CAZyme Information: MGYG000002725_01116

Basic Information

• Species: CAG-485 sp900554345
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485; CAG-485 sp900554345
• CAZyme ID: MGYG000002725_01116
• CAZy Family: CBM50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
310	MGYG000002725_28|CGC1	34786.38	9.6347

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002725	3333010	MAG	Canada	North America

• Gene Location: Start: 6817; End: 7749 Strand: -

Full Sequence      

MNIKAIIPAALLALLMTTGAAAQKIISKSPHSDAHRQLLANQAKNKDQIKLVEKNTFIDL
IDDIEPEPDIYTEGWNSKRVNPFKESDVPYSKVIDVRGYFMPCPGNVTSHYGYRARFGRM
HKGIDLQIRSNDTIYAAFDGKVRLTNYEPRGYGNYVIIRHPNDLETVYGHLNKFLVKPDQ
VVRAGDPIALGGSTGRSTGPHLHFETRYMGYAINPAAIFDFQNHCTHTDTYTFTKKTYTK
ARNYAPSRNLADNDDNPYQSGDDKSTYTVKKGDTLSSIAKSYGLSATTLRKLNDMNSTDL
IRVGQVLKLK

Enzyme Prediction     

No EC number prediction in MGYG000002725_01116.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam01551	Peptidase_M23	1.29e-42	119	215	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	1.26e-36	76	221	114	263	Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
cd12797	M23_peptidase	2.12e-36	121	205	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	5.36e-24	118	215	308	406	putative peptidase; Provisional
PRK10871	nlpD	9.21e-18	122	215	220	312	murein hydrolase activator NlpD.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QJR98293.1	1.62e-170	4	310	5	312
QCD35905.1	3.10e-105	12	310	16	318
ASB37853.1	1.91e-97	2	309	4	312
QQR08585.1	1.91e-97	2	309	4	312
ANU64052.2	1.91e-97	2	309	4	312

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SLU_A	1.19e-19	107	218	228	341	Crystalstructure of NMB0315 [Neisseria meningitidis ATCC 13091],3SLU_B Crystal structure of NMB0315 [Neisseria meningitidis ATCC 13091]
6MUK_A	1.51e-19	107	218	248	361	1.93Angstrom Resolution Crystal Structure of Peptidase M23 from Neisseria gonorrhoeae. [Neisseria gonorrhoeae FA 1090]
5J1L_A	1.66e-19	121	215	65	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]
6UE4_A	2.31e-16	121	214	266	358	ShyAEndopeptidase from Vibrio cholerae (Closed form) [Vibrio cholerae O1 biovar El Tor str. N16961],6UE4_B ShyA Endopeptidase from Vibrio cholerae (Closed form) [Vibrio cholerae O1 biovar El Tor str. N16961]
6U2A_A	2.34e-16	121	214	263	355	ShyAendopeptidase from Vibrio cholera (open form) [Vibrio cholerae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P44693	4.26e-22	104	218	332	445	Uncharacterized metalloprotease HI_0409 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_0409 PE=3 SV=1
P0AFT1	9.95e-17	121	215	314	407	Murein DD-endopeptidase MepM OS=Shigella flexneri OX=623 GN=mepM PE=3 SV=1
P0AFT0	9.95e-17	121	215	314	407	Murein DD-endopeptidase MepM OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=mepM PE=3 SV=1
P0AFS9	9.95e-17	121	215	314	407	Murein DD-endopeptidase MepM OS=Escherichia coli (strain K12) OX=83333 GN=mepM PE=1 SV=1
Q56131	3.20e-16	102	215	257	366	Murein hydrolase activator NlpD OS=Salmonella typhi OX=90370 GN=nlpD PE=3 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
0.000296	0.999035	0.000195	0.000148	0.000149	0.000135

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002725_01116.