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CAZyme Information: MGYG000003374_01413

You are here: Home > Sequence: MGYG000003374_01413

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 bivia
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella bivia
CAZyme ID MGYG000003374_01413
CAZy Family GH73
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
331 MGYG000003374_56|CGC1 38348.9 9.5612
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003374 2286602 MAG United States North America
Gene Location Start: 37687;  End: 38682  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003374_01413.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH73 190 321 6.9e-33 0.984375

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG1705 FlgJ 7.34e-34 183 328 44 191
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility].
NF038016 sporang_Gsm 7.20e-26 182 325 160 312
sporangiospore maturation cell wall hydrolase GsmA. The peptidoglycan-hydrolyzing enzyme GsmA occurs in some sporangia-forming members of the Actinobacteria, such as Actinoplanes missouriensis, and is required for proper separation of spores. GsmA proteins have one or two SH3 domains N-terminal to the hydrolase domain.
COG0739 NlpD 5.39e-24 18 161 116 264
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
cd12797 M23_peptidase 2.29e-23 63 143 1 83
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.
pfam01551 Peptidase_M23 1.14e-22 61 154 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ALO49101.1 5.14e-155 4 330 5 336
AUI56481.1 5.65e-152 5 330 6 336
AUI55521.1 6.55e-151 5 330 6 336
QNT65385.1 4.64e-150 5 330 3 332
QUB78218.1 8.68e-125 21 330 26 335

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6UE4_A 1.50e-14 38 150 239 355
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 1.52e-14 38 150 236 352
ShyAendopeptidase from Vibrio cholera (open form) [Vibrio cholerae]
6JMX_A 6.70e-13 17 158 107 246
ChainA, Peptidase M23 [Campylobacter jejuni],6JMY_A Chain A, Peptidase M23 [Campylobacter jejuni],6KV1_A Chain A, Peptidase M23 [Campylobacter jejuni]
6JN1_A 1.29e-11 17 158 107 246
ChainA, Peptidase M23 [Campylobacter jejuni]
6JN0_A 1.30e-11 17 158 107 246
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
P44693 4.48e-13 52 155 337 443
Uncharacterized metalloprotease HI_0409 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_0409 PE=3 SV=1
P0AFS9 1.00e-12 44 155 294 408
Murein DD-endopeptidase MepM OS=Escherichia coli (strain K12) OX=83333 GN=mepM PE=1 SV=1
P0AFT0 1.00e-12 44 155 294 408
Murein DD-endopeptidase MepM OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=mepM PE=3 SV=1
P0AFT1 1.00e-12 44 155 294 408
Murein DD-endopeptidase MepM OS=Shigella flexneri OX=623 GN=mepM PE=3 SV=1
Q8K9M4 1.25e-12 40 181 267 412
Uncharacterized metalloprotease BUsg_310 OS=Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) OX=198804 GN=BUsg_310 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000212 0.999202 0.000163 0.000141 0.000142 0.000128

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003374_01413.