dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000000877_00140

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Basic Information help

Species

CAG-83 sp900545495

Lineage

Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; CAG-83; CAG-83 sp900545495

CAZyme ID

MGYG000000877_00140

CAZy Family

CBM50

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
577		64420.38	5.381

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000877	2052192	MAG	Netherlands	Europe

Gene Location

Start: 154169; End: 155902 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000000877_00140.

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0739	NlpD	5.30e-46	314	577	3	261	Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
pfam01551	Peptidase_M23	3.57e-41	478	573	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	1.00e-35	480	564	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	1.17e-25	314	577	62	316	murein hydrolase activator NlpD.
COG4942	EnvC	3.01e-24	450	577	295	418	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
BCK82550.1	1.28e-249	27	577	17	568
QUO34525.1	1.77e-231	17	577	12	573
BCK79529.1	5.75e-215	42	577	12	553
QNL44258.1	3.34e-191	62	577	47	561
QUO39608.1	4.19e-180	74	577	63	565

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5J1L_A	1.44e-16	446	576	36	163	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	2.22e-14	452	577	121	246	ChainA, Peptidase M23 [Campylobacter jejuni],6JMY_A Chain A, Peptidase M23 [Campylobacter jejuni],6KV1_A Chain A, Peptidase M23 [Campylobacter jejuni]
4BH5_A	6.04e-14	450	577	17	140	LytMdomain of EnvC, an activator of cell wall amidases in Escherichia coli [Escherichia coli K-12],4BH5_B LytM domain of EnvC, an activator of cell wall amidases in Escherichia coli [Escherichia coli K-12],4BH5_C LytM domain of EnvC, an activator of cell wall amidases in Escherichia coli [Escherichia coli K-12],4BH5_D LytM domain of EnvC, an activator of cell wall amidases in Escherichia coli [Escherichia coli K-12]
6JN1_A	3.94e-13	452	577	121	246	ChainA, Peptidase M23 [Campylobacter jejuni]
6JN0_A	4.00e-13	452	577	121	246	ChainA, Peptidase M23 [Campylobacter jejuni],7E60_A Chain A, Peptidase M23 [Campylobacter jejuni],7E61_A Chain A, Peptidase M23 [Campylobacter jejuni],7E63_A Chain A, Peptidase M23 [Campylobacter jejuni],7E63_B Chain B, Peptidase M23 [Campylobacter jejuni],7E64_A Chain A, Peptidase M23 [Campylobacter jejuni],7E65_A Chain A, Peptidase M23 [Campylobacter jejuni],7E65_B Chain B, Peptidase M23 [Campylobacter jejuni],7E66_A Chain A, Peptidase M23 [Campylobacter jejuni],7E67_A Chain A, Peptidase M23 [Campylobacter jejuni],7E69_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	2.51e-19	311	577	117	374	Murein hydrolase activator NlpD OS=Salmonella dublin OX=98360 GN=nlpD PE=2 SV=2
Q56131	3.23e-19	311	577	113	370	Murein hydrolase activator NlpD OS=Salmonella typhi OX=90370 GN=nlpD PE=3 SV=2
P40827	3.37e-19	311	577	117	374	Murein hydrolase activator NlpD OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=nlpD PE=3 SV=2
Q46798	5.70e-19	308	577	36	242	Uncharacterized lipoprotein YgeR OS=Escherichia coli (strain K12) OX=83333 GN=ygeR PE=3 SV=2
P0ADA3	1.50e-18	314	577	122	376	Murein hydrolase activator NlpD OS=Escherichia coli (strain K12) OX=83333 GN=nlpD PE=1 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
1.000068	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations download full data without filtering help

start	end
140	162