CAZyme Information: MGYG000002592_00145

Basic Information

• Species: Alistipes sp902388705
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp902388705
• CAZyme ID: MGYG000002592_00145
• CAZy Family: CBM50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
349		38774.68	8.1248

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002592	2965227	MAG	China	Asia

• Gene Location: Start: 160130; End: 161179 Strand: -

Full Sequence      

MAAVAALTASAGAPQPDAPQADSLHIAALSPEESAAVDSIAALRLRLQPKQIESIFDTNG
LTVIDTLDSGNDAVQVVLYSNNTWKYIRNREVAKDSTIFEKYWDTTTLFPYKDADMSGMP
KSVVIDLIDSTTSYHCPYQGSVHPRGKYGPRRRRQHQGVDLPLKMGDPVYATFCGRVRIS
QYNKGGYGNLVIIRHDNGLETYYGHLSERMVEPGQWVEAGQIIGLGGSSGRSTGPHLHFE
TRYYGQSFDPERLIDFKSGMLCRETFLLKKSFFSIYSNAGQDFDDEIANEEQDKKEAAEK
AAMQYHRIKSGDTLGAIARKYGTTVTNICRLNGIKSTTTLRIGRSLRVR

Enzyme Prediction     

No EC number prediction in MGYG000002592_00145.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam01551	Peptidase_M23	4.74e-43	154	250	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	3.28e-37	152	258	159	268	Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
cd12797	M23_peptidase	4.07e-37	156	240	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	4.11e-21	156	240	313	396	putative peptidase; Provisional
PRK10871	nlpD	4.10e-15	157	252	220	314	murein hydrolase activator NlpD.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BBL02665.1	1.00e-233	1	349	9	356
BBL13339.1	1.42e-233	1	349	9	356
BBL10545.1	1.42e-233	1	349	9	356
AFL79509.1	7.94e-229	1	349	1	348
BBL07760.1	1.50e-171	30	349	82	399

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5J1L_A	3.28e-23	114	250	21	160	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	2.47e-20	154	250	244	338	Crystalstructure of NMB0315 [Neisseria meningitidis ATCC 13091],3SLU_B Crystal structure of NMB0315 [Neisseria meningitidis ATCC 13091]
6MUK_A	3.22e-20	154	250	264	358	1.93Angstrom Resolution Crystal Structure of Peptidase M23 from Neisseria gonorrhoeae. [Neisseria gonorrhoeae FA 1090]
5J1L_B	4.76e-16	150	254	31	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]
6JMX_A	6.58e-16	156	258	149	247	ChainA, Peptidase M23 [Campylobacter jejuni],6JMY_A Chain A, Peptidase M23 [Campylobacter jejuni],6KV1_A Chain A, Peptidase M23 [Campylobacter jejuni]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P44693	9.06e-19	137	264	322	458	Uncharacterized metalloprotease HI_0409 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_0409 PE=3 SV=1
O64046	1.63e-14	147	252	1567	1676	Probable tape measure protein OS=Bacillus phage SPbeta OX=66797 GN=yomI PE=3 SV=1
O31976	1.63e-14	147	252	1567	1676	SPbeta prophage-derived uncharacterized transglycosylase YomI OS=Bacillus subtilis (strain 168) OX=224308 GN=yomI PE=3 SV=2
P0AFT0	1.98e-14	156	250	314	407	Murein DD-endopeptidase MepM OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=mepM PE=3 SV=1
P0AFT1	1.98e-14	156	250	314	407	Murein DD-endopeptidase MepM OS=Shigella flexneri OX=623 GN=mepM PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000011	0.000041	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002592_00145.