CAZyme Information: MGYG000001344_00276

Basic Information

• Species: Acinetobacter radioresistens
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Moraxellaceae; Acinetobacter; Acinetobacter radioresistens
• CAZyme ID: MGYG000001344_00276
• CAZy Family: CBM50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
681		74910.44	10.1632

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001344	3137190	Isolate	not provided	not provided

• Gene Location: Start: 128204; End: 130249 Strand: +

Full Sequence      

MSKVYIVKSGDTLWGISKKHHITVKELARINSLSGRMIHSLKVGQKIHLKEDSGISHKFE
TQLKIVLMDLSFKPISKATIQLDFDGKKIIKSTTNGIFDDIGIEDHSKGLKVFFKNINGN
FDLIADHKMLPLGRKVLKLTSRKIKVEGSHYVKDGLLNETVSEIKNNLKRVGKPIVDGVS
SVIESLSSTKNPHQPQRTSSKEKNQLPEERQEQKRTDAGNSTHIIAAQFTEDNFLLKPVN
NKYRAYIVSAAKRHGFTPHSLAAVIDAEAAKIKKTGEWNVNSKANSSSAAGLTQFLDETW
LAMCNDRSSLVGQYVKNNPKLTKEQKLNLRFNAEMAIDAAAAYAVSNFKTSGLPYQNLTE
PSSMAKFAYLLHHEGASGGKNFVLNTLSPERAKKLLFIQFGKNGAKQAEEFLKRYKGDAK
AAYGAWLRNYIDGHINIYQYVVDKSKTSGINLSMEETIKLLKGQSIPAPIPKEQKVNSQT
TNAQQSVPKSESSNKPQVQSDEKTVGGDEGWHDPLLQCKLRTAGLANAKGATFGKVRNNG
TKNHQGVDLQANPGTKIYAVCGGVIVFAKDSGGAYGKVIVLRVDINDLAEKQKKYAQSKL
TKNQYVYFFYAHLSDINVAKEDSVDTGEEIGKTGSTGNANKMTAISNGAHLHFEARSAPL
LGVGLDGRIDPIPFINANLPY

Enzyme Prediction     

No EC number prediction in MGYG000001344_00276.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam01551	Peptidase_M23	1.08e-23	542	656	1	88	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	1.45e-22	544	654	1	84	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	8.72e-17	417	678	20	267	Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
cd00118	LysM	6.66e-12	3	47	1	43	Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
pfam01476	LysM	2.63e-11	5	50	1	43	LysM domain. The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QMU04031.1	0.0	1	681	1	681
QHH98763.1	0.0	1	681	1	684
BBL19432.1	0.0	1	681	1	681
ASN72911.1	0.0	1	681	1	681
QQT66100.1	0.0	1	681	1	681

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

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
1.000039	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001344_00276.