CAZyme Information: MGYG000002394_02257

Basic Information

• Species: Prevotella rara
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella rara
• CAZyme ID: MGYG000002394_02257
• CAZy Family: GH73
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
331		36223.77	5.0041

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002394	3788330	Isolate	Russia	Europe

• Gene Location: Start: 3232; End: 4227 Strand: -

Full Sequence      

MFVTSPFGMRADPTTVGSGQVMHKGIDIRCNKDEVLATENNGKVVAVNQNINAPGGKSIT
VEYEREDGSKIQNVYMHLSVIDVKLGDTVQAGQKLGVSGNTGTRTTGEHLHFAVTQITAD
GSKRDVDPAIYLAEIAEKGNIETKALHDGNDLLAKYKADPAHAQRDSKVQSPEEWMKKLL
SSEDSGVGLSDSNDPIIDMVVTAFSSLMALAVIIDNKDEKSQLAAVSDMANRRTIDLTSL
LPNMKTCDIVVNEDNKAVLKADNGNVQFMRELSSNELSRLSVILNNPNLSDESKRMRIAG
MVNSIVLSYQVSENFEQCLSEQQNRNEQIRR

Enzyme Prediction     

No EC number prediction in MGYG000002394_02257.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd12797	M23_peptidase	2.80e-22	23	114	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.
COG0739	NlpD	5.29e-22	3	144	145	276	Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
pfam01551	Peptidase_M23	2.02e-21	22	128	2	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.
PRK11649	PRK11649	2.58e-08	3	119	294	409	putative peptidase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRO48520.1	9.00e-228	1	331	181	511
QRO50306.1	2.28e-166	1	331	183	512
QRM97292.1	2.08e-138	1	331	191	518
ALJ43574.1	2.08e-138	1	331	191	518
QUT68550.1	2.08e-138	1	331	191	518

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KQB_A	2.15e-12	23	112	29	113	Identificationand structural characterization of LytU [Staphylococcus aureus],5KQC_A Identification and structural characterization of LytU [Staphylococcus aureus]
6JMX_A	1.03e-08	2	134	130	248	ChainA, Peptidase M23 [Campylobacter jejuni],6JMY_A Chain A, Peptidase M23 [Campylobacter jejuni],6KV1_A Chain A, Peptidase M23 [Campylobacter jejuni]
4QP5_A	1.68e-08	13	112	23	117	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]
5NMY_A	2.18e-08	13	161	21	168	NMRsolution structure of lysostaphin [Staphylococcus simulans]
4LXC_A	2.38e-08	13	161	23	170	Theantimicrobial peptidase lysostaphin from Staphylococcus simulans [Staphylococcus simulans],4LXC_B The antimicrobial peptidase lysostaphin from Staphylococcus simulans [Staphylococcus simulans],4LXC_C The antimicrobial peptidase lysostaphin from Staphylococcus simulans [Staphylococcus simulans],4LXC_D The antimicrobial peptidase lysostaphin from Staphylococcus simulans [Staphylococcus simulans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8K9M4	7.99e-08	3	157	272	415	Uncharacterized metalloprotease BUsg_310 OS=Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) OX=198804 GN=BUsg_310 PE=3 SV=1
P44693	2.08e-07	3	112	329	431	Uncharacterized metalloprotease HI_0409 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_0409 PE=3 SV=1
P10547	2.84e-07	13	161	269	416	Lysostaphin OS=Staphylococcus simulans OX=1286 GN=lss PE=1 SV=2
P10548	8.78e-07	13	161	256	403	Lysostaphin OS=Staphylococcus staphylolyticus OX=1287 GN=lss PE=3 SV=1
O05156	1.68e-06	7	161	136	285	Glycyl-glycine endopeptidase ALE-1 OS=Staphylococcus capitis OX=29388 PE=1 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
0.878985	0.119774	0.000481	0.000295	0.000159	0.000332

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002394_02257.