CAZyme Information: MGYG000002483_02794

Basic Information

• Species: Clostridium_Q saccharolyticum_A
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Clostridium_Q; Clostridium_Q saccharolyticum_A
• CAZyme ID: MGYG000002483_02794
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
305	MGYG000002483_30|CGC3	34082.11	4.2282

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002483	3781880	Isolate	not provided	not provided

• Gene Location: Start: 71424; End: 72341 Strand: -

Full Sequence      

MQYRKRMRTLWAAVSAAVFCASAPVTVQAAAFEKENGQYVNAEGTAVEGALFRGVSVSKY
QGEIDWAAAAADDVSFAMIRMGYLDSLDPTFDANMREAAASGIQTGVYLYSQALDVDRAV
KEAQFAVRTAKDYRVSYPIAMDVESAYISGLSRQELTDIVNAFCRTVEEAGYHPVVFGYN
DWLVNKMDTSQIPYDIWYARYGTVNTYPNRTIWQCTDSGTVDGIEGPVCLELAFTDYSQV
ISPEGFKKIDGSWYYFKDYAKTDGWVQANGVWYYLDPEDGGRMVSDCWKEIDGQMYQFDA
SGAML

Enzyme Prediction     

No EC number prediction in MGYG000002483_02794.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	55	224	3.6e-42	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	2.50e-65	52	234	1	191	The LytC lysozyme of Streptococcus pneumoniae is a bacterial cell wall hydrolase that cleaves the beta1-4-glycosydic bond located between the N-acetylmuramoyl-N-glucosaminyl residues of the cell wall polysaccharide chains. LytC is composed of a C-terminal glycosyl hydrolase family 25 (GH25) domain and an N-terminal choline-binding module (CBM) consisting of eleven homologous repeats that specifically recognizes the choline residues of pneumococcal lipoteichoic and teichoic acids. This domain arrangement is the reverse of the major pneumococcal autolysin, LytA, and the CPL-1-like lytic enzymes of the pneumococcal bacteriophages, in which the CBM (consisting of six repeats) is at the C-terminus. This model represents the C-terminal catalytic domain of the LytC-like enzymes.
cd00599	GH25_muramidase	1.91e-29	53	228	1	181	Endo-N-acetylmuramidases (muramidases) are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family of muramidases contains a glycosyl hydrolase family 25 (GH25) catalytic domain and is found in bacteria, fungi, slime molds, round worms, protozoans and bacteriophages. The bacteriophage members are referred to as endolysins which are involved in lysing the host cell at the end of the replication cycle to allow release of mature phage particles. Endolysins are typically modular enzymes consisting of a catalytically active domain that hydrolyzes the peptidoglycan cell wall and a cell wall-binding domain that anchors the protein to the cell wall. Endolysins generally have narrow substrate specificities with either intra-species or intra-genus bacteriolytic activity.
pfam01183	Glyco_hydro_25	2.82e-22	55	224	1	180	Glycosyl hydrolases family 25.
cd06415	GH25_Cpl1-like	4.96e-20	54	230	3	195	Cpl-1 lysin (also known as Cpl-9 lysozyme / muramidase) is a bacterial cell wall endolysin encoded by the pneumococcal bacteriophage Cp-1, which cleaves the glycosidic N-acetylmuramoyl-(beta1,4)-N-acetylglucosamine bonds of the pneumococcal glycan chain, thus acting as an enzymatic antimicrobial agent (an enzybiotic) against streptococcal infections. Cpl-1 belongs to the CP family of lysozymes (CPL lysozymes) which includes the Cpl-7 lysin. Cpl-1 has a glycosyl hydrolase family 25 (GH25) catalytic domain with an irregular (beta/alpha)5-beta3 barrel and a C-terminal cell wall-anchoring module formed by six similar choline-binding repeats (ChBr's). The ChBr's facilitate the anchoring of Cpl-1 to the choline-containing teichoic acid of the pneumococcal cell wall. Other members of this domain family have an N-terminal CHAP (cysteine, histidine-dependent amidohydrolases/peptidases) domain similar to that of the firmicute CHAP lysins and associated with endopeptidase activity. The Cpl-7 lysin is also included here as is LysB of Lactococcus phage, and the Mur lysin of Lactobacillus phage.
cd06525	GH25_Lyc-like	3.01e-18	53	226	1	177	Lyc muramidase is an autolytic lysozyme (autolysin) from Clostridium acetobutylicum encoded by the lyc gene. Lyc has a glycosyl hydrolase family 25 (GH25) catalytic domain. Endo-N-acetylmuramidases are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBK77574.1	2.74e-220	1	305	7	311
SET59461.1	4.52e-103	29	305	32	315
ADL03867.1	1.83e-102	22	305	24	315
QRV22095.1	1.83e-102	22	305	24	315
ASN93256.1	9.56e-102	35	291	88	349

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	1.49e-12	55	228	272	462	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae at 1.6 A resolution [Streptococcus pneumoniae R6],2WWD_A 3D-structure of the modular autolysin LytC from Streptococcus pneumoniae in complex with pneummococcal peptidoglycan fragment [Streptococcus pneumoniae R6]
2WWC_A	3.60e-12	55	228	272	462	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P76421	5.07e-08	54	228	69	249	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8FFY2	6.83e-08	54	228	69	249	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
Q8X7H0	7.32e-07	54	228	69	249	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2

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
0.000488	0.992074	0.006662	0.000319	0.000227	0.000188

TMHMM  Annotations     

start	end
9	31