Species | Enterococcus faecalis | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; Enterococcus; Enterococcus faecalis | |||||||||||
CAZyme ID | MGYG000001694_01820 | |||||||||||
CAZy Family | GH73 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 1851296; End: 1852561 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam01551 | Peptidase_M23 | 4.10e-30 | 31 | 131 | 1 | 96 | Peptidase family M23. Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown. |
cd12797 | M23_peptidase | 3.32e-29 | 33 | 120 | 1 | 85 | M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins. This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity. |
COG0739 | NlpD | 1.19e-27 | 27 | 125 | 157 | 253 | Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis]. |
PRK11649 | PRK11649 | 3.35e-15 | 33 | 131 | 313 | 406 | putative peptidase; Provisional |
smart00047 | LYZ2 | 7.60e-08 | 179 | 298 | 24 | 146 | Lysozyme subfamily 2. Eubacterial enzymes distantly related to eukaryotic lysozymes. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
CCO72882.1 | 0.0 | 1 | 421 | 1 | 421 |
ASE66440.1 | 0.0 | 1 | 421 | 10 | 430 |
ACV83371.1 | 0.0 | 1 | 421 | 1 | 421 |
QGI56376.1 | 0.0 | 1 | 421 | 10 | 430 |
VTT47755.1 | 0.0 | 1 | 421 | 1 | 421 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7D55_A | 3.88e-32 | 339 | 420 | 1 | 82 | ChainA, Putative N-acetylmuramoyl-L-alanine amidase [Enterococcus phage phiM1EF22],7D55_B Chain B, Putative N-acetylmuramoyl-L-alanine amidase [Enterococcus phage phiM1EF22],7D55_C Chain C, Putative N-acetylmuramoyl-L-alanine amidase [Enterococcus phage phiM1EF22],7D55_D Chain D, Putative N-acetylmuramoyl-L-alanine amidase [Enterococcus phage phiM1EF22] |
6UE4_A | 1.87e-13 | 33 | 120 | 266 | 350 | ShyAEndopeptidase from Vibrio cholerae (Closed form) [Vibrio cholerae O1 biovar El Tor str. N16961],6UE4_B ShyA Endopeptidase from Vibrio cholerae (Closed form) [Vibrio cholerae O1 biovar El Tor str. N16961] |
6U2A_A | 1.89e-13 | 33 | 120 | 263 | 347 | ShyAendopeptidase from Vibrio cholera (open form) [Vibrio cholerae] |
6JMX_A | 4.82e-13 | 30 | 135 | 146 | 246 | ChainA, Peptidase M23 [Campylobacter jejuni],6JMY_A Chain A, Peptidase M23 [Campylobacter jejuni],6KV1_A Chain A, Peptidase M23 [Campylobacter jejuni] |
5KVP_A | 9.61e-13 | 33 | 135 | 34 | 146 | Solutionstructure of the catalytic domain of zoocin A [Streptococcus equi subsp. zooepidemicus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q89AI9 | 1.67e-09 | 33 | 134 | 251 | 347 | Uncharacterized metalloprotease bbp_296 OS=Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp) OX=224915 GN=bbp_296 PE=3 SV=1 |
Q8K9M4 | 4.49e-09 | 33 | 121 | 291 | 376 | Uncharacterized metalloprotease BUsg_310 OS=Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) OX=198804 GN=BUsg_310 PE=3 SV=1 |
A0A0H3C9Q9 | 1.35e-07 | 35 | 120 | 505 | 588 | Cell division protein DipM OS=Caulobacter vibrioides (strain NA1000 / CB15N) OX=565050 GN=dipM PE=3 SV=1 |
O31976 | 9.84e-07 | 26 | 135 | 1573 | 1678 | SPbeta prophage-derived uncharacterized transglycosylase YomI OS=Bacillus subtilis (strain 168) OX=224308 GN=yomI PE=3 SV=2 |
O64046 | 9.84e-07 | 26 | 135 | 1573 | 1678 | Probable tape measure protein OS=Bacillus phage SPbeta OX=66797 GN=yomI PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000040 | 0.000006 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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