Species | CAG-873 sp009775195 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-873; CAG-873 sp009775195 | |||||||||||
CAZyme ID | MGYG000002721_01337 | |||||||||||
CAZy Family | GH23 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 4779; End: 6497 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH23 | 124 | 259 | 1.3e-26 | 0.8740740740740741 |
CBM50 | 528 | 570 | 2.9e-17 | 0.975 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd16894 | MltD-like | 2.97e-67 | 132 | 261 | 1 | 129 | 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). |
PRK10783 | mltD | 5.77e-46 | 91 | 567 | 72 | 444 | membrane-bound lytic murein transglycosylase D; Provisional |
pfam01464 | SLT | 6.42e-34 | 127 | 237 | 1 | 112 | Transglycosylase SLT domain. This family is distantly related to pfam00062. Members are found in phages, type II, type III and type IV secretion systems. |
cd13401 | Slt70-like | 1.90e-24 | 122 | 253 | 4 | 139 | 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. |
cd00254 | LT-like | 3.01e-23 | 148 | 261 | 11 | 110 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QQR10036.1 | 1.14e-181 | 15 | 570 | 12 | 546 |
ANU62627.1 | 1.14e-181 | 15 | 570 | 12 | 546 |
QIM10870.1 | 4.65e-155 | 1 | 572 | 1 | 541 |
QCD38174.1 | 3.30e-150 | 6 | 572 | 4 | 572 |
QCP71857.1 | 3.30e-150 | 6 | 572 | 4 | 572 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7EYB_I | 1.88e-08 | 124 | 253 | 12 | 139 | ChainI, Peptidoglycan transglycosylase gp16 [Escherichia phage T7],7EYB_J Chain J, Peptidoglycan transglycosylase gp16 [Escherichia phage T7],7EYB_K Chain K, Peptidoglycan transglycosylase gp16 [Escherichia phage T7],7EYB_L Chain L, Peptidoglycan transglycosylase gp16 [Escherichia phage T7],7K5C_B Chain B, Peptidoglycan transglycosylase gp16 [Escherichia phage T7],7K5C_D Chain D, Peptidoglycan transglycosylase gp16 [Escherichia phage T7],7K5C_F Chain F, Peptidoglycan transglycosylase gp16 [Escherichia phage T7],7K5C_G Chain G, Peptidoglycan transglycosylase gp16 [Escherichia phage T7],7K5C_J Chain J, Peptidoglycan transglycosylase gp16 [Escherichia phage T7],7K5C_L Chain L, Peptidoglycan transglycosylase gp16 [Escherichia phage T7] |
6YT5_G | 1.89e-08 | 124 | 253 | 34 | 161 | ChainG, Peptidoglycan transglycosylase gp16 [Escherichia phage T7],6YT5_H Chain H, Peptidoglycan transglycosylase gp16 [Escherichia phage T7],6YT5_I Chain I, Peptidoglycan transglycosylase gp16 [Escherichia phage T7],6YT5_J Chain J, Peptidoglycan transglycosylase gp16 [Escherichia phage T7],6YT5_K Chain K, Peptidoglycan transglycosylase gp16 [Escherichia phage T7],6YT5_L Chain L, Peptidoglycan transglycosylase gp16 [Escherichia phage T7] |
6FBT_A | 2.74e-06 | 148 | 253 | 474 | 582 | ChainA, Lytic murein transglycosylase [Pseudomonas aeruginosa] |
5OHU_A | 2.81e-06 | 148 | 253 | 503 | 611 | TheX-ray Structure of Lytic Transglycosylase Slt from Pseudomonas aeruginosa [Pseudomonas aeruginosa] |
2MKX_A | 4.49e-06 | 525 | 567 | 4 | 46 | Solutionstructure of LysM the peptidoglycan binding domain of autolysin AtlA from Enterococcus faecalis [Enterococcus faecalis V583] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P0AEZ7 | 2.82e-32 | 93 | 425 | 71 | 384 | Membrane-bound lytic murein transglycosylase D OS=Escherichia coli (strain K12) OX=83333 GN=mltD PE=1 SV=1 |
P0AEZ8 | 2.82e-32 | 93 | 425 | 71 | 384 | Membrane-bound lytic murein transglycosylase D OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=mltD PE=3 SV=1 |
O31608 | 2.70e-12 | 129 | 261 | 65 | 180 | Putative murein lytic transglycosylase YjbJ OS=Bacillus subtilis (strain 168) OX=224308 GN=yjbJ PE=3 SV=1 |
P03726 | 1.03e-07 | 124 | 253 | 12 | 139 | Peptidoglycan transglycosylase gp16 OS=Escherichia phage T7 OX=10760 GN=16 PE=1 SV=1 |
P39434 | 1.28e-06 | 148 | 258 | 505 | 620 | Soluble lytic murein transglycosylase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=slt PE=3 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.042523 | 0.496509 | 0.458839 | 0.000945 | 0.000629 | 0.000528 |
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