGYgsGLMQVDSQHFNELaryGIKPEHLTTdPCMNIYTGAYYLAIAFKKW-GVSWEAV 114


                  ....*.
gi 1905965604 230 AAYNAG 235
Cdd:PRK13722  115 GAYNAG 120
Lyz-like cd00442
lysozyme-like domains; This family contains several members, including soluble lytic ...
 159-198 1.82e-04

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: 39.32  E-value: 1.82e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1905965604 159 LQALIWQESRFTIGAR--SPVGAFGLTQIMPGTASDLGINPE 198
Cdd:cd00442     2 LAAIIGQESGGNKPANagSGSGAAGLFQFMPGTWKAYGKNSS 43
LT_IagB-like cd13400
Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like ...
 158-236 1.24e-03

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: 38.28  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905965604 158 LLQALIWQESRFTIGA--RSPVGAF--GLTQI----------MPGTASDLGINPEYydspylQVHGGARYLATQLNTFdG 223
Cdd:cd13400     7 LLRAIAKVESGFNPNAinRNKNGSYdiGLMQInsiwlpelarYGITREELLNDPCT------NIYVGAWILARNIKRY-G 79

                          90
                  ....*....|...
gi 1905965604 224 NIINALAAYNAGP 236
Cdd:cd13400    80 NTWKAVGAYNSGT 92
 
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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