dbCAN-seq: a database of CAZyme sequence and annotation

You are browsing environment: HUMAN GUT

help

CAZyme Information: MGYG000001438_02401

You are here: Home > Sequence: MGYG000001438_02401

Basic Information help

Species

Paenisporosarcina sp000411295

Lineage

Bacteria; Firmicutes; Bacilli; Bacillales_A; Planococcaceae; Paenisporosarcina; Paenisporosarcina sp000411295

CAZyme ID

MGYG000001438_02401

CAZy Family

CBM50

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
491	MGYG000001438_1\|CGC16	54016.06	7.2954

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001438	3493887	Isolate	not provided	not provided

Gene Location

Start: 2468530; End: 2470005 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000001438_02401.

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0739	NlpD	7.12e-45	230	490	2	262	Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
pfam01551	Peptidase_M23	4.73e-41	390	485	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	2.29e-37	392	476	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.
PRK11649	PRK11649	1.68e-20	232	486	98	407	putative peptidase; Provisional
PRK10871	nlpD	1.75e-19	373	489	202	316	murein hydrolase activator NlpD.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QBP42899.1	2.36e-237	1	491	1	492
AYC28401.1	1.35e-192	1	490	1	489
ALC87164.1	3.61e-191	1	490	1	493
QEY21410.1	3.88e-190	20	489	20	490
QGM31923.1	5.50e-190	20	489	20	490

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SLU_A	8.70e-21	390	486	244	339	Crystalstructure of NMB0315 [Neisseria meningitidis ATCC 13091],3SLU_B Crystal structure of NMB0315 [Neisseria meningitidis ATCC 13091]
6MUK_A	1.18e-20	390	486	264	359	1.93Angstrom Resolution Crystal Structure of Peptidase M23 from Neisseria gonorrhoeae. [Neisseria gonorrhoeae FA 1090]
5KVP_A	1.27e-17	357	476	1	125	Solutionstructure of the catalytic domain of zoocin A [Streptococcus equi subsp. zooepidemicus]
6JMX_A	1.39e-16	345	491	97	248	ChainA, Peptidase M23 [Campylobacter jejuni],6JMY_A Chain A, Peptidase M23 [Campylobacter jejuni],6KV1_A Chain A, Peptidase M23 [Campylobacter jejuni]
6JN7_A	2.85e-15	345	491	97	248	ChainA, Peptidase M23 [Campylobacter jejuni],6JN7_B Chain B, Peptidase M23 [Campylobacter jejuni],6JN7_C Chain C, Peptidase M23 [Campylobacter jejuni],6JN8_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
P39700	8.91e-16	231	489	120	374	Murein hydrolase activator NlpD OS=Salmonella dublin OX=98360 GN=nlpD PE=2 SV=2
P0ADA3	9.05e-16	222	489	113	376	Murein hydrolase activator NlpD OS=Escherichia coli (strain K12) OX=83333 GN=nlpD PE=1 SV=1
P0ADA4	9.05e-16	222	489	113	376	Murein hydrolase activator NlpD OS=Shigella flexneri OX=623 GN=nlpD PE=3 SV=1
Q56131	2.08e-15	231	489	116	370	Murein hydrolase activator NlpD OS=Salmonella typhi OX=90370 GN=nlpD PE=3 SV=2
P40827	2.14e-15	231	489	120	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 SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.041403	0.954979	0.002738	0.000406	0.000254	0.000202

TMHMM Annotations help

There is no transmembrane helices in MGYG000001438_02401.