CAZyme Information: MGYG000000128_02162

Basic Information

• Species: Alistipes sp902363575
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp902363575
• CAZyme ID: MGYG000000128_02162
• CAZy Family: CBM50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
354		39880.44	9.1226

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000128	2906288	Isolate	Canada	North America

• Gene Location: Start: 18674; End: 19738 Strand: +

Full Sequence      

MKLRHMIALMLAAGVSATAAAQNINRVRELLEEMQQEVEMIEKRQAETATVVPVKTEPVE
SVADTNGVLPLDTLPTMNDAVKIVIYNDNTWKYMRDRQYVKDSAVYVQYWDTTTLFPYRD
VTLASLPASVAIDLVDSLKCYHYPGKGKLRSKYGPRRRRQHQGVDIPLKMGEPVYAVFNG
RVRISQYNRGGYGNLVVIRHDNGLETFSGHLSERLVQSGDWVEAGQIIGFCGSTGRSTGP
HLHFETRYCGQTFDPERLIDFESGNLRRQTFLLKKSFFDIRSNMAQDFEDEISLAEEDQK
AAAEKAAMAYHKIRSGDTLGAIAQRYGTTVSKLCSLNGITSKTTLRIGRTLRVR

Enzyme Prediction     

No EC number prediction in MGYG000000128_02162.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam01551	Peptidase_M23	7.42e-42	159	255	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	1.01e-39	137	267	130	272	Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
cd12797	M23_peptidase	6.41e-38	161	245	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.
PRK11649	PRK11649	6.75e-20	148	245	293	396	putative peptidase; Provisional
PRK10871	nlpD	3.59e-14	162	257	220	314	murein hydrolase activator NlpD.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BBL05143.1	1.18e-162	1	354	1	359
BBL14649.1	1.67e-162	1	354	1	359
BBL02665.1	5.33e-151	13	354	13	356
BBL13339.1	5.33e-151	13	354	13	356
BBL10545.1	5.33e-151	13	354	13	356

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5J1L_A	3.33e-21	161	267	65	169	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	4.92e-20	159	255	244	338	Crystalstructure of NMB0315 [Neisseria meningitidis ATCC 13091],3SLU_B Crystal structure of NMB0315 [Neisseria meningitidis ATCC 13091]
6MUK_A	6.37e-20	159	255	264	358	1.93Angstrom Resolution Crystal Structure of Peptidase M23 from Neisseria gonorrhoeae. [Neisseria gonorrhoeae FA 1090]
5KVP_A	3.30e-15	161	245	34	124	Solutionstructure of the catalytic domain of zoocin A [Streptococcus equi subsp. zooepidemicus]
4QP5_A	5.51e-15	161	245	33	118	Catalyticdomain of the antimicrobial peptidase lysostaphin from Staphylococcus simulans crystallized in the presence of phosphate [Staphylococcus simulans bv. staphylolyticus],4QP5_B Catalytic domain of the antimicrobial peptidase lysostaphin from Staphylococcus simulans crystallized in the presence of phosphate [Staphylococcus simulans bv. staphylolyticus],4QPB_A Catalytic domain of the antimicrobial peptidase lysostaphin from Staphylococcus simulans crystallized in the absence of phosphate [Staphylococcus simulans],4QPB_B Catalytic domain of the antimicrobial peptidase lysostaphin from Staphylococcus simulans crystallized in the absence of phosphate [Staphylococcus simulans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P44693	4.71e-17	141	274	321	465	Uncharacterized metalloprotease HI_0409 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_0409 PE=3 SV=1
O31976	3.12e-14	148	259	1563	1678	SPbeta prophage-derived uncharacterized transglycosylase YomI OS=Bacillus subtilis (strain 168) OX=224308 GN=yomI PE=3 SV=2
O64046	3.12e-14	148	259	1563	1678	Probable tape measure protein OS=Bacillus phage SPbeta OX=66797 GN=yomI PE=3 SV=1
P47764	6.92e-14	165	259	1	94	Lipoprotein NlpD (Fragment) OS=Yersinia enterocolitica OX=630 GN=nlpD PE=3 SV=1
P0AFS9	9.47e-13	148	255	294	407	Murein DD-endopeptidase MepM OS=Escherichia coli (strain K12) OX=83333 GN=mepM PE=1 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
0.010650	0.987570	0.001016	0.000279	0.000230	0.000226

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000128_02162.