CAZyme Information: MGYG000002357_02448

Basic Information

• Species: Bacillus licheniformis
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; Bacillus licheniformis
• CAZyme ID: MGYG000002357_02448
• CAZy Family: CBM50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
274	MGYG000002357_1|CGC33	30693.78	9.5921

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002357	4208157	Isolate	South Korea	Asia

• Gene Location: Start: 2367001; End: 2367825 Strand: -

Full Sequence      

MKKLRHQNFLFAIAWLSGLALFVNAPGAEASEWIEPIKGEITDQFGTRGGKHKGLDIAAP
EGEAVAAAADGTISKSYQSDSYGQVIFIKHDNGYETVYAHLSKRLKKEKERVKKGEQIGI
IGNTGISTGTHLHFEMHHGSWTEDKRYAINPLTVLREEAFRQNSIHVHQNAGTMSGAVTV
QKGDTLWRISKDSGISIEEIMRINGLKHSNLKAGQTLRLHDDESKTGTYVVRKGDTLHHI
AEKMGVTVQRLKEWNDLKGERIYPRQMLEIRENS

Enzyme Prediction     

No EC number prediction in MGYG000002357_02448.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam01551	Peptidase_M23	4.82e-41	50	151	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	3.29e-37	52	136	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	8.59e-35	2	156	102	265	Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
PRK11649	PRK11649	2.13e-23	34	154	303	409	putative peptidase; Provisional
PRK10871	nlpD	2.15e-21	27	155	194	316	murein hydrolase activator NlpD.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QAW29457.1	9.17e-202	1	274	1	274
QDF79706.1	9.17e-202	1	274	1	274
QAT53898.1	9.17e-202	1	274	1	274
ARC59324.1	9.17e-202	1	274	1	274
AKQ73647.1	9.17e-202	1	274	1	274

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SLU_A	1.94e-18	52	135	246	328	Crystalstructure of NMB0315 [Neisseria meningitidis ATCC 13091],3SLU_B Crystal structure of NMB0315 [Neisseria meningitidis ATCC 13091]
6MUK_A	2.38e-18	52	135	266	348	1.93Angstrom Resolution Crystal Structure of Peptidase M23 from Neisseria gonorrhoeae. [Neisseria gonorrhoeae FA 1090]
5KQB_A	2.64e-17	31	152	2	135	Identificationand structural characterization of LytU [Staphylococcus aureus],5KQC_A Identification and structural characterization of LytU [Staphylococcus aureus]
5J1L_A	4.14e-15	52	136	65	151	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	6.78e-15	52	136	266	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P44693	4.20e-23	52	189	348	466	Uncharacterized metalloprotease HI_0409 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_0409 PE=3 SV=1
A0A0H3C9Q9	1.13e-20	23	155	474	607	Cell division protein DipM OS=Caulobacter vibrioides (strain NA1000 / CB15N) OX=565050 GN=dipM PE=3 SV=1
Q56131	2.50e-19	24	155	245	370	Murein hydrolase activator NlpD OS=Salmonella typhi OX=90370 GN=nlpD PE=3 SV=2
P39700	2.59e-19	24	155	249	374	Murein hydrolase activator NlpD OS=Salmonella dublin OX=98360 GN=nlpD PE=2 SV=2
P40827	2.59e-19	24	155	249	374	Murein hydrolase activator NlpD OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 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
0.000272	0.999071	0.000186	0.000161	0.000142	0.000131

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002357_02448.