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CAZyme Information: MGYG000000025_02647

You are here: Home > Sequence: MGYG000000025_02647

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 Staphylococcus nepalensis
Lineage Bacteria; Firmicutes; Bacilli; Staphylococcales; Staphylococcaceae; Staphylococcus; Staphylococcus nepalensis
CAZyme ID MGYG000000025_02647
CAZy Family GH19
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
674 73685.95 4.1258
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000025 2822370 Isolate United Kingdom Europe
Gene Location Start: 4598;  End: 6622  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000025_02647.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH19 385 500 4.9e-19 0.4935064935064935

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK06347 PRK06347 4.29e-28 95 318 316 591
1,4-beta-N-acetylmuramoylhydrolase.
cd12797 M23_peptidase 3.56e-27 562 648 1 84
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 5.89e-27 561 655 2 93
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.
PRK06347 PRK06347 3.18e-24 12 262 291 591
1,4-beta-N-acetylmuramoylhydrolase.
COG3179 COG3179 4.20e-24 351 518 3 199
Predicted chitinase [General function prediction only].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ASB55626.1 1.27e-172 5 523 9 556
BAI83666.2 1.27e-172 5 523 9 556
QAW02787.1 1.27e-172 5 523 9 556
AYK78650.1 1.27e-172 5 523 9 556
ARI86935.1 1.27e-172 5 523 9 556

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4QP5_A 3.38e-41 531 670 2 140
Catalyticdomain of the antimicrobial peptidase lysostaphin from Staphylococcus simulans crystallized in the presence of phosphate [Staphylococcus simulans bv. staphylolyticus],4QP5_B Catalytic domain of the antimicrobial peptidase lysostaphin from Staphylococcus simulans crystallized in the presence of phosphate [Staphylococcus simulans bv. staphylolyticus],4QPB_A Catalytic domain of the antimicrobial peptidase lysostaphin from Staphylococcus simulans crystallized in the absence of phosphate [Staphylococcus simulans],4QPB_B Catalytic domain of the antimicrobial peptidase lysostaphin from Staphylococcus simulans crystallized in the absence of phosphate [Staphylococcus simulans]
5NMY_A 5.39e-40 533 670 2 138
NMRsolution structure of lysostaphin [Staphylococcus simulans]
4LXC_A 9.73e-40 531 670 2 140
Theantimicrobial peptidase lysostaphin from Staphylococcus simulans [Staphylococcus simulans],4LXC_B The antimicrobial peptidase lysostaphin from Staphylococcus simulans [Staphylococcus simulans],4LXC_C The antimicrobial peptidase lysostaphin from Staphylococcus simulans [Staphylococcus simulans],4LXC_D The antimicrobial peptidase lysostaphin from Staphylococcus simulans [Staphylococcus simulans]
6RK4_A 1.40e-37 531 670 248 386
LysostaphinSH3b P4-G5 complex, synchrotron dataset [Staphylococcus simulans]
5KQB_A 1.39e-32 545 669 12 135
Identificationand structural characterization of LytU [Staphylococcus aureus],5KQC_A Identification and structural characterization of LytU [Staphylococcus aureus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P10547 7.65e-37 531 670 248 386
Lysostaphin OS=Staphylococcus simulans OX=1286 GN=lss PE=1 SV=2
P10548 2.14e-36 531 670 235 373
Lysostaphin OS=Staphylococcus staphylolyticus OX=1287 GN=lss PE=3 SV=1
O05156 1.97e-35 537 673 125 260
Glycyl-glycine endopeptidase ALE-1 OS=Staphylococcus capitis OX=29388 PE=1 SV=1
Q6GK35 1.12e-29 447 667 95 314
Glycyl-glycine endopeptidase LytM OS=Staphylococcus aureus (strain MRSA252) OX=282458 GN=lytM PE=3 SV=1
A0A0H3K6J4 1.30e-28 528 667 179 314
Glycyl-glycine endopeptidase LytM OS=Staphylococcus aureus (strain Newman) OX=426430 GN=lytM 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
0.999463 0.000553 0.000004 0.000001 0.000000 0.000001

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000025_02647.