CAZyme Information: MGYG000002382_02189

Basic Information

• Species: Stenotrophomonas maltophilia_AK
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia_AK
• CAZyme ID: MGYG000002382_02189
• CAZy Family: GH19
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
574		61854.51	7.4664

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002382	4489830	Isolate	not provided	not provided

• Gene Location: Start: 44867; End: 46591 Strand: -

Full Sequence      

MADIYQDMVQPRGAAYSSDRIKSWSHYREPIDQSDGRLHGNSRRWGDATPEVQSRVIDTI
IESAREKGLTPRETAHVLAIARVESGFNPDAAAGTTSASGLGQFIDKTGNHYHLNNRNRF
DVGAQSDALVDHYIDNRTLAHKRGQGEEYIYKYHHDGPTRDYGGLTLSEKKVMPYVDKYE
RFVEQRLGLTHGQPQGSHAAPAVAAATHAQAKPAAAHAEAQTRNFEQTMQVMLPPQNGVK
PHITGEFGEHRAHKPHGGTDFNYVGGQHGRNLQHPTVNAPISGTVTFVGGDYGTVKIRDA
QGNSHEILHLQSTQVKEGQPIKAGEPIGTMGGRGPGGAGQYAQHVHYQLKDPHGKLLSPQ
DFWDHGKLKETGKGGHSHDADHNGVLRQGAKGEEVTALQKELNRLGVRDGQGNPLSEDGK
FGANTRDALIAYQKQHGLSADGVAGPATLGKLAEGRSHAEAAPKGPQLGDKAHPDTPLHN
AIRGHMPGMISNEMSAHVTAQAKAAGIDSPEKLQGVTVQDGKAFVVGTVPGFRTAVDMTQ
AAPSLQETSAAMLAKHEPSQQHVQDEQQRVAMGR

Enzyme Prediction     

No EC number prediction in MGYG000002382_02189.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam01471	PG_binding_1	2.15e-15	391	452	1	57	Putative peptidoglycan binding domain. This domain is composed of three alpha helices. This domain is found at the N or C-terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.
pfam01551	Peptidase_M23	6.92e-10	254	327	1	69	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.
COG3409	PGRP	1.23e-09	384	460	37	110	Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis].
cd12797	M23_peptidase	7.43e-09	256	327	1	67	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.
pfam01464	SLT	1.07e-06	60	122	1	63	Transglycosylase SLT domain. This family is distantly related to pfam00062. Members are found in phages, type II, type III and type IV secretion systems.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AEO40768.1	4.99e-150	176	573	179	582
AQS76613.1	2.00e-149	176	573	179	582
APP00140.1	2.00e-149	176	573	179	582
QWM98304.1	5.47e-149	224	573	226	581
CAD1787034.1	2.33e-148	189	573	200	583

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5TV7_A	3.30e-09	385	452	108	169	ChainA, Putative peptidoglycan-binding/hydrolysing protein [Clostridioides difficile 630],5TV7_B Chain B, Putative peptidoglycan-binding/hydrolysing protein [Clostridioides difficile 630]
5NM7_A	4.50e-09	385	456	4	69	Crystalstructure of Burkholderia AP3 phage endolysin [Burkholderia],5NM7_G Crystal structure of Burkholderia AP3 phage endolysin [Burkholderia]
1LBU_A	4.73e-08	383	452	7	73	HydrolaseMetallo (zn) Dd-peptidase [Streptomyces albus G]
3BKH_A	6.75e-06	376	452	2	73	ChainA, lytic transglycosylase [Pseudomonas phage phiKZ],3BKV_A Chain A, lytic transglycosylase [Pseudomonas phage phiKZ]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P00733	4.19e-07	383	452	49	115	Zinc D-Ala-D-Ala carboxypeptidase OS=Streptomyces albus G OX=1962 PE=1 SV=2
L7N653	4.99e-06	392	452	105	160	N-acetylmuramoyl-L-alanine amidase CwlM OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=cwlM PE=1 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
1.000068	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002382_02189.