CAZyme Information: MGYG000001453_04442

Basic Information

• Species: Aneurinibacillus aneurinilyticus
• Lineage: Bacteria; Firmicutes; Bacilli; Aneurinibacillales; Aneurinibacillaceae; Aneurinibacillus; Aneurinibacillus aneurinilyticus
• CAZyme ID: MGYG000001453_04442
• CAZy Family: GH23
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
350		37725.02	6.4221

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001453	5302959	Isolate	not provided	not provided

• Gene Location: Start: 11882; End: 12934 Strand: -

Full Sequence      

MKKWGWLIAAIPILLVVALCGMFLFPLLFMGGGSIGYGFLGGSISPIGEREIPVEYIPIY
KEAEARYGVPWNLLAAHHRVETVFSTLQPMISSVGAEGHMQFMPCTWVGWSHPSCYGAGK
GSFTEEEKTSLTMIARYAGYGVDADRDGRASMWSLRDSIFSAANYLAKNGAATGNLERAI
FAYNHSQDYVAEVMMYARLYVTEGFIPIEVIEPSESGFARPVAGEVTSGFGIRIDPVTGK
PGASHEGIDFACQAGQRIPASKAGKVVFAGWQDANDHSKGYGLFVWVDHGGGFKTTYAHM
SQTTVQVGDVVQAGDVVGVCGSTGKSTGLHLHFEIFVNGRRVDPSPFIGL

Enzyme Prediction     

No EC number prediction in MGYG000001453_04442.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH23	61	200	1.5e-17	0.8740740740740741

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam01551	Peptidase_M23	5.17e-38	245	344	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.
COG0739	NlpD	2.09e-37	198	344	114	257	Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
cd12797	M23_peptidase	5.57e-33	245	335	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.
cd13399	Slt35-like	1.98e-26	67	194	1	103	Slt35-like lytic transglycosylase. Lytic transglycosylase similar to Escherichia coli lytic transglycosylase Slt35 and Pseudomonas aeruginosa Sltb1. Lytic transglycosylase (LT) catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc) as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).
COG4942	EnvC	4.47e-22	214	349	288	419	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
AWP25350.1	2.93e-259	1	350	1	350
QPK61329.1	5.31e-155	1	350	1	356
QDA30293.1	5.31e-155	1	350	1	356
QPK56312.1	5.31e-155	1	350	1	356
ALP39382.1	1.76e-153	1	350	1	356

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2HSI_A	3.25e-22	213	349	149	278	Crystalstructure of putative peptidase M23 from pseudomonas aeruginosa, New York Structural Genomics Consortium [Pseudomonas aeruginosa PAO1],2HSI_B Crystal structure of putative peptidase M23 from pseudomonas aeruginosa, New York Structural Genomics Consortium [Pseudomonas aeruginosa PAO1]
4QP5_A	1.15e-16	229	348	18	136	Catalyticdomain of the antimicrobial peptidase lysostaphin from Staphylococcus simulans crystallized in the presence of phosphate [Staphylococcus simulans bv. staphylolyticus],4QP5_B Catalytic domain of the antimicrobial peptidase lysostaphin from Staphylococcus simulans crystallized in the presence of phosphate [Staphylococcus simulans bv. staphylolyticus],4QPB_A Catalytic domain of the antimicrobial peptidase lysostaphin from Staphylococcus simulans crystallized in the absence of phosphate [Staphylococcus simulans],4QPB_B Catalytic domain of the antimicrobial peptidase lysostaphin from Staphylococcus simulans crystallized in the absence of phosphate [Staphylococcus simulans]
3SLU_A	1.32e-16	226	344	228	338	Crystalstructure of NMB0315 [Neisseria meningitidis ATCC 13091],3SLU_B Crystal structure of NMB0315 [Neisseria meningitidis ATCC 13091]
6MUK_A	1.59e-16	226	344	248	358	1.93Angstrom Resolution Crystal Structure of Peptidase M23 from Neisseria gonorrhoeae. [Neisseria gonorrhoeae FA 1090]
5NMY_A	9.61e-16	229	348	16	134	NMRsolution structure of lysostaphin [Staphylococcus simulans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O64046	1.98e-17	55	348	1421	1678	Probable tape measure protein OS=Bacillus phage SPbeta OX=66797 GN=yomI PE=3 SV=1
O31976	1.98e-17	55	348	1421	1678	SPbeta prophage-derived uncharacterized transglycosylase YomI OS=Bacillus subtilis (strain 168) OX=224308 GN=yomI PE=3 SV=2
P44693	6.45e-16	158	344	266	442	Uncharacterized metalloprotease HI_0409 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_0409 PE=3 SV=1
O05156	1.86e-14	212	348	118	253	Glycyl-glycine endopeptidase ALE-1 OS=Staphylococcus capitis OX=29388 PE=1 SV=1
P0AFT1	2.00e-14	217	344	283	407	Murein DD-endopeptidase MepM OS=Shigella flexneri OX=623 GN=mepM 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
0.999982	0.000048	0.000005	0.000000	0.000000	0.000008

TMHMM  Annotations     

start	end
7	29