CAZyme Information: MGYG000000083_03499

Basic Information

• Species: Peribacillus simplex
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales_B; DSM-1321; Peribacillus; Peribacillus simplex
• CAZyme ID: MGYG000000083_03499
• CAZy Family: CBM50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
472		52669.77	4.464

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000083	5860218	Isolate	United Kingdom	Europe

• Gene Location: Start: 558201; End: 559619 Strand: -

Full Sequence      

MFSLKGKGIILLMVSVILVLAGNRATAAGLSETTTIHHVYLNDEFVGSVTDETEIEKIVA
DKVEEAQDDYPDFTFDRESQLTFVPEEVFDEKVKEDEAVKGIQDQLNVKAEAYEIDIDNQ
AVAYVASKDDAEDVLKKITLLYVNEEEYAEYESGNKDSEKDADSLKEPGSRILDIQFSHP
FTFKETMVNPDEIKSVDKTLSMIEEGKEETTIYEAKEDEELEAIATRHDMDLDQLLELNP
GQDENKGVKEGERLYVTQRTPYVNVMVEREVFKEERIPFEKKVKEDDELPKGELITEQIG
NEGILAFTYNVSETNGKKISETIVNKEVTEKAKTEITRKGTKVIPSQGSGTYSWPADGGY
ISSKQGQRWGKLHKGIDIARPTTRTITAADHGIIETAGNSGGYGNKITINHNNGYKTVYA
HLDSIDVTAGQKVEKGMKIGMMGSTGHSTGVHLHFEIYKNGSLVNPLNYISQ

Enzyme Prediction     

No EC number prediction in MGYG000000083_03499.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0739	NlpD	1.81e-43	212	471	3	262	Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
pfam01551	Peptidase_M23	8.38e-41	373	466	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	7.17e-36	373	457	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	1.50e-27	316	472	164	318	murein hydrolase activator NlpD.
PRK11649	PRK11649	1.45e-21	373	467	313	407	putative peptidase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QYF83140.1	7.34e-308	1	472	1	472
QOS91780.1	1.55e-277	1	472	1	473
AND42644.1	1.05e-131	18	472	36	493
QOK26190.1	2.10e-131	18	472	36	493
SQI63726.1	1.68e-126	3	469	10	476

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SLU_A	1.24e-18	371	468	244	340	Crystalstructure of NMB0315 [Neisseria meningitidis ATCC 13091],3SLU_B Crystal structure of NMB0315 [Neisseria meningitidis ATCC 13091]
6MUK_A	1.61e-18	371	468	264	360	1.93Angstrom Resolution Crystal Structure of Peptidase M23 from Neisseria gonorrhoeae. [Neisseria gonorrhoeae FA 1090]
5J1L_A	1.95e-16	373	469	65	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	4.33e-16	373	472	149	248	ChainA, Peptidase M23 [Campylobacter jejuni],6JMY_A Chain A, Peptidase M23 [Campylobacter jejuni],6KV1_A Chain A, Peptidase M23 [Campylobacter jejuni]
6JN1_A	7.87e-15	373	472	149	248	ChainA, Peptidase M23 [Campylobacter jejuni]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q56131	1.26e-17	318	472	220	372	Murein hydrolase activator NlpD OS=Salmonella typhi OX=90370 GN=nlpD PE=3 SV=2
P40827	1.30e-17	318	472	224	376	Murein hydrolase activator NlpD OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=nlpD PE=3 SV=2
P39700	1.30e-17	318	472	224	376	Murein hydrolase activator NlpD OS=Salmonella dublin OX=98360 GN=nlpD PE=2 SV=2
P0ADA3	2.40e-17	351	472	259	378	Murein hydrolase activator NlpD OS=Escherichia coli (strain K12) OX=83333 GN=nlpD PE=1 SV=1
P0ADA4	2.40e-17	351	472	259	378	Murein hydrolase activator NlpD OS=Shigella flexneri OX=623 GN=nlpD PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000430	0.998675	0.000382	0.000162	0.000161	0.000156

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000083_03499.