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CAZyme Information: MGYG000000923_00293

You are here: Home > Sequence: MGYG000000923_00293

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 Phocaeicola sp900552645
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola sp900552645
CAZyme ID MGYG000000923_00293
CAZy Family GH73
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
522 56783.84 5.5284
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000923 2732014 MAG China Asia
Gene Location Start: 310282;  End: 311850  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000923_00293.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH73 14 145 6e-34 0.9765625

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
NF038016 sporang_Gsm 1.15e-33 2 149 157 312
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.
COG1705 FlgJ 8.37e-31 21 150 59 189
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility].
pfam01551 Peptidase_M23 6.14e-26 211 318 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.
COG0739 NlpD 2.28e-25 182 323 134 265
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
cd12797 M23_peptidase 3.47e-24 213 304 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUR43544.1 2.90e-223 1 519 1 513
QCQ31411.1 2.90e-223 1 519 1 513
QDM08698.1 2.90e-223 1 519 1 513
QQA07764.1 1.86e-222 4 519 3 516
SCV08209.1 7.52e-222 3 519 2 516

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5KQB_A 1.77e-10 213 327 29 137
Identificationand structural characterization of LytU [Staphylococcus aureus],5KQC_A Identification and structural characterization of LytU [Staphylococcus aureus]
6JMX_A 2.65e-10 140 324 82 248
ChainA, Peptidase M23 [Campylobacter jejuni],6JMY_A Chain A, Peptidase M23 [Campylobacter jejuni],6KV1_A Chain A, Peptidase M23 [Campylobacter jejuni]
6JN1_A 4.68e-09 140 324 82 248
ChainA, Peptidase M23 [Campylobacter jejuni]
6JN0_A 4.73e-09 140 324 82 248
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]
6JN7_A 5.08e-09 140 324 82 248
ChainA, Peptidase M23 [Campylobacter jejuni],6JN7_B Chain B, Peptidase M23 [Campylobacter jejuni],6JN7_C Chain C, Peptidase M23 [Campylobacter jejuni],6JN8_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
O32083 4.10e-10 23 151 66 200
Exo-glucosaminidase LytG OS=Bacillus subtilis (strain 168) OX=224308 GN=lytG PE=1 SV=1
P44693 7.86e-09 184 301 321 430
Uncharacterized metalloprotease HI_0409 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_0409 PE=3 SV=1
Q2G222 1.08e-06 25 157 340 480
N-acetylmuramoyl-L-alanine amidase domain-containing protein SAOUHSC_02979 OS=Staphylococcus aureus (strain NCTC 8325 / PS 47) OX=93061 GN=SAOUHSC_02979 PE=1 SV=1
Q8K9M4 1.08e-06 194 347 272 415
Uncharacterized metalloprotease BUsg_310 OS=Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) OX=198804 GN=BUsg_310 PE=3 SV=1
O05156 3.83e-06 213 339 150 270
Glycyl-glycine endopeptidase ALE-1 OS=Staphylococcus capitis OX=29388 PE=1 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
0.999625 0.000389 0.000002 0.000001 0.000000 0.000001

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000923_00293.