CAZyme Information: MGYG000001379_03133

Basic Information

• Species: Schaedlerella glycyrrhizinilytica
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Schaedlerella; Schaedlerella glycyrrhizinilytica
• CAZyme ID: MGYG000001379_03133
• CAZy Family: GH73
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
352	MGYG000001379_12|CGC1	37920.5	4.3584

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001379	3227618	Isolate	not provided	not provided

• Gene Location: Start: 29677; End: 30735 Strand: -

Full Sequence      

MKRMKRILIAGGAVLLGLFLVLAAALLVYVQESIRAEQRMEDSQSGDYDIDLGNLPGWIT
VEMVSAAIDMMNETGYPASVVLGQMILESGAAGSELANPPYYNCLGQKSPSYLETGSVTM
NTAEAWGYEDAAFSTFASYVDCMRAWGHKFTMPPYVDNVTACIRDPVTGHYDANAFIEAV
WKSGYATDPNYVDKVIQIMTSYDLYRFNSMTAEDLEQGGGDVVISGNGQFTHPCPGMTCQ
TSYFGEIREFEVGGHKGNDYAAPVGTPTYAAAAGTVIIAGWSDSAGNWVVIDHGGGLTTK
YMHHSRILVSAGQTVEKGQQIGEVGSTGQSTGPHLHFQVEVNGVAVNPDDYY

Enzyme Prediction     

No EC number prediction in MGYG000001379_03133.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH73	63	204	4.9e-24	0.9921875

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam01551	Peptidase_M23	4.62e-47	253	348	1	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.
COG0739	NlpD	1.89e-39	241	351	146	260	Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
cd12797	M23_peptidase	6.34e-39	255	339	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.
PRK11649	PRK11649	4.46e-34	241	348	295	406	putative peptidase; Provisional
COG1705	FlgJ	1.27e-24	62	207	49	187	Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBL24986.1	7.65e-172	2	351	5	348
QBF73601.1	8.39e-51	49	351	194	494
QRO36914.1	8.39e-51	49	351	194	494
QYX26960.1	1.01e-50	49	351	222	522
BBM16246.1	1.12e-35	78	343	219	470

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6UE4_A	8.16e-22	255	347	266	358	ShyAEndopeptidase from Vibrio cholerae (Closed form) [Vibrio cholerae O1 biovar El Tor str. N16961],6UE4_B ShyA Endopeptidase from Vibrio cholerae (Closed form) [Vibrio cholerae O1 biovar El Tor str. N16961]
6U2A_A	8.38e-22	255	347	263	355	ShyAendopeptidase from Vibrio cholera (open form) [Vibrio cholerae]
6JMX_A	8.46e-22	227	351	120	245	ChainA, Peptidase M23 [Campylobacter jejuni],6JMY_A Chain A, Peptidase M23 [Campylobacter jejuni],6KV1_A Chain A, Peptidase M23 [Campylobacter jejuni]
6JN1_A	1.80e-20	227	351	120	245	ChainA, Peptidase M23 [Campylobacter jejuni]
6JN0_A	1.84e-20	227	351	120	245	ChainA, Peptidase M23 [Campylobacter jejuni],7E60_A Chain A, Peptidase M23 [Campylobacter jejuni],7E61_A Chain A, Peptidase M23 [Campylobacter jejuni],7E63_A Chain A, Peptidase M23 [Campylobacter jejuni],7E63_B Chain B, Peptidase M23 [Campylobacter jejuni],7E64_A Chain A, Peptidase M23 [Campylobacter jejuni],7E65_A Chain A, Peptidase M23 [Campylobacter jejuni],7E65_B Chain B, Peptidase M23 [Campylobacter jejuni],7E66_A Chain A, Peptidase M23 [Campylobacter jejuni],7E67_A Chain A, Peptidase M23 [Campylobacter jejuni],7E69_A Chain A, Peptidase M23 [Campylobacter jejuni]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O31976	1.19e-21	255	351	1580	1677	SPbeta prophage-derived uncharacterized transglycosylase YomI OS=Bacillus subtilis (strain 168) OX=224308 GN=yomI PE=3 SV=2
O64046	1.19e-21	255	351	1580	1677	Probable tape measure protein OS=Bacillus phage SPbeta OX=66797 GN=yomI PE=3 SV=1
P0AFT0	8.38e-21	255	348	314	407	Murein DD-endopeptidase MepM OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=mepM PE=3 SV=1
P0AFS9	8.38e-21	255	348	314	407	Murein DD-endopeptidase MepM OS=Escherichia coli (strain K12) OX=83333 GN=mepM PE=1 SV=1
P0AFT1	8.38e-21	255	348	314	407	Murein DD-endopeptidase MepM OS=Shigella flexneri OX=623 GN=mepM PE=3 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
0.660834	0.329756	0.002689	0.001575	0.000997	0.004148

TMHMM  Annotations     

start	end
7	29