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CAZyme Information: MGYG000003691_02548

You are here: Home > Sequence: MGYG000003691_02548

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Prevotella disiens
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella disiens
CAZyme ID MGYG000003691_02548
CAZy Family GH73
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
258 29266.56 9.6123
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003691 2802053 Isolate China Asia
Gene Location Start: 139;  End: 915  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003691_02548.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH73 161 257 5.2e-17 0.9140625

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG0739 NlpD 5.28e-30 5 142 138 277
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
pfam01551 Peptidase_M23 4.71e-27 29 122 2 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 2.39e-24 30 113 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.
smart00047 LYZ2 1.48e-13 160 254 21 135
Lysozyme subfamily 2. Eubacterial enzymes distantly related to eukaryotic lysozymes.
pfam01832 Glucosaminidase 1.82e-13 159 224 5 80
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase. This family includes Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase EC:3.2.1.96. As well as the flageller protein J that has been shown to hydrolyze peptidoglycan.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ATV39431.1 2.55e-192 1 258 111 368
QUB71734.1 1.71e-128 1 258 96 353
QUB41748.1 9.59e-126 1 258 93 350
ASE17922.1 4.81e-125 1 258 93 350
QUB53548.1 6.83e-125 1 258 93 350

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3SLU_A 1.53e-16 6 122 222 338
Crystalstructure of NMB0315 [Neisseria meningitidis ATCC 13091],3SLU_B Crystal structure of NMB0315 [Neisseria meningitidis ATCC 13091]
6MUK_A 1.79e-16 6 122 242 358
1.93Angstrom Resolution Crystal Structure of Peptidase M23 from Neisseria gonorrhoeae. [Neisseria gonorrhoeae FA 1090]
6JMX_A 4.91e-16 12 130 131 250
ChainA, Peptidase M23 [Campylobacter jejuni],6JMY_A Chain A, Peptidase M23 [Campylobacter jejuni],6KV1_A Chain A, Peptidase M23 [Campylobacter jejuni]
6JN1_A 1.08e-14 12 130 131 250
ChainA, Peptidase M23 [Campylobacter jejuni]
6JN0_A 1.09e-14 12 130 131 250
ChainA, Peptidase M23 [Campylobacter jejuni],7E60_A Chain A, Peptidase M23 [Campylobacter jejuni],7E61_A Chain A, Peptidase M23 [Campylobacter jejuni],7E63_A Chain A, Peptidase M23 [Campylobacter jejuni],7E63_B Chain B, Peptidase M23 [Campylobacter jejuni],7E64_A Chain A, Peptidase M23 [Campylobacter jejuni],7E65_A Chain A, Peptidase M23 [Campylobacter jejuni],7E65_B Chain B, Peptidase M23 [Campylobacter jejuni],7E66_A Chain A, Peptidase M23 [Campylobacter jejuni],7E67_A Chain A, Peptidase M23 [Campylobacter jejuni],7E69_A Chain A, Peptidase M23 [Campylobacter jejuni]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O05156 4.30e-12 16 187 136 290
Glycyl-glycine endopeptidase ALE-1 OS=Staphylococcus capitis OX=29388 PE=1 SV=1
P44693 1.01e-11 30 122 348 442
Uncharacterized metalloprotease HI_0409 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_0409 PE=3 SV=1
P10548 3.36e-11 16 126 252 369
Lysostaphin OS=Staphylococcus staphylolyticus OX=1287 GN=lss PE=3 SV=1
P10547 3.41e-11 16 126 265 382
Lysostaphin OS=Staphylococcus simulans OX=1286 GN=lss PE=1 SV=2
O31976 2.11e-10 12 126 1564 1678
SPbeta prophage-derived uncharacterized transglycosylase YomI OS=Bacillus subtilis (strain 168) OX=224308 GN=yomI PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000086 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003691_02548.