dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000001713_02608

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Basic Information help

Species

Vibrio furnissii

Lineage

Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Vibrionaceae; Vibrio; Vibrio furnissii

CAZyme ID

MGYG000001713_02608

CAZy Family

CBM50

CAZyme Description

Murein DD-endopeptidase MepM

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
437	MGYG000001713_14\|CGC9	48824.48	9.846

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001713	4958658	Isolate	Japan	Asia

Gene Location

Start: 594438; End: 595751 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000001713_02608.

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK11649	PRK11649	1.24e-98	48	415	79	432	putative peptidase; Provisional
COG0739	NlpD	7.95e-53	72	398	2	266	Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
pfam01551	Peptidase_M23	5.32e-47	295	388	2	95	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	1.51e-41	296	380	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.
COG4942	EnvC	5.28e-15	270	388	279	413	Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning].

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QTH06511.1	1.38e-292	1	437	1	437
QKE36659.1	1.38e-292	1	437	1	437
QTG93693.1	1.38e-292	1	437	1	437
QUF70707.1	1.38e-292	1	437	1	437
QTH10510.1	1.38e-292	1	437	1	437

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6UE4_A	5.84e-219	33	428	2	398	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	1.31e-218	36	428	2	395	ShyAendopeptidase from Vibrio cholera (open form) [Vibrio cholerae]
2GU1_A	8.08e-130	74	416	10	352	Crystalstructure of a zinc containing peptidase from vibrio cholerae [Vibrio cholerae]
3SLU_A	4.19e-25	76	420	19	368	Crystalstructure of NMB0315 [Neisseria meningitidis ATCC 13091],3SLU_B Crystal structure of NMB0315 [Neisseria meningitidis ATCC 13091]
6JMX_A	5.93e-25	296	390	149	243	ChainA, Peptidase M23 [Campylobacter jejuni],6JMY_A Chain A, Peptidase M23 [Campylobacter jejuni],6KV1_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
P0AFT1	2.09e-78	72	415	96	433	Murein DD-endopeptidase MepM OS=Shigella flexneri OX=623 GN=mepM PE=3 SV=1
P0AFT0	2.09e-78	72	415	96	433	Murein DD-endopeptidase MepM OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=mepM PE=3 SV=1
P0AFS9	2.09e-78	72	415	96	433	Murein DD-endopeptidase MepM OS=Escherichia coli (strain K12) OX=83333 GN=mepM PE=1 SV=1
P44693	5.26e-70	72	419	129	473	Uncharacterized metalloprotease HI_0409 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_0409 PE=3 SV=1
Q8K9M4	4.71e-44	59	408	64	403	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 OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.743549	0.229353	0.022827	0.001032	0.000793	0.002450

TMHMM Annotations help

There is no transmembrane helices in MGYG000001713_02608.