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CAZyme Information: MGYG000003152_02111

You are here: Home > Sequence: MGYG000003152_02111

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 denticola
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella denticola
CAZyme ID MGYG000003152_02111
CAZy Family GH19
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1047 118040.92 10.1548
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003152 2774939 MAG United States North America
Gene Location Start: 68713;  End: 71856  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003152_02111.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH19 582 775 4.1e-18 0.5454545454545454

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3179 COG3179 4.38e-19 565 721 7 131
Predicted chitinase [General function prediction only].
pfam14107 DUF4280 1.19e-15 23 125 1 109
Domain of unknown function (DUF4280). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 129 and 456 amino acids in length. There is a single completely conserved residue C that may be functionally important.
cd12797 M23_peptidase 1.31e-08 878 1002 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 7.38e-07 838 1013 135 259
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
pfam01551 Peptidase_M23 1.22e-06 876 1002 1 87
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUB90499.1 0.0 1 1047 1 1047
QUB76016.1 0.0 1 1047 1 1046
QUB70001.1 0.0 1 1045 1 1034
AUI55267.1 0.0 1 1045 1 1029
QUB81456.1 0.0 1 1047 1 1035

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4OK7_A 8.95e-07 601 721 54 151
ChainA, Endolysin [Salmonella phage SPN1S],4OK7_B Chain B, Endolysin [Salmonella phage SPN1S],4OK7_C Chain C, Endolysin [Salmonella phage SPN1S]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P44187 6.84e-11 571 720 10 128
Glycosyl hydrolase family 19 domain-containing protein HI_1415 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_1415 PE=3 SV=1

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
1.000055 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003152_02111.