CAZyme Information: MGYG000002346_03662

Basic Information

• Species: Acinetobacter pittii
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Moraxellaceae; Acinetobacter; Acinetobacter pittii
• CAZyme ID: MGYG000002346_03662
• CAZy Family: CBM50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
667		72841.24	9.7553

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002346	3962855	Isolate	United States	North America

• Gene Location: Start: 519; End: 2522 Strand: -

Full Sequence      

MMIKGNTYKVEGIPRTNTKTIEKELKVNSKKVQHSSGASGASGASGASGASGASGASGAS
GASGASGASGASETRIEGGLPAVTVAPVYSEENLYLHPDNEKYRKIIIDAAKKYNLAPQA
LAAKINAEAGTKKGSQEWNPQAQASTSSAVGLTQFLSGTWYEICTVSTYKDTLLQQYVIK
KKLISNFKENMALKLISNTDKAKLKALGTDPTFSVDSAAAYARANINIVKKIYSKIDSLE
PGDLAKVGYVAHHDGPTGFGKIVEATNDPSWSKLQGQVCPKNNPNCDTYLNYKERFSNGR
DAYRWWLCTEYTDSKINVNRFTLSPKDGKKFKNARTMEEIIVFLGGKPLVRPSRDFEKKG
TTDNSKLNDNINIVITSLVNNKVQANISYFVKSKYGLKPHSTNVNGHEIIHAKKGDKIEV
IFNDQVIASINAINDKEEFKINFPSKNITNASTEKQSSNSEQKLNFNRWRNPLNGICQIR
RFGYNSLPLKANASSYNEKNLEQATKVASRFNRTSYRASGIHQGVDLEADNGVNIYPVCV
GTIAKVIPAYPGYGKTIILECDVNDLPSSKKVLAKNLDTIYFIYAHLNSINVSEGDSITT
LDTVLGKTGNSGNAGSMTRVEDGSHLHFEVRSEIMKSMGKSGMSYRLDPFPWLDNCMTTE
NGVKVNR

Enzyme Prediction     

No EC number prediction in MGYG000002346_03662.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd12797	M23_peptidase	1.49e-19	522	630	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.
pfam01551	Peptidase_M23	2.17e-17	520	631	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.
COG0739	NlpD	5.42e-15	387	631	44	249	Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
cd13399	Slt35-like	2.15e-05	114	160	1	40	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).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QOW99409.1	0.0	1	667	143	812
QJH01352.1	0.0	1	667	143	800
QAB38943.1	0.0	1	667	143	776
QKY25471.1	0.0	1	667	143	812
APX48846.1	0.0	1	667	143	812

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
1.000068	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002346_03662.