CAZyme Information: MGYG000001384_04458

Basic Information

• Species: Ralstonia pickettii
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Burkholderiales; Burkholderiaceae; Ralstonia; Ralstonia pickettii
• CAZyme ID: MGYG000001384_04458
• CAZy Family: GH19
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
761		84660.11	6.6972

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001384	5243975	Isolate	not provided	not provided

• Gene Location: Start: 246447; End: 248732 Strand: -

Full Sequence      

MLISPPFLPPRAADQTEDQWLEAAMPGGEPGNGAYPVSYNLGWHGGLHLTAPPRGNSGVE
LVRAIADGTVVYRRGSAEPPAPPEENAPLNYRGRTSDGVVVIRHETEIGVATTGNAPTRV
VFFSIYMHLHTVRSTVQQGRRIYRKDELGQAGYIGGRPNQIHFEIVCDDTNLRQLIGRVS
GDVPLAGDGRSDAIFGELYFHLAADTQVFPQHPPLNQPSPPGGTPLGEEVFVGVRYAEGD
GAQGARGHAYVTTYRLTGLPLGDAVTEAEAEYNRKRDATQICDAYPANARPSPSAVYELL
RFGRVIGPDALSPTDVPHWRKIRTPTGTGWVNLNAQGVRKFSDADFPHWRGWRLVEDAQG
GDSLCSDPAILRELDGDHDDTITAEEAHTRLDSPEVKALLKKLICKFPTEWEAATIEARW
GWLKQASPTNPEPMTEEQFQALRAHIEALAFWQQANLQVPQYDAQGQPSGGQPLPNAHWR
FDPREFVRIFRRCGWLNADEMARCFPRRLLHLTGTQFVPHSTTWNVAHARSIAWVLPFNQ
ATRKYGLSISRQRLLHFFAHVIPETGNLHFVKEINGESKTYTPYYGRGLIQLTHLENYLP
YGRFRKFPATVTTGQFSGLGWDPDVFIARNNEGDHNAYNCADSACFYVATRAGMLSHMDA
GVGQDNAVVVSKDVNGNVSIENLNGLDARLQAVLYLRNALLDDVFPDQMLPLTFEWRRNT
QKEPVFDAQGNPVMVGNPPHQKKKFYPTQHTISVSLELQRP

Enzyme Prediction     

No EC number prediction in MGYG000001384_04458.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd12797	M23_peptidase	1.51e-07	44	165	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.
cd00325	chitinase_GH19	9.39e-06	549	607	44	123	Glycoside hydrolase family 19, chitinase domain. Chitinases are enzymes that catalyze the hydrolysis of the beta-1,4-N-acetyl-D-glucosamine linkages in chitin polymers. Glycoside hydrolase family 19 chitinases are found primarily in plants (classes I, III, and IV), but some are found in bacteria. Class I and II chitinases are similar in their catalytic domains. Class I chitinases have an N-terminal cysteine-rich, chitin-binding domain which is separated from the catalytic domain by a proline and glycine-rich hinge region. Class II chitinases lack both the chitin-binding domain and the hinge region. Class IV chitinases are similar to class I chitinases, but they are smaller in size due to certain deletions. Despite lacking any significant sequence homology with lysozymes, structural analysis reveals that family 19 chitinases, together with family 46 chitosanases, are similar to several lysozymes including those from T4-phage and from goose. The structures reveal that the different enzyme groups arose from a common ancestor glycohydrolase antecedent to the prokaryotic/eukaryotic divergence.
COG0739	NlpD	6.64e-04	31	165	150	248	Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
pfam01551	Peptidase_M23	0.001	44	165	3	87	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQK38095.1	0.0	1	761	1	761
CAP63495.1	9.32e-275	1	629	1	639
QNB11811.1	1.02e-173	1	761	1	790
QJP99928.1	2.38e-173	1	703	1	748
QBO07204.1	1.90e-161	1	605	1	613

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
1.000037	0.000009	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001384_04458.