CAZyme Information: MGYG000003187_01785

Basic Information

• Species: Leclercia adecarboxylata_C
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Leclercia; Leclercia adecarboxylata_C
• CAZyme ID: MGYG000003187_01785
• CAZy Family: GH0
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
753	MGYG000003187_4|CGC4	86506.48	6.8039

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003187	4670976	MAG	United States	North America

• Gene Location: Start: 365327; End: 367588 Strand: -

Full Sequence      

MIISPPFIRPRNAGESEPSWVSRMMPVDTNRDFPLNRRASWHGGVHVLHTDRDGEEGYDR
IEFVRAIADGEVVSFRSPSSTDKRDTFPLNYDGRTDDGYVLLKHQTDIGENCSVVYYSLY
MHLMNRLAPSISVGARIWRKDRIGQSGMVSETNAFHFQVFCDNENMLKLTGRTTPELDIT
RDGRIDTVYGDIHFYLPPGTRFYESVPDAASPGTDRLNAVHTSAEPLFVSMTFEKGDCTM
VTRRQNTTTEARFDTVGEPLTNTDASPADNSIAETYLKYEYNLYRTARRLYPQNPSAGFE
LLRFGRVISAEYETLTPADAPLWRTVSYPGGTGMVNLASPDIKKFSDADFPHWTSWRVVN
DDTDNNSQCNSSLIAGLQDSEHFSDLKSRLICHFPLEWNAATFDQRYAWLRTGSDDVPAM
SEENYERLKSHVSALCFDTGEHGIGRLWHFHPEAFITHFRKCCWLSKSELKQLVPRNALR
MAGRNDYRWEAITYRDGNGSIADNIRTHINRTMQKHLITTPLRIACFLGNGIQETGWLGT
MEEGYRYTETDPRTHQVIRRYNIWYYPWYGRGLLQLTSPVNYFEYFSFRGRTCPENITNT
LINKYNRLYAHRPLRYSDNHLSDAENHVPENIIRWRDNVRSDRHEAASSAGFYWVARDMS
PYADAEHVLERCSVTPRRSGIKIYYRSPAFWRASAAVNLPNQVSNTEYQGLNGFDTRCCV
YGSAIAVLTEQKFPDSHNNPVNEKPESDQLRRG

Enzyme Prediction     

No EC number prediction in MGYG000003187_01785.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd12797	M23_peptidase	2.67e-06	64	159	14	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	0.006	64	159	16	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.
cd00325	chitinase_GH19	0.009	524	582	49	117	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
VEI19559.1	0.0	1	753	1	753
QZX95659.1	0.0	1	753	1	748
QAB32936.1	0.0	24	753	1	725
QFH50174.1	0.0	24	753	1	729
QIV50378.1	0.0	1	753	1	751

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
1.000043	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003187_01785.