dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000002532_03079

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Basic Information help

Species

Enterovibrio hollisae

Lineage

Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Vibrionaceae; Enterovibrio; Enterovibrio hollisae

CAZyme ID

MGYG000002532_03079

CAZy Family

CBM50

CAZyme Description

Murein DD-endopeptidase MepM

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
426		48150.11	10.0305

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002532	4096279	Isolate	not provided	not provided

Gene Location

Start: 3387036; End: 3388316 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000002532_03079.

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK11649	PRK11649	3.18e-97	31	425	61	438	putative peptidase; Provisional
COG0739	NlpD	2.17e-48	199	398	60	265	Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
pfam01551	Peptidase_M23	1.42e-45	295	390	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.
cd12797	M23_peptidase	7.40e-39	297	381	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	1.14e-14	269	390	300	414	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
AJR05159.1	5.61e-164	13	420	51	456
QSV16209.1	1.24e-163	13	424	13	422
QIJ86911.1	2.04e-162	20	424	1	404
QOU32679.1	2.04e-162	20	424	1	404
QFT39345.1	3.96e-162	21	424	1	403

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6UE4_A	4.08e-154	43	424	14	393	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	4.53e-154	43	424	11	390	ShyAendopeptidase from Vibrio cholera (open form) [Vibrio cholerae]
2GU1_A	3.01e-119	75	417	10	352	Crystalstructure of a zinc containing peptidase from vibrio cholerae [Vibrio cholerae]
3SLU_A	2.38e-24	76	396	18	344	Crystalstructure of NMB0315 [Neisseria meningitidis ATCC 13091],3SLU_B Crystal structure of NMB0315 [Neisseria meningitidis ATCC 13091]
6JMX_A	1.16e-22	295	391	147	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
P0AFS9	3.27e-77	32	409	49	426	Murein DD-endopeptidase MepM OS=Escherichia coli (strain K12) OX=83333 GN=mepM PE=1 SV=1
P0AFT1	3.27e-77	32	409	49	426	Murein DD-endopeptidase MepM OS=Shigella flexneri OX=623 GN=mepM PE=3 SV=1
P0AFT0	3.27e-77	32	409	49	426	Murein DD-endopeptidase MepM OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=mepM PE=3 SV=1
P44693	2.43e-67	73	400	129	452	Uncharacterized metalloprotease HI_0409 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_0409 PE=3 SV=1
Q8K9M4	4.95e-46	73	411	77	405	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
0.992076	0.007479	0.000102	0.000035	0.000021	0.000314

TMHMM Annotations download full data without filtering help

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