CAZyme Information: MGYG000001712_01440

Basic Information

• Species: Bacillus_A thuringiensis_S
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae_G; Bacillus_A; Bacillus_A thuringiensis_S
• CAZyme ID: MGYG000001712_01440
• CAZy Family: CBM50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
204	MGYG000001712_1|CGC12	22965.31	9.4515

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001712	5736823	Isolate	United States	North America

• Gene Location: Start: 1413492; End: 1414106 Strand: +

Full Sequence      

MKVLKCGVMLLSILFVSQLHVYAEENRWTWPVEGQISDYFGTRHGKHYGIDVAAPIGTPV
AAIQDGKVTKSYYSSSYGNVVFIKHGEYEAVYAHLNKRYVGQGDYISKGEKIGEVGNTGE
SRGAHLHLELHQGRWTMAKKNAMNPLLVLSEQRNEVVSSSLYVVQKGDTLVSIARKFSMT
LKEIKEKNGLQQELIYPNQQLYVK

Enzyme Prediction     

No EC number prediction in MGYG000001712_01440.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam01551	Peptidase_M23	4.16e-37	45	145	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.
cd12797	M23_peptidase	5.22e-35	47	130	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	2.79e-29	23	149	129	264	Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
PRK11649	PRK11649	2.35e-24	16	146	289	407	putative peptidase; Provisional
COG4942	EnvC	1.64e-19	30	134	301	410	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
AXR16016.1	7.27e-146	1	204	1	204
AXR21750.1	7.27e-146	1	204	1	204
AFQ16121.1	7.27e-146	1	204	1	204
AZV65457.1	7.27e-146	1	204	1	204
AQY37978.1	7.27e-146	1	204	1	204

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KQB_A	3.78e-16	45	133	27	118	Identificationand structural characterization of LytU [Staphylococcus aureus],5KQC_A Identification and structural characterization of LytU [Staphylococcus aureus]
6MUK_A	1.07e-14	47	183	266	399	1.93Angstrom Resolution Crystal Structure of Peptidase M23 from Neisseria gonorrhoeae. [Neisseria gonorrhoeae FA 1090]
3SLU_A	2.45e-14	47	129	246	328	Crystalstructure of NMB0315 [Neisseria meningitidis ATCC 13091],3SLU_B Crystal structure of NMB0315 [Neisseria meningitidis ATCC 13091]
6UE4_A	4.97e-14	43	130	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	5.01e-14	43	130	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	6.75e-16	31	148	340	445	Uncharacterized metalloprotease HI_0409 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_0409 PE=3 SV=1
Q89AI9	8.32e-15	43	164	247	369	Uncharacterized metalloprotease bbp_296 OS=Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp) OX=224915 GN=bbp_296 PE=3 SV=1
P0AFS9	6.38e-14	27	146	302	408	Murein DD-endopeptidase MepM OS=Escherichia coli (strain K12) OX=83333 GN=mepM PE=1 SV=1
P0AFT1	6.38e-14	27	146	302	408	Murein DD-endopeptidase MepM OS=Shigella flexneri OX=623 GN=mepM PE=3 SV=1
P0AFT0	6.38e-14	27	146	302	408	Murein DD-endopeptidase MepM OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=mepM PE=3 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
0.000231	0.999089	0.000197	0.000159	0.000157	0.000149

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001712_01440.