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Conserved domains on  [gi|2562478261|gb|WLP55399|]
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lytic transglycosylase domain-containing protein [Agrobacterium fabrum]

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 ...
40-170 5.92e-20

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: 80.27  E-value: 5.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2562478261  40 YGVPEGILYSVGLTETGRKGRldpnamniegkpvfaasteeamvtfeAAKRNGAKLIDLGCMQINHYFHGE----NFTSA 115
Cdd:cd13400     1 YGVPPRLLRAIAKVESGFNPN--------------------------AINRNKNGSYDIGLMQINSIWLPElaryGITRE 54
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2562478261 116 REMFDPRRNVEYAAMFLRNLHNRHETWTMAVARYHAGPNNDpaQKKYVCRVIANL 170
Cdd:cd13400    55 ELLNDPCTNIYVGAWILARNIKRYGNTWKAVGAYNSGTPKK--NDKYARKVYRIY 107
 
Name Accession Description Interval E-value
LT_IagB-like cd13400
Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like ...
40-170 5.92e-20

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: 80.27  E-value: 5.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2562478261  40 YGVPEGILYSVGLTETGRKGRldpnamniegkpvfaasteeamvtfeAAKRNGAKLIDLGCMQINHYFHGE----NFTSA 115
Cdd:cd13400     1 YGVPPRLLRAIAKVESGFNPN--------------------------AINRNKNGSYDIGLMQINSIWLPElaryGITRE 54
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2562478261 116 REMFDPRRNVEYAAMFLRNLHNRHETWTMAVARYHAGPNNDpaQKKYVCRVIANL 170
Cdd:cd13400    55 ELLNDPCTNIYVGAWILARNIKRYGNTWKAVGAYNSGTPKK--NDKYARKVYRIY 107
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
32-155 1.18e-07

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: 49.99  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2562478261  32 EIQSAARKYGVPEGILYSVGLTETGrkgrLDPNAMNiegkpvfaasteeamvtfeaakRNGAklidLGCMQI-----NHY 106
Cdd:COG0741   106 LIEEAAKKYGVDPALVLALIRQESA----FNPNAVS----------------------PAGA----RGLMQLmpataRRL 155
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2562478261 107 -FHGENFTSAREMFDPRRNVEYAAMFLRNLHNRHE-TWTMAVARYHAGPNN 155
Cdd:COG0741   156 gLKLGLGPSPDDLFDPETNIRAGAAYLRELLDRFDgDLVLALAAYNAGPGR 206
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
33-163 4.47e-07

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: 46.53  E-value: 4.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2562478261  33 IQSAARKYGVPEGILYSVGLTETGrkgrLDPNAMNiegkpvfaasteeamvtfeaakRNGAklidLGCMQINHyFHGENF 112
Cdd:pfam01464   1 IIKAAQKYGVDPSLLLAIAQQESG----FNPKAVS----------------------KSGA----VGLMQIMP-STAKRL 49
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2562478261 113 -----TSAREMFDPRRNVEYAAMFLRNLHNRH-ETWTMAVARYHAGPNNDPAQKKYV 163
Cdd:pfam01464  50 glrvnPGVDDLFDPEKNIKAGTKYLKELYKQYgGDLWLALAAYNAGPGRVRKWIKNA 106
 
Name Accession Description Interval E-value
LT_IagB-like cd13400
Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like ...
40-170 5.92e-20

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: 80.27  E-value: 5.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2562478261  40 YGVPEGILYSVGLTETGRKGRldpnamniegkpvfaasteeamvtfeAAKRNGAKLIDLGCMQINHYFHGE----NFTSA 115
Cdd:cd13400     1 YGVPPRLLRAIAKVESGFNPN--------------------------AINRNKNGSYDIGLMQINSIWLPElaryGITRE 54
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2562478261 116 REMFDPRRNVEYAAMFLRNLHNRHETWTMAVARYHAGPNNDpaQKKYVCRVIANL 170
Cdd:cd13400    55 ELLNDPCTNIYVGAWILARNIKRYGNTWKAVGAYNSGTPKK--NDKYARKVYRIY 107
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
32-155 1.18e-07

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: 49.99  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2562478261  32 EIQSAARKYGVPEGILYSVGLTETGrkgrLDPNAMNiegkpvfaasteeamvtfeaakRNGAklidLGCMQI-----NHY 106
Cdd:COG0741   106 LIEEAAKKYGVDPALVLALIRQESA----FNPNAVS----------------------PAGA----RGLMQLmpataRRL 155
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2562478261 107 -FHGENFTSAREMFDPRRNVEYAAMFLRNLHNRHE-TWTMAVARYHAGPNN 155
Cdd:COG0741   156 gLKLGLGPSPDDLFDPETNIRAGAAYLRELLDRFDgDLVLALAAYNAGPGR 206
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
33-163 4.47e-07

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: 46.53  E-value: 4.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2562478261  33 IQSAARKYGVPEGILYSVGLTETGrkgrLDPNAMNiegkpvfaasteeamvtfeaakRNGAklidLGCMQINHyFHGENF 112
Cdd:pfam01464   1 IIKAAQKYGVDPSLLLAIAQQESG----FNPKAVS----------------------KSGA----VGLMQIMP-STAKRL 49
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2562478261 113 -----TSAREMFDPRRNVEYAAMFLRNLHNRH-ETWTMAVARYHAGPNNDPAQKKYV 163
Cdd:pfam01464  50 glrvnPGVDDLFDPEKNIKAGTKYLKELYKQYgGDLWLALAAYNAGPGRVRKWIKNA 106
Slt70-like cd13401
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ...
32-171 4.94e-07

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: 47.09  E-value: 4.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2562478261  32 EIQSAARKYGVPEGILYSVGLTETgrkgRLDPNAMNiegkPVFAasteeamvtfeaakrngaklidLGCMQI-----NHY 106
Cdd:cd13401     9 LVERAAKKNGLDPALVYAIIRQES----AFDPDAVS----PAGA----------------------LGLMQLmpataKDV 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2562478261 107 F--HGENFTSAREMFDPRRNVEYAAMFLRNLHNRHE-TWTMAVARYHAGPNN-----------DPAQ----------KKY 162
Cdd:cd13401    59 AkkLGLPYYSPRDLFDPEYNIRLGSAYLAELLDRFDgNPVLALAAYNAGPGRvrrwlkrrgdlDPDLwietipfsetRNY 138

                  ....*....
gi 2562478261 163 VCRVIANLV 171
Cdd:cd13401   139 VKRVLENYV 147
LT_Slt70-like cd16896
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ...
30-155 9.99e-06

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: 43.27  E-value: 9.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2562478261  30 EREIQSAARKYGVPEGILYSVGLTETgrkgRLDPNAmniegkpvfaASteeamvtfeaakRNGAKlidlGCMQI------ 103
Cdd:cd16896     5 REYIEKYAKEYGVDPLLVAAVIKVES----NFNPNA----------VS------------SKGAI----GLMQImpetae 54
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2562478261 104 ---NHYfhGENFTSAREMFDPRRNVEYAAMFLRNLHNR-HETWTMAVARYHAGPNN 155
Cdd:cd16896    55 wiaEKL--GLEDFSEDDLYDPETNIRLGTWYLSYLLKEfDGNLVLALAAYNAGPGN 108
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
111-155 3.18e-04

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: 38.73  E-value: 3.18e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2562478261 111 NFTSAREMFDPRRNVEYAAMFLRNLHNRHE-TWTMAVARYHAGPNN 155
Cdd:cd00254    39 GRRGVDDLFDPEENIRAGARYLRELLDRFGgDLELALAAYNAGPGA 84
LT_VirB1-like cd16892
VirB1-like subfamily; This subfamily includes VirB1 protein, one of twelve proteins making up ...
60-169 1.19e-03

VirB1-like subfamily; This subfamily includes VirB1 protein, one of twelve proteins making up type IV secretion systems (T4SS). T4SS are macromolecular assemblies generally composed of VirB1-11 and VirD4 proteins, and are used by bacteria to transport material across their membranes. VirB1 acts as a lytic transglycosylase (LT), and is important with respect to piercing the peptidoglycan layer in the periplasm. 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, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).


Pssm-ID: 381613 [Multi-domain]  Cd Length: 143  Bit Score: 37.53  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2562478261  60 RLDPNAMNIEGKPV--FAASTEEAMVTFEAAKRNGAKlIDLGCMQINHyfhgENF----TSAREMFDPRRNVEYAAMFLR 133
Cdd:cd16892    23 GGNPYAIGVNGGKLsrQPKTKAEAIATARQLIAAGHN-FDVGLGQINS----RNLarlgLTVEDVFDPCTNLKAGATILT 97
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2562478261 134 NLHNRH--------ETWTMAVARYHAGPNNDPAQKKYVCRVIAN 169
Cdd:cd16892    98 ECYARAkktggdgqAALRAALSCYNTGNFTRGFSNGYVQKVVAA 141
 
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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