Species | RC9 sp001915575 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; UBA932; RC9; RC9 sp001915575 | |||||||||||
CAZyme ID | MGYG000003991_01576 | |||||||||||
CAZy Family | GH23 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 1624; End: 3237 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH23 | 168 | 310 | 4.4e-26 | 0.9333333333333333 |
CBM50 | 492 | 535 | 4.3e-16 | 0.975 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd16894 | MltD-like | 7.28e-63 | 176 | 304 | 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 | 2.27e-59 | 176 | 532 | 112 | 444 | membrane-bound lytic murein transglycosylase D; Provisional |
pfam01464 | SLT | 3.48e-27 | 178 | 277 | 7 | 108 | Transglycosylase SLT domain. This family is distantly related to pfam00062. Members are found in phages, type II, type III and type IV secretion systems. |
PRK06347 | PRK06347 | 1.19e-20 | 325 | 534 | 225 | 449 | 1,4-beta-N-acetylmuramoylhydrolase. |
cd00254 | LT-like | 4.80e-20 | 188 | 297 | 7 | 104 | 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 |
---|---|---|---|---|---|
AGY53188.1 | 1.61e-138 | 25 | 534 | 28 | 538 |
AHF12926.1 | 1.48e-125 | 87 | 535 | 2 | 443 |
QJE29305.1 | 9.65e-125 | 42 | 536 | 11 | 514 |
QUT50531.1 | 3.97e-124 | 87 | 536 | 54 | 515 |
ALB75652.1 | 3.97e-124 | 87 | 536 | 54 | 515 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7EYB_I | 7.87e-07 | 185 | 323 | 30 | 169 | 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 | 7.90e-07 | 185 | 323 | 52 | 191 | 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] |
4UZ2_A | 6.34e-06 | 492 | 535 | 5 | 47 | Crystalstructure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ2_B Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ2_C Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ2_D Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ3_A Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus bound to N-acetyl-chitohexaose [Thermus thermophilus HB8],4UZ3_B Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus bound to N-acetyl-chitohexaose [Thermus thermophilus HB8],4UZ3_C Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus bound to N-acetyl-chitohexaose [Thermus thermophilus HB8] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P0AEZ8 | 4.32e-41 | 111 | 534 | 36 | 442 | Membrane-bound lytic murein transglycosylase D OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=mltD PE=3 SV=1 |
P0AEZ7 | 4.32e-41 | 111 | 534 | 36 | 442 | Membrane-bound lytic murein transglycosylase D OS=Escherichia coli (strain K12) OX=83333 GN=mltD PE=1 SV=1 |
P37710 | 3.81e-13 | 419 | 534 | 632 | 736 | Autolysin OS=Enterococcus faecalis (strain ATCC 700802 / V583) OX=226185 GN=EF_0799 PE=1 SV=2 |
Q6GJK9 | 4.74e-12 | 324 | 534 | 25 | 201 | N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain MRSA252) OX=282458 GN=sle1 PE=3 SV=1 |
P54421 | 8.49e-12 | 420 | 534 | 88 | 192 | Probable peptidoglycan endopeptidase LytE OS=Bacillus subtilis (strain 168) OX=224308 GN=lytE PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000211 | 0.999171 | 0.000149 | 0.000160 | 0.000146 | 0.000135 |
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