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Conserved domains on  [gi|1111317626|gb|APH73640|]
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lytic transglycosylase [Aquibium oceanicum]

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 ...
 38-167 5.72e-18

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: 75.26  E-value: 5.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111317626  38 YGVPAGILYAVGLTETGHKGSlqpyalniegkasfarspaeaesifaAARREGKKLIDVGCMQINHHYHST--EFG--SL 113
Cdd:cd13400     1 YGVPPRLLRAIAKVESGFNPN--------------------------AINRNKNGSYDIGLMQINSIWLPElaRYGitRE 54

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1111317626 114 SDMFDPHKNVDYAARFLSNLKRRHATWSMAVARYHAGPDNDpaQKRYVCRVIAN 167
Cdd:cd13400    55 ELLNDPCTNIYVGAWILARNIKRYGNTWKAVGAYNSGTPKK--NDKYARKVYRI 106
 
Name Accession Description Interval E-value
LT_IagB-like cd13400
Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like ...
 38-167 5.72e-18

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: 75.26  E-value: 5.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111317626  38 YGVPAGILYAVGLTETGHKGSlqpyalniegkasfarspaeaesifaAARREGKKLIDVGCMQINHHYHST--EFG--SL 113
Cdd:cd13400     1 YGVPPRLLRAIAKVESGFNPN--------------------------AINRNKNGSYDIGLMQINSIWLPElaRYGitRE 54

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1111317626 114 SDMFDPHKNVDYAARFLSNLKRRHATWSMAVARYHAGPDNDpaQKRYVCRVIAN 167
Cdd:cd13400    55 ELLNDPCTNIYVGAWILARNIKRYGNTWKAVGAYNSGTPKK--NDKYARKVYRI 106
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 30-169 6.67e-09

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: 53.46  E-value: 6.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111317626  30 EILRASHKYGVPAGILYAVGLTETGhkgsLQPYalniegkasfARSPAEAesifaaarregkklidVGCMQI------NH 103
Cdd:COG0741   106 LIEEAAKKYGVDPALVLALIRQESA----FNPN----------AVSPAGA----------------RGLMQLmpatarRL 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111317626 104 HYHSTEFGSLSDMFDPHKNVDYAARFLSNLKRRHA-TWSMAVARYHAGP-----------DNDPAQ------KRYVCRVI 165
Cdd:COG0741   156 GLKLGLGPSPDDLFDPETNIRAGAAYLRELLDRFDgDLVLALAAYNAGPgrvrrwlrrngDRDGEIipyaetRNYVKKVL 235


                  ....
gi 1111317626 166 ANMV 169
Cdd:COG0741   236 ANYA 239
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 31-161 1.02e-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: 48.07  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111317626  31 ILRASHKYGVPAGILYAVGLTETGhkgsLQPYAlniegkasfaRSPAEAesifaaarregkklidVGCMQINHHyHSTEF 110
Cdd:pfam01464   1 IIKAAQKYGVDPSLLLAIAQQESG----FNPKA----------VSKSGA----------------VGLMQIMPS-TAKRL 49

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1111317626 111 G-----SLSDMFDPHKNVDYAARFLSNLKRRHAT-WSMAVARYHAGPDNDPAQKRYV 161
Cdd:pfam01464  50 GlrvnpGVDDLFDPEKNIKAGTKYLKELYKQYGGdLWLALAAYNAGPGRVRKWIKNA 106
PRK15328 PRK15328
type III secretion system invasion protein IagB;
32-164 2.90e-05

type III secretion system invasion protein IagB;


Pssm-ID: 185228 [Multi-domain]  Cd Length: 160  Bit Score: 42.54  E-value: 2.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111317626  32 LRASHKYGVPAGILYAVGLTETGHKgslqPYALNIEgkasfarspaeaesifaaarREGKKliDVGCMQINH-HYHSTEF 110
Cdd:PRK15328   23 LQAEKMFNIESELLYAIAQQESAMK----PGAIGHN--------------------RDGST--DLGLMQINSfHMKRLKK 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1111317626 111 GSLSD---MFDPHKNVDYAARFLSNLKRRHATWSMAVARYHAG--PDNDPAQKRYVCRV 164
Cdd:PRK15328   77 MGISEkqlLQDPCISVIVGASILSDMMKIYGYSWEAVGAYNAGtsPKRSDIRKRYAKKI 135
 
Name Accession Description Interval E-value
LT_IagB-like cd13400
Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like ...
 38-167 5.72e-18

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: 75.26  E-value: 5.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111317626  38 YGVPAGILYAVGLTETGHKGSlqpyalniegkasfarspaeaesifaAARREGKKLIDVGCMQINHHYHST--EFG--SL 113
Cdd:cd13400     1 YGVPPRLLRAIAKVESGFNPN--------------------------AINRNKNGSYDIGLMQINSIWLPElaRYGitRE 54

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1111317626 114 SDMFDPHKNVDYAARFLSNLKRRHATWSMAVARYHAGPDNDpaQKRYVCRVIAN 167
Cdd:cd13400    55 ELLNDPCTNIYVGAWILARNIKRYGNTWKAVGAYNSGTPKK--NDKYARKVYRI 106
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 30-169 6.67e-09

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: 53.46  E-value: 6.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111317626  30 EILRASHKYGVPAGILYAVGLTETGhkgsLQPYalniegkasfARSPAEAesifaaarregkklidVGCMQI------NH 103
Cdd:COG0741   106 LIEEAAKKYGVDPALVLALIRQESA----FNPN----------AVSPAGA----------------RGLMQLmpatarRL 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111317626 104 HYHSTEFGSLSDMFDPHKNVDYAARFLSNLKRRHA-TWSMAVARYHAGP-----------DNDPAQ------KRYVCRVI 165
Cdd:COG0741   156 GLKLGLGPSPDDLFDPETNIRAGAAYLRELLDRFDgDLVLALAAYNAGPgrvrrwlrrngDRDGEIipyaetRNYVKKVL 235


                  ....
gi 1111317626 166 ANMV 169
Cdd:COG0741   236 ANYA 239
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 31-161 1.02e-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: 48.07  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111317626  31 ILRASHKYGVPAGILYAVGLTETGhkgsLQPYAlniegkasfaRSPAEAesifaaarregkklidVGCMQINHHyHSTEF 110
Cdd:pfam01464   1 IIKAAQKYGVDPSLLLAIAQQESG----FNPKA----------VSKSGA----------------VGLMQIMPS-TAKRL 49

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1111317626 111 G-----SLSDMFDPHKNVDYAARFLSNLKRRHAT-WSMAVARYHAGPDNDPAQKRYV 161
Cdd:pfam01464  50 GlrvnpGVDDLFDPEKNIKAGTKYLKELYKQYGGdLWLALAAYNAGPGRVRKWIKNA 106
LT_VirB1-like cd16892
VirB1-like subfamily; This subfamily includes VirB1 protein, one of twelve proteins making up ...
 55-168 1.01e-06

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: 46.00  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111317626  55 HKGSLQPYALNIEG--KASFARSPAEAESIFAAARREGKKlIDVGCMQINhhyhSTEFGSL----SDMFDPHKNVDYAAR 128
Cdd:cd16892    20 VESGGNPYAIGVNGgkLSRQPKTKAEAIATARQLIAAGHN-FDVGLGQIN----SRNLARLgltvEDVFDPCTNLKAGAT 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1111317626 129 FLSNLKRRH--------ATWSMAVARYHAGPDNDPAQKRYVCRVIANM 168
Cdd:cd16892    95 ILTECYARAkktggdgqAALRAALSCYNTGNFTRGFSNGYVQKVVAAA 142
Slt70-like cd13401
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ...
 30-169 2.43e-06

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: 45.16  E-value: 2.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111317626  30 EILRASHKYGVPAGILYAVGLTETghkgSLQPYAlniegkasfaRSPAEAES----IFAAARREGKKLidvgcmqiNHHY 105
Cdd:cd13401     9 LVERAAKKNGLDPALVYAIIRQES----AFDPDA----------VSPAGALGlmqlMPATAKDVAKKL--------GLPY 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111317626 106 HSTEfgslsDMFDPHKNVDYAARFLSNLKRRHA-TWSMAVARYHAGP-----------DNDPA---------QKR-YVCR 163
Cdd:cd13401    67 YSPR-----DLFDPEYNIRLGSAYLAELLDRFDgNPVLALAAYNAGPgrvrrwlkrrgDLDPDlwietipfsETRnYVKR 141


                  ....*.
gi 1111317626 164 VIANMV 169
Cdd:cd13401   142 VLENYV 147
PRK15328 PRK15328
type III secretion system invasion protein IagB;
32-164 2.90e-05

type III secretion system invasion protein IagB;


Pssm-ID: 185228 [Multi-domain]  Cd Length: 160  Bit Score: 42.54  E-value: 2.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111317626  32 LRASHKYGVPAGILYAVGLTETGHKgslqPYALNIEgkasfarspaeaesifaaarREGKKliDVGCMQINH-HYHSTEF 110
Cdd:PRK15328   23 LQAEKMFNIESELLYAIAQQESAMK----PGAIGHN--------------------RDGST--DLGLMQINSfHMKRLKK 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1111317626 111 GSLSD---MFDPHKNVDYAARFLSNLKRRHATWSMAVARYHAG--PDNDPAQKRYVCRV 164
Cdd:PRK15328   77 MGISEkqlLQDPCISVIVGASILSDMMKIYGYSWEAVGAYNAGtsPKRSDIRKRYAKKI 135
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
 110-168 2.36e-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: 39.12  E-value: 2.36e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1111317626 110 FGSLSDMFDPHKNVDYAARFLS-NLKRRHATWSMAVARYHAGPDN-----------DPAQKRYVCRVIANM 168
Cdd:cd00254    40 RRGVDDLFDPEENIRAGARYLReLLDRFGGDLELALAAYNAGPGAvdrwgggevppYKETRNYVQRVLAYY 110
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
 117-153 7.14e-03

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: 35.19  E-value: 7.14e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1111317626 117 FDPHKNVDYAARFLSNLKRRHATWSMAVARYHAGPDN 153
Cdd:cd16894    56 RDPEKSTRAAARYLKDLYKRFGDWLLALAAYNAGEGR 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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