CAZyme Information: MGYG000001525_01328

Basic Information

• Species: Paenibacillus_A rubinfantis
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A rubinfantis
• CAZyme ID: MGYG000001525_01328
• CAZy Family: CBM50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
285	MGYG000001525_17|CGC7	31115.16	8.2136

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001525	5369528	Isolate	not provided	not provided

• Gene Location: Start: 329542; End: 330399 Strand: +

Full Sequence      

MGNKKWMLGIAGAIIGTLLFGGVSQAASYTVKSGDSLWKIANAYRISTTQLKTMNQLTGD
WIYPGQVLQVPGTTAYTVQNGETMWLISLKFNVTLDSLLKANPQLSNPNNIWAGLQINLP
AEAKITSTVAKPDRFENGFFPLAKGTYTPMTNSYGDGRAWAEEGSAQRTHEGIDIFAEEG
TPVYSAMAGEVINYGWNELGGWRLTVRVDGSTAFYYAHLSRYAEGIGPGSKVTKGQLIGY
VGSTGYGPEGTSGLFLPHLHFGIYQTSPWKALNAYPYLSWWEANR

Enzyme Prediction     

No EC number prediction in MGYG000001525_01328.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM50	29	71	9.1e-17	0.975

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0739	NlpD	1.43e-26	29	280	4	266	Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
pfam01551	Peptidase_M23	7.63e-25	168	264	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.
cd12797	M23_peptidase	4.06e-24	170	263	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.
PRK06347	PRK06347	6.42e-17	21	153	325	479	1,4-beta-N-acetylmuramoylhydrolase.
PRK06347	PRK06347	6.98e-17	24	107	477	581	1,4-beta-N-acetylmuramoylhydrolase.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKS47651.1	3.30e-89	10	282	12	278
ATY83590.1	3.91e-82	10	285	6	288
CAB3389674.1	4.87e-82	10	285	2	284
ADG04808.1	7.84e-82	10	285	6	288
AZB44109.1	3.04e-65	24	282	23	274

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3NYY_A	1.59e-24	139	277	93	235	Crystalstructure of a putative glycyl-glycine endopeptidase lytM (RUMGNA_02482) from Ruminococcus gnavus ATCC 29149 at 1.60 A resolution [[Ruminococcus] gnavus ATCC 29149]
4QP5_A	6.42e-12	170	261	33	117	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]
4RNY_A	9.80e-12	138	278	188	317	Structureof Helicobacter pylori Csd3 from the orthorhombic crystal [Helicobacter pylori 26695],4RNY_B Structure of Helicobacter pylori Csd3 from the orthorhombic crystal [Helicobacter pylori 26695],4RNZ_A Structure of Helicobacter pylori Csd3 from the hexagonal crystal [Helicobacter pylori 26695]
5NMY_A	3.53e-11	170	261	31	115	NMRsolution structure of lysostaphin [Staphylococcus simulans]
4LXC_A	3.92e-11	170	261	33	117	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O32130	2.22e-31	140	282	178	318	L-Ala--D-Glu endopeptidase OS=Bacillus subtilis (strain 168) OX=224308 GN=lytH PE=2 SV=2
P10548	5.31e-10	170	261	266	350	Lysostaphin OS=Staphylococcus staphylolyticus OX=1287 GN=lss PE=3 SV=1
P10547	5.39e-10	170	261	279	363	Lysostaphin OS=Staphylococcus simulans OX=1286 GN=lss PE=1 SV=2
O05156	1.02e-09	170	261	150	234	Glycyl-glycine endopeptidase ALE-1 OS=Staphylococcus capitis OX=29388 PE=1 SV=1
Q49UX4	1.20e-09	10	75	5	75	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

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000382	0.998736	0.000346	0.000198	0.000173	0.000147

TMHMM  Annotations     

start	end
7	29