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CAZyme Information: MGYG000001508_00853

You are here: Home > Sequence: MGYG000001508_00853

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 Thalassobacillus devorans
Lineage Bacteria; Firmicutes; Bacilli; Bacillales_D; Halobacillaceae; Thalassobacillus; Thalassobacillus devorans
CAZyme ID MGYG000001508_00853
CAZy Family GH23
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
366 40372.61 4.6447
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001508 4066265 Isolate not provided not provided
Gene Location Start: 485592;  End: 486692  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001508_00853.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd16891 CwlT-like 9.36e-65 71 219 1 150
CwlT-like N-terminal lysozyme domain and similar domains. CwlT is a bifunctional cell wall hydrolase containing an N-terminal lysozyme domain and a C-terminal NlpC/P60 endopeptidase domain (gamma-d-D-glutamyl-L-diamino acid endopeptidase), and has been implicated in the spread of transposons. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).
pfam13702 Lysozyme_like 4.62e-57 65 219 1 165
Lysozyme-like.
COG0739 NlpD 1.89e-36 245 365 146 265
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
pfam01551 Peptidase_M23 2.39e-32 261 360 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 1.52e-30 262 348 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
AKG05329.1 2.40e-257 1 366 1 366
QAS52333.1 1.97e-256 1 366 1 366
CCG47040.1 2.80e-256 1 366 1 366
ASF40976.1 2.80e-256 1 366 1 366
CCG44007.1 9.15e-230 1 366 1 366

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4FDY_A 2.67e-30 46 219 4 178
ChainA, Similar to lipoprotein, NLP/P60 family [Staphylococcus aureus subsp. aureus Mu50],4FDY_B Chain B, Similar to lipoprotein, NLP/P60 family [Staphylococcus aureus subsp. aureus Mu50]
4HPE_A 1.27e-22 64 228 20 186
ChainA, Putative cell wall hydrolase Tn916-like,CTn1-Orf17 [Clostridioides difficile 630],4HPE_B Chain B, Putative cell wall hydrolase Tn916-like,CTn1-Orf17 [Clostridioides difficile 630],4HPE_C Chain C, Putative cell wall hydrolase Tn916-like,CTn1-Orf17 [Clostridioides difficile 630],4HPE_D Chain D, Putative cell wall hydrolase Tn916-like,CTn1-Orf17 [Clostridioides difficile 630],4HPE_E Chain E, Putative cell wall hydrolase Tn916-like,CTn1-Orf17 [Clostridioides difficile 630],4HPE_F Chain F, Putative cell wall hydrolase Tn916-like,CTn1-Orf17 [Clostridioides difficile 630]
4QP5_A 1.41e-17 248 364 19 136
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 1.26e-16 248 364 17 134
NMRsolution structure of lysostaphin [Staphylococcus simulans]
4LXC_A 1.47e-16 248 364 19 136
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P96645 3.89e-43 61 258 50 229
Probable endopeptidase YddH OS=Bacillus subtilis (strain 168) OX=224308 GN=yddH PE=3 SV=1
O34636 8.01e-26 64 229 48 212
Uncharacterized membrane protein YocA OS=Bacillus subtilis (strain 168) OX=224308 GN=yocA PE=4 SV=1
O31976 1.72e-19 71 364 1422 1678
SPbeta prophage-derived uncharacterized transglycosylase YomI OS=Bacillus subtilis (strain 168) OX=224308 GN=yomI PE=3 SV=2
O64046 1.72e-19 71 364 1422 1678
Probable tape measure protein OS=Bacillus phage SPbeta OX=66797 GN=yomI PE=3 SV=1
P10547 4.74e-15 248 364 265 382
Lysostaphin OS=Staphylococcus simulans OX=1286 GN=lss PE=1 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
1.000031 0.000003 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      download full data without filtering help

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