dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000001491_01549

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Basic Information help

Species

Rubeoparvulum massiliense

Lineage

Bacteria; Firmicutes; Bacilli; Rubeoparvulales; Rubeoparvulaceae; Rubeoparvulum; Rubeoparvulum massiliense

CAZyme ID

MGYG000001491_01549

CAZy Family

CBM50

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
553		61102.58	8.8448

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001491	2843796	Isolate	not provided	not provided

Gene Location

Start: 516291; End: 517952 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000001491_01549.

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam01551	Peptidase_M23	2.52e-47	454	549	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.
COG0739	NlpD	5.33e-46	295	552	3	260	Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
cd12797	M23_peptidase	6.72e-42	456	540	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.
PRK10871	nlpD	9.36e-24	286	550	53	313	murein hydrolase activator NlpD.
COG4942	EnvC	1.37e-22	401	549	261	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
AWX59068.1	6.76e-119	77	550	36	494
QRG67663.1	2.69e-118	77	550	36	494
ASJ56529.1	1.07e-117	77	550	36	494
ATF16429.1	4.25e-117	77	550	36	494
VEF92616.1	2.39e-116	77	550	36	494

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SLU_A	2.16e-20	444	550	228	339	Crystalstructure of NMB0315 [Neisseria meningitidis ATCC 13091],3SLU_B Crystal structure of NMB0315 [Neisseria meningitidis ATCC 13091]
6MUK_A	2.96e-20	444	550	248	359	1.93Angstrom Resolution Crystal Structure of Peptidase M23 from Neisseria gonorrhoeae. [Neisseria gonorrhoeae FA 1090]
5J1L_A	2.56e-18	456	550	65	161	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]
6JMX_A	3.44e-15	432	551	120	244	ChainA, Peptidase M23 [Campylobacter jejuni],6JMY_A Chain A, Peptidase M23 [Campylobacter jejuni],6KV1_A Chain A, Peptidase M23 [Campylobacter jejuni]
6JN1_A	6.14e-14	432	551	120	244	ChainA, 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
P0ADA4	1.45e-17	286	550	113	373	Murein hydrolase activator NlpD OS=Shigella flexneri OX=623 GN=nlpD PE=3 SV=1
P0ADA3	1.45e-17	286	550	113	373	Murein hydrolase activator NlpD OS=Escherichia coli (strain K12) OX=83333 GN=nlpD PE=1 SV=1
Q56131	1.91e-16	256	550	72	367	Murein hydrolase activator NlpD OS=Salmonella typhi OX=90370 GN=nlpD PE=3 SV=2
P44693	3.72e-16	456	550	348	443	Uncharacterized metalloprotease HI_0409 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_0409 PE=3 SV=1
P39700	4.76e-16	264	550	84	371	Murein hydrolase activator NlpD OS=Salmonella dublin OX=98360 GN=nlpD PE=2 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
1.000051	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations download full data without filtering help

start	end
83	105