CAZyme Information: MGYG000000822_00639

Basic Information

• Species: Companilactobacillus farciminis_A
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Companilactobacillus; Companilactobacillus farciminis_A
• CAZyme ID: MGYG000000822_00639
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
319	MGYG000000822_5|CGC2	35064.66	6.217

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000822	2370791	MAG	China	Asia

• Gene Location: Start: 36501; End: 37460 Strand: -

Full Sequence      

MSKKKISAIIATIVSLVTLFFCVTTVDAARMDMVDVSNHNGAMTIANFQDMHNNYGVKAA
VTKISEGTTYKDAYAANNIKTAQAAGLYIHGYHYAHYSNVNEAIAEADFAAQTAKADGLP
AGAVLVTDVESTEQQHNNPETNTQSNIAFINQVAKYGYRSDIYTMGSWANLVMQVKKGWI
AAYPSDATDQYWYPNAHGWQWTSHYQFDGSYGNFDVSQLYDNYFTSYQAPQTVSVDNSNQ
TNNNSTNNAISSKGVISVNNANGSYVPLVAIQNNSTKTITNRALANNTPWVTDQTKTIDG
VTYHRVATNEWVDAKYIVG

Enzyme Prediction     

No EC number prediction in MGYG000000822_00639.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	34	209	6.6e-35	0.9887005649717514

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06522	GH25_AtlA-like	1.83e-59	31	220	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	4.53e-31	34	209	1	179	Glycosyl hydrolases family 25.
cd06415	GH25_Cpl1-like	2.33e-23	34	216	4	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.
cd00599	GH25_muramidase	1.02e-22	33	217	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.
cd06414	GH25_LytC-like	5.38e-16	34	220	4	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QMT84165.1	4.46e-227	1	319	1	319
QCX24641.1	2.63e-217	1	319	1	320
ATO46321.1	8.55e-191	4	318	3	320
APU71289.1	1.24e-148	6	318	3	320
AYE38332.1	1.46e-134	3	317	4	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
0.000215	0.999200	0.000173	0.000156	0.000142	0.000132

TMHMM  Annotations     

start	end
7	29