dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000004536_00142

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Basic Information help

Species

Alistipes sp900542505

Lineage

Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp900542505

CAZyme ID

MGYG000004536_00142

CAZy Family

CBM50

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
403		45508.41	8.2179

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004536	2335647	MAG	Israel	Asia

Gene Location

Start: 171230; End: 172441 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000004536_00142.

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam01551	Peptidase_M23	5.53e-43	210	304	3	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	7.48e-38	210	294	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.
COG0739	NlpD	1.26e-34	210	312	163	268	Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
PRK11649	PRK11649	6.28e-19	209	294	312	396	putative peptidase; Provisional
PRK10871	nlpD	1.12e-16	211	306	220	314	murein hydrolase activator NlpD.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BBL07760.1	1.31e-186	5	403	2	399
BBL02665.1	1.25e-183	79	403	27	356
BBL13339.1	1.25e-183	79	403	27	356
BBL10545.1	1.25e-183	79	403	27	356
AFL79509.1	4.16e-180	79	403	19	348

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5J1L_A	2.23e-21	210	304	65	160	Crystalstructure of Csd1-Csd2 dimer I [Helicobacter pylori 26695],5J1L_C Crystal structure of Csd1-Csd2 dimer I [Helicobacter pylori 26695],5J1M_A Crystal structure of Csd1-Csd2 dimer II [Helicobacter pylori 26695],5J1M_C Crystal structure of Csd1-Csd2 dimer II [Helicobacter pylori 26695]
3SLU_A	2.19e-19	204	304	240	338	Crystalstructure of NMB0315 [Neisseria meningitidis ATCC 13091],3SLU_B Crystal structure of NMB0315 [Neisseria meningitidis ATCC 13091]
6MUK_A	2.83e-19	204	304	260	358	1.93Angstrom Resolution Crystal Structure of Peptidase M23 from Neisseria gonorrhoeae. [Neisseria gonorrhoeae FA 1090]
5J1L_B	3.37e-15	212	329	48	170	Crystalstructure of Csd1-Csd2 dimer I [Helicobacter pylori 26695],5J1L_D Crystal structure of Csd1-Csd2 dimer I [Helicobacter pylori 26695],5J1M_B Crystal structure of Csd1-Csd2 dimer II [Helicobacter pylori 26695],5J1M_D Crystal structure of Csd1-Csd2 dimer II [Helicobacter pylori 26695]
5J1K_A	5.65e-15	212	329	67	189	Crystalstructure of Csd2-Csd2 dimer [Helicobacter pylori 26695]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P44693	1.09e-16	206	304	344	442	Uncharacterized metalloprotease HI_0409 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_0409 PE=3 SV=1
P47764	1.86e-14	214	308	1	94	Lipoprotein NlpD (Fragment) OS=Yersinia enterocolitica OX=630 GN=nlpD PE=3 SV=1
Q56131	5.71e-14	202	308	266	370	Murein hydrolase activator NlpD OS=Salmonella typhi OX=90370 GN=nlpD PE=3 SV=2
P39700	5.85e-14	202	308	270	374	Murein hydrolase activator NlpD OS=Salmonella dublin OX=98360 GN=nlpD PE=2 SV=2
P40827	5.85e-14	202	308	270	374	Murein hydrolase activator NlpD OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=nlpD PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.002977	0.399792	0.596095	0.000503	0.000346	0.000283

TMHMM Annotations download full data without filtering help

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