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Conserved domains on  [gi|695631428|ref|WP_032610469|]
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MULTISPECIES: lytic transglycosylase domain-containing protein [Enterobacteriaceae]

Protein Classification

lytic transglycosylase domain-containing protein( domain architecture ID 12989917)

lytic transglycosylase domain-containing protein similar to phage exolysin that catalyzes the cleavage of the host peptidoglycans during virus entry

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LT_IagB-like cd13400
Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like ...
 30-140 8.74e-35

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: 117.63  E-value: 8.74e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695631428  30 FGIDAELVFTLFDNEGGKVGTF-SRNKNGTYDIGPMQINSSNLPEIRGHFpsVTWRVLAYDACASFWVGTWWLYRKIvDR 108
Cdd:cd13400    1 YGVPPRLLRAIAKVESGFNPNAiNRNKNGSYDIGLMQINSIWLPELARYG--ITREELLNDPCTNIYVGAWILARNI-KR 77

                         90       100       110
                 ....*....|....*....|....*....|..
gi 695631428 109 NGNVFEGIADYNSKTPKVRARYIFNFMVKYNR 140
Cdd:cd13400   78 YGNTWKAVGAYNSGTPKKNDKYARKVYRIYRR 109
 
Name Accession Description Interval E-value
LT_IagB-like cd13400
Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like ...
 30-140 8.74e-35

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: 117.63  E-value: 8.74e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695631428  30 FGIDAELVFTLFDNEGGKVGTF-SRNKNGTYDIGPMQINSSNLPEIRGHFpsVTWRVLAYDACASFWVGTWWLYRKIvDR 108
Cdd:cd13400    1 YGVPPRLLRAIAKVESGFNPNAiNRNKNGSYDIGLMQINSIWLPELARYG--ITREELLNDPCTNIYVGAWILARNI-KR 77

                         90       100       110
                 ....*....|....*....|....*....|..
gi 695631428 109 NGNVFEGIADYNSKTPKVRARYIFNFMVKYNR 140
Cdd:cd13400   78 YGNTWKAVGAYNSGTPKKNDKYARKVYRIYRR 109
PRK13888 PRK13888
conjugal transfer protein TrbN; Provisional
 34-137 1.37e-17

conjugal transfer protein TrbN; Provisional


Pssm-ID: 237545  Cd Length: 206  Bit Score: 76.40  E-value: 1.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695631428  34 AELVFTLFDNEGGKVGTFSRNKNGTYDIGPMQINSSNLPEIRGHfpSVTWRVLAYDACASFWVGTWWLYRKIVDRNGNVF 113
Cdd:PRK13888  29 ANIVLAVAEKEGGKPGQWVRNTNGTHDVGPMQFNTAYLGDLARY--GITANDVAAAGCYSFDLAAWRLRMHIRNDKGDLW 106

                         90       100
                 ....*....|....*....|....
gi 695631428 114 EGIADYNSKTPKVRARYIFNFMVK 137
Cdd:PRK13888 107 TKAANYHSRTPQYNAVYRADLMRK 130
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 30-127 5.83e-03

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


Pssm-ID: 396169 [Multi-domain]  Cd Length: 114  Bit Score: 34.98  E-value: 5.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695631428   30 FGIDAELVFTLFDNEGGkvgtFSRN-KNGTYDIGPMQINSSNLPEIRghFPSVTWRVLAYDACASFWVGTWWLYRKIVDR 108
Cdd:pfam01464   8 YGVDPSLLLAIAQQESG----FNPKaVSKSGAVGLMQIMPSTAKRLG--LRVNPGVDDLFDPEKNIKAGTKYLKELYKQY 81

                          90
                  ....*....|....*....
gi 695631428  109 NGNVFEGIADYNSKTPKVR 127
Cdd:pfam01464  82 GGDLWLALAAYNAGPGRVR 100
 
Name Accession Description Interval E-value
LT_IagB-like cd13400
Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like ...
 30-140 8.74e-35

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: 117.63  E-value: 8.74e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695631428  30 FGIDAELVFTLFDNEGGKVGTF-SRNKNGTYDIGPMQINSSNLPEIRGHFpsVTWRVLAYDACASFWVGTWWLYRKIvDR 108
Cdd:cd13400    1 YGVPPRLLRAIAKVESGFNPNAiNRNKNGSYDIGLMQINSIWLPELARYG--ITREELLNDPCTNIYVGAWILARNI-KR 77

                         90       100       110
                 ....*....|....*....|....*....|..
gi 695631428 109 NGNVFEGIADYNSKTPKVRARYIFNFMVKYNR 140
Cdd:cd13400   78 YGNTWKAVGAYNSGTPKKNDKYARKVYRIYRR 109
PRK13888 PRK13888
conjugal transfer protein TrbN; Provisional
 34-137 1.37e-17

conjugal transfer protein TrbN; Provisional


Pssm-ID: 237545  Cd Length: 206  Bit Score: 76.40  E-value: 1.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695631428  34 AELVFTLFDNEGGKVGTFSRNKNGTYDIGPMQINSSNLPEIRGHfpSVTWRVLAYDACASFWVGTWWLYRKIVDRNGNVF 113
Cdd:PRK13888  29 ANIVLAVAEKEGGKPGQWVRNTNGTHDVGPMQFNTAYLGDLARY--GITANDVAAAGCYSFDLAAWRLRMHIRNDKGDLW 106

                         90       100
                 ....*....|....*....|....
gi 695631428 114 EGIADYNSKTPKVRARYIFNFMVK 137
Cdd:PRK13888 107 TKAANYHSRTPQYNAVYRADLMRK 130
PRK15328 PRK15328
type III secretion system invasion protein IagB;
19-144 2.71e-11

type III secretion system invasion protein IagB;


Pssm-ID: 185228 [Multi-domain]  Cd Length: 160  Bit Score: 58.72  E-value: 2.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695631428  19 YTQCITDASRFFGIDAELVFTLFDNEGG-KVGTFSRNKNGTYDIGPMQINSSNLPEIRGHfpSVTWRVLAYDACASFWVG 97
Cdd:PRK15328  18 WADCWLQAEKMFNIESELLYAIAQQESAmKPGAIGHNRDGSTDLGLMQINSFHMKRLKKM--GISEKQLLQDPCISVIVG 95

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 695631428  98 TWWLyRKIVDRNGNVFEGIADYNSKTPK----VRARYIFNFMVKYnRRIQG 144
Cdd:PRK15328  96 ASIL-SDMMKIYGYSWEAVGAYNAGTSPkrsdIRKRYAKKIWENY-RKLKG 144
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 30-127 5.83e-03

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


Pssm-ID: 396169 [Multi-domain]  Cd Length: 114  Bit Score: 34.98  E-value: 5.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695631428   30 FGIDAELVFTLFDNEGGkvgtFSRN-KNGTYDIGPMQINSSNLPEIRghFPSVTWRVLAYDACASFWVGTWWLYRKIVDR 108
Cdd:pfam01464   8 YGVDPSLLLAIAQQESG----FNPKaVSKSGAVGLMQIMPSTAKRLG--LRVNPGVDDLFDPEKNIKAGTKYLKELYKQY 81

                          90
                  ....*....|....*....
gi 695631428  109 NGNVFEGIADYNSKTPKVR 127
Cdd:pfam01464  82 GGDLWLALAAYNAGPGRVR 100
 
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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