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Conserved domains on  [gi|2485327363|gb|WGB90857|]
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transglycosylase SLT domain-containing protein (plasmid) [Escherichia coli]

Protein Classification

transglycosylase SLT domain-containing protein( domain architecture ID 10793850)

transglycosylase SLT domain-containing protein similar to Escherichia coli X polypeptide

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK13722 PRK13722
lytic transglycosylase; Provisional
47-215 1.06e-125

lytic transglycosylase; Provisional


:

Pssm-ID: 184274 [Multi-domain]  Cd Length: 169  Bit Score: 352.08  E-value: 1.06e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485327363  47 MKKWMLAICLMFINEICHATDCFDLAGRDYKIDPDLLRAISWKESRYRVNAIGINPVTGYGSGLMQVDSQHFNELARYGI 126
Cdd:PRK13722    1 MKKWMLAICLMFINEICHATDCFDLAGRDYKIDPDLLRAISWKESRYRVNAIGINPVTGYGSGLMQVDSQHFNELARYGI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485327363 127 KPEHLTTDPCMNIYTGAYYLAIAFKKWGVTWEAVGAYNAGFRKSERQNQRRLAYASEVYRIYTGIKSSKGIRLPATKKSL 206
Cdd:PRK13722   81 KPEHLTTDPCMNIYTGAYYLAIAFKKWGVSWEAVGAYNAGFRKTERQNQRRLAYASEVYRIYTGIKSSKGIRIPATKKSL 160

                  ....*....
gi 2485327363 207 PEINSVQNN 215
Cdd:PRK13722  161 PEINSVQNN 169
 
Name Accession Description Interval E-value
PRK13722 PRK13722
lytic transglycosylase; Provisional
47-215 1.06e-125

lytic transglycosylase; Provisional


Pssm-ID: 184274 [Multi-domain]  Cd Length: 169  Bit Score: 352.08  E-value: 1.06e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485327363  47 MKKWMLAICLMFINEICHATDCFDLAGRDYKIDPDLLRAISWKESRYRVNAIGINPVTGYGSGLMQVDSQHFNELARYGI 126
Cdd:PRK13722    1 MKKWMLAICLMFINEICHATDCFDLAGRDYKIDPDLLRAISWKESRYRVNAIGINPVTGYGSGLMQVDSQHFNELARYGI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485327363 127 KPEHLTTDPCMNIYTGAYYLAIAFKKWGVTWEAVGAYNAGFRKSERQNQRRLAYASEVYRIYTGIKSSKGIRLPATKKSL 206
Cdd:PRK13722   81 KPEHLTTDPCMNIYTGAYYLAIAFKKWGVSWEAVGAYNAGFRKTERQNQRRLAYASEVYRIYTGIKSSKGIRIPATKKSL 160

                  ....*....
gi 2485327363 207 PEINSVQNN 215
Cdd:PRK13722  161 PEINSVQNN 169
LT_IagB-like cd13400
Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like ...
76-189 2.83e-45

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: 146.13  E-value: 2.83e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485327363  76 YKIDPDLLRAISWKESRYRVNAIGINPVTGYGSGLMQVDSQHFNELARYGIKPEHLTTDPCMNIYTGAYYLAIAFKKWGV 155
Cdd:cd13400     1 YGVPPRLLRAIAKVESGFNPNAINRNKNGSYDIGLMQINSIWLPELARYGITREELLNDPCTNIYVGAWILARNIKRYGN 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2485327363 156 TWEAVGAYNAGFRKserqnqRRLAYASEVYRIYT 189
Cdd:cd13400    81 TWKAVGAYNSGTPK------KNDKYARKVYRIYR 108
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
72-181 6.53e-19

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: 78.50  E-value: 6.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485327363  72 AGRDYKIDPDLLRAISWKESRYRVNAIgiNPVTGYGsgLMQVDSQHFNELARYGIKPEHLTTDPCMNIYTGAYYLAIAFK 151
Cdd:pfam01464   4 AAQKYGVDPSLLLAIAQQESGFNPKAV--SKSGAVG--LMQIMPSTAKRLGLRVNPGVDDLFDPEKNIKAGTKYLKELYK 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2485327363 152 KWG-VTWEAVGAYNAGF---RKSERQNQRRLAYA 181
Cdd:pfam01464  80 QYGgDLWLALAAYNAGPgrvRKWIKNAGAKDKKL 113
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
72-166 8.10e-12

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: 62.32  E-value: 8.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485327363  72 AGRDYKIDPDLLRAISWKESRYRVNAIGinPVtgyG-SGLMQVDSQHFNELA-RYGIKP-EHLTTDPCMNIYTGAYYLAI 148
Cdd:COG0741   110 AAKKYGVDPALVLALIRQESAFNPNAVS--PA---GaRGLMQLMPATARRLGlKLGLGPsPDDLFDPETNIRAGAAYLRE 184
                          90
                  ....*....|....*....
gi 2485327363 149 AFKKWGVTWE-AVGAYNAG 166
Cdd:COG0741   185 LLDRFDGDLVlALAAYNAG 203
 
Name Accession Description Interval E-value
PRK13722 PRK13722
lytic transglycosylase; Provisional
47-215 1.06e-125

lytic transglycosylase; Provisional


Pssm-ID: 184274 [Multi-domain]  Cd Length: 169  Bit Score: 352.08  E-value: 1.06e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485327363  47 MKKWMLAICLMFINEICHATDCFDLAGRDYKIDPDLLRAISWKESRYRVNAIGINPVTGYGSGLMQVDSQHFNELARYGI 126
Cdd:PRK13722    1 MKKWMLAICLMFINEICHATDCFDLAGRDYKIDPDLLRAISWKESRYRVNAIGINPVTGYGSGLMQVDSQHFNELARYGI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485327363 127 KPEHLTTDPCMNIYTGAYYLAIAFKKWGVTWEAVGAYNAGFRKSERQNQRRLAYASEVYRIYTGIKSSKGIRLPATKKSL 206
Cdd:PRK13722   81 KPEHLTTDPCMNIYTGAYYLAIAFKKWGVSWEAVGAYNAGFRKTERQNQRRLAYASEVYRIYTGIKSSKGIRIPATKKSL 160

                  ....*....
gi 2485327363 207 PEINSVQNN 215
Cdd:PRK13722  161 PEINSVQNN 169
LT_IagB-like cd13400
Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like ...
76-189 2.83e-45

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: 146.13  E-value: 2.83e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485327363  76 YKIDPDLLRAISWKESRYRVNAIGINPVTGYGSGLMQVDSQHFNELARYGIKPEHLTTDPCMNIYTGAYYLAIAFKKWGV 155
Cdd:cd13400     1 YGVPPRLLRAIAKVESGFNPNAINRNKNGSYDIGLMQINSIWLPELARYGITREELLNDPCTNIYVGAWILARNIKRYGN 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2485327363 156 TWEAVGAYNAGFRKserqnqRRLAYASEVYRIYT 189
Cdd:cd13400    81 TWKAVGAYNSGTPK------KNDKYARKVYRIYR 108
PRK15328 PRK15328
type III secretion system invasion protein IagB;
49-192 5.18e-30

type III secretion system invasion protein IagB;


Pssm-ID: 185228 [Multi-domain]  Cd Length: 160  Bit Score: 108.80  E-value: 5.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485327363  49 KWMLAICLMFINEICHATDCFDLAGRDYKIDPDLLRAISWKESRYRVNAIGINPVTGYGSGLMQVDSQHFNELARYGIKP 128
Cdd:PRK15328    2 HYFFIIVIWLLSINTAWADCWLQAEKMFNIESELLYAIAQQESAMKPGAIGHNRDGSTDLGLMQINSFHMKRLKKMGISE 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2485327363 129 EHLTTDPCMNIYTGAYYLAIAFKKWGVTWEAVGAYNAGFRKsERQNQRRLaYASEVYRIYTGIK 192
Cdd:PRK15328   82 KQLLQDPCISVIVGASILSDMMKIYGYSWEAVGAYNAGTSP-KRSDIRKR-YAKKIWENYRKLK 143
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
72-181 6.53e-19

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: 78.50  E-value: 6.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485327363  72 AGRDYKIDPDLLRAISWKESRYRVNAIgiNPVTGYGsgLMQVDSQHFNELARYGIKPEHLTTDPCMNIYTGAYYLAIAFK 151
Cdd:pfam01464   4 AAQKYGVDPSLLLAIAQQESGFNPKAV--SKSGAVG--LMQIMPSTAKRLGLRVNPGVDDLFDPEKNIKAGTKYLKELYK 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2485327363 152 KWG-VTWEAVGAYNAGF---RKSERQNQRRLAYA 181
Cdd:pfam01464  80 QYGgDLWLALAAYNAGPgrvRKWIKNAGAKDKKL 113
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
72-166 8.10e-12

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: 62.32  E-value: 8.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485327363  72 AGRDYKIDPDLLRAISWKESRYRVNAIGinPVtgyG-SGLMQVDSQHFNELA-RYGIKP-EHLTTDPCMNIYTGAYYLAI 148
Cdd:COG0741   110 AAKKYGVDPALVLALIRQESAFNPNAVS--PA---GaRGLMQLMPATARRLGlKLGLGPsPDDLFDPETNIRAGAAYLRE 184
                          90
                  ....*....|....*....
gi 2485327363 149 AFKKWGVTWE-AVGAYNAG 166
Cdd:COG0741   185 LLDRFDGDLVlALAAYNAG 203
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
80-166 2.17e-10

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: 56.07  E-value: 2.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485327363  80 PDLLRAISWKESRYRVNAigINPVTGYgsGLMQVDSQHFNELARYGikPEHLtTDPCMNIYTGAYYLAIAFKKWGVTWE- 158
Cdd:cd00254     1 PALVLAVIRVESGFNPRA--VSPAGAR--GLMQLMPGTARDLGRRG--VDDL-FDPEENIRAGARYLRELLDRFGGDLEl 73

                  ....*...
gi 2485327363 159 AVGAYNAG 166
Cdd:cd00254    74 ALAAYNAG 81
Slt70-like cd13401
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ...
72-166 1.53e-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: 46.32  E-value: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485327363  72 AGRDYKIDPDLLRAISWKESRY------RVNAIginpvtgygsGLMQVDSQHFNELAR-YGIK--PEHLTTDPCMNIYTG 142
Cdd:cd13401    13 AAKKNGLDPALVYAIIRQESAFdpdavsPAGAL----------GLMQLMPATAKDVAKkLGLPyySPRDLFDPEYNIRLG 82
                          90       100
                  ....*....|....*....|....*
gi 2485327363 143 AYYLAIAFKKW-GVTWEAVGAYNAG 166
Cdd:cd13401    83 SAYLAELLDRFdGNPVLALAAYNAG 107
LT_Slt70-like cd16896
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ...
76-166 4.59e-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: 44.81  E-value: 4.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485327363  76 YKIDPDLLRAISWKESRYRVNAIGinpvtGYGS-GLMQVDSQHFNELA-RYGI---KPEHLtTDPCMNIYTGAYYLAIAF 150
Cdd:cd16896    15 YGVDPLLVAAVIKVESNFNPNAVS-----SKGAiGLMQIMPETAEWIAeKLGLedfSEDDL-YDPETNIRLGTWYLSYLL 88
                          90
                  ....*....|....*..
gi 2485327363 151 KKWGVTWE-AVGAYNAG 166
Cdd:cd16896    89 KEFDGNLVlALAAYNAG 105
MLTF-like cd13403
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily ...
69-179 1.25e-05

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: 43.68  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485327363  69 FDLAGRDYKIDPDLLRAISWKESRYRVNAIGINPVTGygsgLMQVdsqhFNELAR-YGIKPEHlttDPCMNIYTGAYYLA 147
Cdd:cd13403     1 FKKYAEKYGFDWRLLAAQAYQESRFNPNARSPAGARG----LMQL----MPSTAReLGVNDRL---DPEQNIHAGAKYLR 69
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2485327363 148 IAFKKW--GVT-----WEAVGAYNAGFRKSErqNQRRLA 179
Cdd:cd13403    70 YLRDRFppDIDepdrlKFALAAYNAGPGHVR--DARRLA 106
GEWL cd01021
Goose egg-white lysozyme; Eukaryotic goose-type or G-type lysozyme (goose egg-white lysozyme; ...
67-166 8.60e-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: 41.43  E-value: 8.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485327363  67 DCFDLAGRDYKIDPDLLRAISWKESRyrvnAIGINPVTGYGS-----GLMQVDSQHfnelarYGIK-----PEHLttDPC 136
Cdd:cd01021    39 DCIKQVGKKLCIDPALIAAIISRESR----AGAALDKNGWGDhgngfGLMQVDKRY------HPPKgawdsEEHI--EQA 106
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2485327363 137 MNIYTGaYYLAIA--FKKWgvTWE-----AVGAYNAG 166
Cdd:cd01021   107 TGILID-FIKTVQrkHPSW--SPEqqlkgGIAAYNAG 140
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
69-179 1.14e-04

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


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 42.36  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485327363  69 FDLAGRDYKIDPDLLRAISWKESRYRVNAIGinpVTGyGSGLMQVdsqhFNELAR-YGIKPehlTTDPCMNIYTGAYYLA 147
Cdd:COG4623   268 FEKYAEEYGLDWRLLAALAYQESHWNPRARS---PTG-ARGLMQL----MPATAKeLGVDD---RLDPEQSIRAGAKYLR 336
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2485327363 148 IAFKKWGV-------TWEAVGAYNAGFRKSERqnQRRLA 179
Cdd:COG4623   337 WLYDRFPEaidepdrWWFALAAYNAGPGHVQD--ARRLA 373
LT_VirB1-like cd16892
VirB1-like subfamily; This subfamily includes VirB1 protein, one of twelve proteins making up ...
78-143 1.86e-04

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: 40.22  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485327363  78 IDPDLLRAISWKESRYRVNAIGIN-------PVT--------------GY--GSGLMQVDSQHFnelARYGIKPEHLtTD 134
Cdd:cd16892     9 VHPETLAAIVQVESGGNPYAIGVNggklsrqPKTkaeaiatarqliaaGHnfDVGLGQINSRNL---ARLGLTVEDV-FD 84

                  ....*....
gi 2485327363 135 PCMNIYTGA 143
Cdd:cd16892    85 PCTNLKAGA 93
LT_MltC_MltE cd16893
membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and ...
74-166 2.68e-03

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: 37.15  E-value: 2.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485327363  74 RDYKIDPDLLRAISWKESRY------RVNAIginpvtgygsGLMQV--------DSQhfnelaRYGIKPEHLTT----DP 135
Cdd:cd16893     8 KKYGVDPALILAIIETESSFnpyavsHSPAY----------GLMQIvpstagrdVYR------LLGGKGGLPSKsylfDP 71
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2485327363 136 CMNIYTGAYYLAIAFKKW--GVTWE------AVGAYNAG 166
Cdd:cd16893    72 ENNIDIGTAYLHILQNRYlkGIKNPksreycAIAAYNGG 110
 
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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