Species | RC9 sp900544195 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; UBA932; RC9; RC9 sp900544195 | |||||||||||
CAZyme ID | MGYG000000584_01273 | |||||||||||
CAZy Family | GH23 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 18936; End: 20540 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH23 | 174 | 313 | 5.2e-26 | 0.9111111111111111 |
CBM50 | 426 | 467 | 1e-15 | 0.95 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd16894 | MltD-like | 1.08e-63 | 182 | 310 | 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 | 8.19e-58 | 174 | 530 | 104 | 444 | membrane-bound lytic murein transglycosylase D; Provisional |
pfam01464 | SLT | 1.75e-29 | 177 | 284 | 1 | 109 | 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 | 1.31e-18 | 382 | 532 | 435 | 591 | 1,4-beta-N-acetylmuramoylhydrolase. |
cd00254 | LT-like | 1.62e-18 | 194 | 303 | 5 | 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 | 2.11e-157 | 29 | 534 | 31 | 540 |
AZS28203.1 | 7.33e-132 | 90 | 532 | 53 | 523 |
QRO49268.1 | 2.34e-130 | 90 | 532 | 53 | 523 |
QPH59243.1 | 8.32e-128 | 93 | 469 | 60 | 438 |
QBJ18933.1 | 8.32e-128 | 93 | 469 | 60 | 438 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2MKX_A | 3.40e-07 | 422 | 470 | 2 | 51 | 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 |
---|---|---|---|---|---|---|
P0AEZ8 | 3.66e-39 | 143 | 532 | 71 | 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 | 3.66e-39 | 143 | 532 | 71 | 442 | Membrane-bound lytic murein transglycosylase D OS=Escherichia coli (strain K12) OX=83333 GN=mltD PE=1 SV=1 |
Q5HRU2 | 9.53e-14 | 406 | 533 | 66 | 191 | N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) OX=176279 GN=sle1 PE=3 SV=1 |
Q8CMN2 | 9.53e-14 | 406 | 533 | 66 | 191 | N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) OX=176280 GN=sle1 PE=3 SV=1 |
Q49UX4 | 1.03e-12 | 425 | 532 | 87 | 193 | N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41) OX=342451 GN=sle1 PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000195 | 0.999194 | 0.000153 | 0.000155 | 0.000146 | 0.000135 |
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