CAZyme Information: MGYG000002488_03531

Basic Information

• Species: Proteus penneri
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Proteus; Proteus penneri
• CAZyme ID: MGYG000002488_03531
• CAZy Family: CBM50
• CAZyme Description: Murein DD-endopeptidase MepM

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
441	MGYG000002488_5|CGC1	48476.65	9.4497

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002488	3747729	Isolate	United States	North America

• Gene Location: Start: 150833; End: 152158 Strand: +

Full Sequence      

MQQKKSIAQVYLSLPLPHKIMLGSLTAATLAVAIWRPVVLQNEQNREVPVSIQMPSAVQS
ENTDDIITDSSDQLTDEGLVGAEDGTDTSTAVAQVPHTYIVSSGDSLSSILTQFGIDSSD
IATISNQNKDLRNLKIGQSISWELDDNGLLQELNWGVSRRETRVYTRTETGFKETKEFQK
GEWKNSVTSGVIRGSFSVSATNAGLTNSEARAVTKALQWQVDFKKLQSGDQFAALFSREV
LDGRTEQSELIGVRLRSAGKDYYAFLAEDGRFYDSQAGGLERGFMRFPTVKQFRVSSQFN
PRRINPVTGRLAAHKGVDFAMPVGTPVLATGDGEVIVAKYSGAAGNFIAIRHGSQYTTRY
MHLRQLLVKPGQRVKRGDRIALSGNTGRSTGPHLHYELWINQQAVNPLTATLPRADGLTG
KDKQEYLAKVKEIKPQLVLAD

Enzyme Prediction     

No EC number prediction in MGYG000002488_03531.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK11649	PRK11649	0.0	1	439	1	438	putative peptidase; Provisional
COG0739	NlpD	6.70e-53	98	426	3	277	Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
pfam01551	Peptidase_M23	9.72e-49	314	407	3	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	1.34e-42	314	398	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.
PRK10871	nlpD	1.68e-14	315	408	220	313	murein hydrolase activator NlpD.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QPT33928.1	3.04e-314	1	441	1	441
QNH67209.1	1.68e-311	1	441	1	441
ATN00451.1	1.32e-308	1	441	1	441
QJW51113.1	2.67e-308	1	441	1	441
VTP86564.1	2.67e-308	1	441	1	441

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2GU1_A	1.44e-84	99	432	10	350	Crystalstructure of a zinc containing peptidase from vibrio cholerae [Vibrio cholerae]
6UE4_A	5.34e-79	92	437	38	389	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	5.82e-79	92	437	35	386	ShyAendopeptidase from Vibrio cholera (open form) [Vibrio cholerae]
3SLU_A	1.72e-28	101	429	19	359	Crystalstructure of NMB0315 [Neisseria meningitidis ATCC 13091],3SLU_B Crystal structure of NMB0315 [Neisseria meningitidis ATCC 13091]
6MUK_A	1.56e-26	101	429	39	379	1.93Angstrom Resolution Crystal Structure of Peptidase M23 from Neisseria gonorrhoeae. [Neisseria gonorrhoeae FA 1090]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P0AFT1	1.04e-182	1	437	1	437	Murein DD-endopeptidase MepM OS=Shigella flexneri OX=623 GN=mepM PE=3 SV=1
P0AFT0	1.04e-182	1	437	1	437	Murein DD-endopeptidase MepM OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=mepM PE=3 SV=1
P0AFS9	1.04e-182	1	437	1	437	Murein DD-endopeptidase MepM OS=Escherichia coli (strain K12) OX=83333 GN=mepM PE=1 SV=1
P44693	3.97e-96	62	437	97	473	Uncharacterized metalloprotease HI_0409 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_0409 PE=3 SV=1
Q8K9M4	1.55e-82	97	437	77	414	Uncharacterized metalloprotease BUsg_310 OS=Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) OX=198804 GN=BUsg_310 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
0.998531	0.001420	0.000033	0.000007	0.000004	0.000038

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002488_03531.