CAZyme Information: MGYG000001959_01064

Basic Information

• Species: UBA3631 sp900546275
• Lineage: Bacteria; Firmicutes; Bacilli; RF39; UBA660; UBA3631; UBA3631 sp900546275
• CAZyme ID: MGYG000001959_01064
• CAZy Family: CBM50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
220		24656.3	9.6585

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001959	1132371	MAG	Denmark	Europe

• Gene Location: Start: 15917; End: 16579 Strand: +

Full Sequence      

MRGEKITDFHTGIDITNLGQVTCIGDGKVVECVKNIKGYDTVNKSGNYIMVYHGKNIEGK
KIYTKYNHLDYGSVKLNIGDEVKTGAIMGTNNIKTTGYSTGLHLHFSVKENSSYVDPKPY
LKAVKLLPNVIDETSDSEETIYIVKKGDTLSGIAKKYNITYQELARYNNITNPNLIYPNQ
KIKIPSKTSNNIITYIVKKGDTISMGNNEYINLKNKKIML

Enzyme Prediction     

No EC number prediction in MGYG000001959_01064.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM50	142	185	2.5e-17	0.975

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam01551	Peptidase_M23	1.01e-18	9	117	2	96	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.
cd00118	LysM	4.25e-16	140	184	1	45	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.
cd12797	M23_peptidase	1.74e-15	10	108	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.
pfam01476	LysM	6.79e-15	142	185	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.
COG0739	NlpD	7.20e-14	9	121	162	264	Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AYV70100.1	1.01e-22	8	187	21	190
AYV67030.1	1.01e-22	8	187	21	190
QJX62919.1	1.01e-22	8	187	21	190
QKH62171.1	3.86e-22	8	187	21	190
BAM46363.1	1.39e-21	5	184	28	199

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4QP5_A	1.70e-07	10	123	33	138	Catalyticdomain of the antimicrobial peptidase lysostaphin from Staphylococcus simulans crystallized in the presence of phosphate [Staphylococcus simulans bv. staphylolyticus],4QP5_B Catalytic domain of the antimicrobial peptidase lysostaphin from Staphylococcus simulans crystallized in the presence of phosphate [Staphylococcus simulans bv. staphylolyticus],4QPB_A Catalytic domain of the antimicrobial peptidase lysostaphin from Staphylococcus simulans crystallized in the absence of phosphate [Staphylococcus simulans],4QPB_B Catalytic domain of the antimicrobial peptidase lysostaphin from Staphylococcus simulans crystallized in the absence of phosphate [Staphylococcus simulans]
5NMY_A	5.48e-07	10	123	31	136	NMRsolution structure of lysostaphin [Staphylococcus simulans]
4LXC_A	5.79e-07	10	123	33	138	Theantimicrobial peptidase lysostaphin from Staphylococcus simulans [Staphylococcus simulans],4LXC_B The antimicrobial peptidase lysostaphin from Staphylococcus simulans [Staphylococcus simulans],4LXC_C The antimicrobial peptidase lysostaphin from Staphylococcus simulans [Staphylococcus simulans],4LXC_D The antimicrobial peptidase lysostaphin from Staphylococcus simulans [Staphylococcus simulans]
6RK4_A	9.06e-07	10	123	279	384	LysostaphinSH3b P4-G5 complex, synchrotron dataset [Staphylococcus simulans]
2L9Y_A	1.25e-06	144	187	67	110	Solutionstructure of the MoCVNH-LysM module from the rice blast fungus Magnaporthe oryzae protein (MGG_03307) [Pyricularia oryzae 70-15]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9RVY3	1.43e-09	132	185	196	252	Uncharacterized protein DR_0888 OS=Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) OX=243230 GN=DR_0888 PE=1 SV=1
Q5HRU2	7.27e-09	134	204	78	158	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) OX=176279 GN=sle1 PE=3 SV=1
Q8CMN2	7.27e-09	134	204	78	158	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) OX=176280 GN=sle1 PE=3 SV=1
Q49UX4	1.82e-08	134	204	21	97	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41) OX=342451 GN=sle1 PE=3 SV=1
Q7A5Y8	2.78e-08	141	185	176	220	Probable cell wall hydrolase LytN OS=Staphylococcus aureus (strain N315) OX=158879 GN=lytN PE=3 SV=2

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
1.000051	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001959_01064.