Species | Pediococcus pentosaceus | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Pediococcus; Pediococcus pentosaceus | |||||||||||
CAZyme ID | MGYG000002367_00938 | |||||||||||
CAZy Family | GH73 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 263289; End: 264413 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd06583 | PGRP | 8.72e-13 | 53 | 180 | 5 | 126 | Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in certain cases, hydrolyze peptidoglycans (PGNs) of bacterial cell walls. PGRPs have been divided into three classes: short PGRPs (PGRP-S), that are small (20 kDa) extracellular proteins; intermediate PGRPs (PGRP-I) that are 40-45 kDa and are predicted to be transmembrane proteins; and long PGRPs (PGRP-L), up to 90 kDa, which may be either intracellular or transmembrane. Several structures of PGRPs are known in insects and mammals, some bound with substrates like Muramyl Tripeptide (MTP) or Tracheal Cytotoxin (TCT). The substrate binding site is conserved in PGRP-LCx, PGRP-LE, and PGRP-Ialpha proteins. This family includes Zn-dependent N-Acetylmuramoyl-L-alanine Amidase, EC:3.5.1.28. This enzyme cleaves the amide bond between N-acetylmuramoyl and L-amino acids, preferentially D-lactyl-L-Ala, in bacterial cell walls. The structure for the bacteriophage T7 lysozyme shows that two of the conserved histidines and a cysteine are zinc binding residues. Site-directed mutagenesis of T7 lysozyme indicates that two conserved residues, a Tyr and a Lys, are important for amidase activity. |
pfam01510 | Amidase_2 | 2.78e-11 | 51 | 177 | 3 | 119 | N-acetylmuramoyl-L-alanine amidase. This family includes zinc amidases that have N-acetylmuramoyl-L-alanine amidase activity EC:3.5.1.28. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls (preferentially: D-lactyl-L-Ala). The structure is known for the bacteriophage T7 structure and shows that two of the conserved histidines are zinc binding. |
smart00644 | Ami_2 | 1.68e-09 | 52 | 169 | 5 | 123 | Ami_2 domain. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ABJ67868.1 | 1.08e-104 | 1 | 374 | 1 | 438 |
QGZ70144.1 | 9.97e-103 | 1 | 374 | 1 | 416 |
QYY85690.1 | 4.79e-99 | 1 | 374 | 1 | 421 |
QYY86091.1 | 4.20e-91 | 1 | 374 | 1 | 419 |
APR28090.1 | 2.62e-89 | 219 | 374 | 287 | 442 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4IVV_A | 1.78e-17 | 81 | 200 | 53 | 175 | Catalyticamidase domain of the major autolysin LytA from Streptococcus pneumaniae [Streptococcus pneumoniae TIGR4] |
4X36_A | 1.94e-16 | 81 | 200 | 51 | 173 | Crystalstructure of the autolysin LytA from Streptococcus pneumoniae TIGR4 [Streptococcus pneumoniae TIGR4] |
5CTV_A | 4.19e-16 | 81 | 200 | 53 | 175 | Catalyticdomain of LytA, the major autolysin of Streptococcus pneumoniae, (C60A, H133A, C136A mutant) complexed with peptidoglycan fragment [Streptococcus pneumoniae TIGR4] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q38135 | 9.48e-31 | 36 | 238 | 8 | 213 | N-acetylmuramoyl-L-alanine amidase OS=Lactococcus phage r1t OX=43685 PE=3 SV=1 |
Q38653 | 2.41e-25 | 51 | 195 | 23 | 170 | Endolysin OS=Listeria phage A511 OX=40523 GN=PLY511 PE=2 SV=1 |
P06653 | 1.44e-15 | 81 | 200 | 51 | 173 | Autolysin OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=lytA PE=1 SV=2 |
P32762 | 2.20e-14 | 91 | 202 | 60 | 175 | Lytic amidase OS=Streptococcus pneumoniae phage HB-3 OX=10728 GN=HBL PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000593 | 0.998399 | 0.000285 | 0.000271 | 0.000231 | 0.000211 |
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