CAZyme Information: MGYG000001501_02539

Basic Information

• Species: Bacillus_J andreraoultii
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales_B; Caldibacillaceae; Bacillus_J; Bacillus_J andreraoultii
• CAZyme ID: MGYG000001501_02539
• CAZy Family: CBM50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
243	MGYG000001501_14|CGC10	27048.76	7.1998

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001501	4050118	Isolate	not provided	not provided

• Gene Location: Start: 1523290; End: 1524021 Strand: +

Full Sequence      

MVEYIKRLLLGIVMVIIITFLIIGSKQSIAKAEGLEKGGEGWIWPANGVITDTYGTRGGQ
HKGIDIAEVIGTPVYSVDNGQVTKSYYSDTYGNVVFIKHKVGYETVYAHLSDRKVQEGQH
VKKGEIIGLMGNTGESSGPHLHFEIHKNEWTITKENSLDPTRLFGMGDVGQYVQAGTSNG
KDVEVTKEIDMEQGKRNHTVKRGDTLWDIANKYETTVTKIKEWNGLKSERIIPGQEITIK
QIN

Enzyme Prediction     

No EC number prediction in MGYG000001501_02539.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM50	198	239	6.4e-16	0.95

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam01551	Peptidase_M23	1.39e-42	61	152	3	94	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	1.11e-37	61	145	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	3.65e-37	41	167	133	267	Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
PRK11649	PRK11649	2.22e-25	61	149	313	401	putative peptidase; Provisional
COG4942	EnvC	2.69e-23	25	148	282	408	Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AWI12739.1	4.46e-118	1	241	1	233
QIZ11147.1	2.90e-79	3	239	3	247
AIM15479.1	8.16e-75	1	240	1	252
QOK24927.1	3.28e-72	3	242	3	250
AND41282.1	3.28e-72	3	242	3	250

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5J1L_A	9.06e-21	60	164	64	175	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-17	61	172	246	356	Crystalstructure of NMB0315 [Neisseria meningitidis ATCC 13091],3SLU_B Crystal structure of NMB0315 [Neisseria meningitidis ATCC 13091]
6MUK_A	1.52e-17	61	172	266	376	1.93Angstrom Resolution Crystal Structure of Peptidase M23 from Neisseria gonorrhoeae. [Neisseria gonorrhoeae FA 1090]
6UE4_A	7.08e-17	57	145	262	350	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	7.18e-17	57	145	259	347	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	3.67e-18	61	148	348	436	Uncharacterized metalloprotease HI_0409 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_0409 PE=3 SV=1
A0A0H3C9Q9	5.99e-18	22	160	462	603	Cell division protein DipM OS=Caulobacter vibrioides (strain NA1000 / CB15N) OX=565050 GN=dipM PE=3 SV=1
Q89AI9	2.06e-17	57	156	247	346	Uncharacterized metalloprotease bbp_296 OS=Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp) OX=224915 GN=bbp_296 PE=3 SV=1
P0AFT0	2.84e-17	57	152	310	405	Murein DD-endopeptidase MepM OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=mepM PE=3 SV=1
P0AFS9	2.84e-17	57	152	310	405	Murein DD-endopeptidase MepM OS=Escherichia coli (strain K12) OX=83333 GN=mepM PE=1 SV=1

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
0.495485	0.498260	0.004222	0.000613	0.000478	0.000929

TMHMM  Annotations     

start	end
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