CAZyme Information: MGYG000004788_01709

Basic Information

• Species: Companilactobacillus farciminis
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Companilactobacillus; Companilactobacillus farciminis
• CAZyme ID: MGYG000004788_01709
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
320	MGYG000004788_37|CGC1	35216.72	5.7665

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004788	2403188	MAG	China	Asia

• Gene Location: Start: 2927; End: 3889 Strand: -

Full Sequence      

MSKKISVIVAAFFSLMVLFFGATNVDAARMDMVDVSNHNGDMTVANFQDMHNNYGVKAAV
TKISEGTTYKDAYAANNIKTARAAGLFIHGYHYAHYSNVSEAIAEANFAAQTAKADGLPS
GSVLVTDVESTEQQHNDPGLNTQSNVAFINQVAKYGYRSDIYTMGSWVDTVMQVKKGWIA
AYPSDATDQYWYPSSHGWQWTSHYEFDGSYGYFDVSQLYDNYFTSYQAPQTVSLDNTNNQ
TNNSSNTTNNAVSSKGVINVSNANGSYVPLVAIQGNSTKTITNRALANNTPWVTDQTKTI
DGVTYHRVATNEWVDAKYII

Enzyme Prediction     

No EC number prediction in MGYG000004788_01709.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	33	208	6.9e-34	0.9887005649717514

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06522	GH25_AtlA-like	1.39e-60	30	219	1	192	AtlA is an autolysin found in Gram-positive lactic acid bacteria that degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family includes the AtlA and Aml autolysins from Streptococcus mutans which have a C-terminal glycosyl hydrolase family 25 (GH25) catalytic domain as well as six tandem N-terminal repeats of the GBS (group B Streptococcus) Bsp-like peptidoglycan-binding domain. Other members of this family have one or more C-terminal peptidoglycan-binding domain(s) (SH3 or LysM) in addition to the GH25 domain.
pfam01183	Glyco_hydro_25	3.29e-29	33	208	1	179	Glycosyl hydrolases family 25.
cd06415	GH25_Cpl1-like	1.04e-23	33	204	4	184	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.
cd00599	GH25_muramidase	5.12e-21	32	216	2	184	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.
cd06525	GH25_Lyc-like	3.64e-16	33	203	3	169	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
ATO46321.1	8.56e-221	1	320	1	320
QCX24641.1	1.77e-197	3	320	4	319
QMT84165.1	1.33e-194	3	320	4	318
APU71289.1	2.00e-145	5	320	3	320
AYE38332.1	6.56e-136	1	319	3	327

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

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
0.000232	0.999129	0.000159	0.000165	0.000152	0.000145

TMHMM  Annotations     

start	end
5	22