CAZyme Information: MGYG000000823_00303

Basic Information

• Species: Alistipes sp900550375
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp900550375
• CAZyme ID: MGYG000000823_00303
• CAZy Family: CBM50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
359		40825.21	8.3066

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000823	2131500	MAG	China	Asia

• Gene Location: Start: 59482; End: 60561 Strand: -

Full Sequence      

MKLRYLILTLLFAGTTAGLQAQSLDHMRKLLQEIQTEIDCLEKEQAETLKPQKEPQPVES
TEYINGVIAVDTLPSGNDAVMIVLFNDNTWKYLRNRDYVKDSEVYTRCWDTTKLFPYRET
VTLADLPRTVDIELVDSLKCYHYPYKANIRSKFGMRRRRKHQGVDLPLKMGDPIYASFNG
KVRISMPSSKSGGYGNLVVIRHDNGLETFYGHLSERIVHADEWVEAGQIIGYGGSTGRST
GPHLHFETRYCGQSFDPERLIDFQSGNLRRETFLLKKGYLDIHSNASQDFEDEEAEANDE
KKAEEARKALASAQYHKIRSGDTLGGIASRYGTSISRLCQLNGISRTTTLRIGRSLRVR

Enzyme Prediction     

No EC number prediction in MGYG000000823_00303.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam01551	Peptidase_M23	3.61e-40	159	257	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	3.56e-36	161	247	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.
COG0739	NlpD	1.65e-35	146	269	142	272	Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
PRK11649	PRK11649	6.29e-18	149	247	294	396	putative peptidase; Provisional
PRK10871	nlpD	8.95e-14	162	259	220	314	murein hydrolase activator NlpD.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BBL05143.1	5.11e-244	1	359	1	359
BBL14649.1	2.08e-243	1	359	1	359
BBL02665.1	6.89e-136	54	359	55	356
BBL13339.1	6.89e-136	54	359	55	356
BBL10545.1	6.89e-136	54	359	55	356

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5J1L_A	1.98e-23	161	269	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	1.28e-21	147	257	226	338	Crystalstructure of NMB0315 [Neisseria meningitidis ATCC 13091],3SLU_B Crystal structure of NMB0315 [Neisseria meningitidis ATCC 13091]
6MUK_A	1.71e-21	147	257	246	358	1.93Angstrom Resolution Crystal Structure of Peptidase M23 from Neisseria gonorrhoeae. [Neisseria gonorrhoeae FA 1090]
5KVP_A	1.43e-16	161	247	34	124	Solutionstructure of the catalytic domain of zoocin A [Streptococcus equi subsp. zooepidemicus]
5J1L_B	2.52e-15	163	261	48	145	Crystalstructure of Csd1-Csd2 dimer I [Helicobacter pylori 26695],5J1L_D Crystal structure of Csd1-Csd2 dimer I [Helicobacter pylori 26695],5J1M_B Crystal structure of Csd1-Csd2 dimer II [Helicobacter pylori 26695],5J1M_D Crystal structure of Csd1-Csd2 dimer II [Helicobacter pylori 26695]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P44693	1.74e-15	141	276	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
P47764	5.20e-14	165	261	1	94	Lipoprotein NlpD (Fragment) OS=Yersinia enterocolitica OX=630 GN=nlpD PE=3 SV=1
O64046	5.99e-13	116	261	1526	1678	Probable tape measure protein OS=Bacillus phage SPbeta OX=66797 GN=yomI PE=3 SV=1
O31976	5.99e-13	116	261	1526	1678	SPbeta prophage-derived uncharacterized transglycosylase YomI OS=Bacillus subtilis (strain 168) OX=224308 GN=yomI PE=3 SV=2
P10547	4.77e-12	139	247	263	364	Lysostaphin OS=Staphylococcus simulans OX=1286 GN=lss PE=1 SV=2

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
0.000409	0.998911	0.000191	0.000167	0.000161	0.000149

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000823_00303.