CAZyme Information: MGYG000000248_02018

Basic Information

• Species: Weissella cibaria
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Weissella; Weissella cibaria
• CAZyme ID: MGYG000000248_02018
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
334		36301.96	6.2567

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000248	2506217	Isolate	China	Asia

• Gene Location: Start: 95338; End: 96342 Strand: -

Full Sequence      

MNKTMKLVAVGAAFLFGTTLVSDHTVHADTPRFDMVDVSNWNGYLSVGDFVNMRNQGVKA
ITTKVSEGTWYQDPTAANNIANAQAAGLYVNGYYFAHATDNATAVQEANYAVATAQADGL
GVGAVLAVDAESPNQMAMGTAMQAVNATAEHQVGIAGGYRSTTYTMGSHVETTPDGDKSW
IAHYPYTPTASQNYYSSEHGWQWFDHATCDGVSGAFDITQLYDNFFTADQAVIKKNHGDS
ATVWSKGGVWYTDKSFKHKANGIKKHMGSYWSFANGKLIKSNWTNSWGLHYWSDGDGKLV
QGEGDWHGYHFNFGTDGTFNAKTATVNNLADIIK

Enzyme Prediction     

No EC number prediction in MGYG000000248_02018.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	36	212	2e-29	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06522	GH25_AtlA-like	4.68e-42	34	222	2	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	5.36e-17	36	212	1	180	Glycosyl hydrolases family 25.
cd00599	GH25_muramidase	5.56e-16	35	217	2	182	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.
cd06415	GH25_Cpl1-like	3.99e-14	36	219	4	196	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	1.58e-12	36	225	3	184	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
AVO66243.1	1.33e-231	1	334	1	334
AWF95155.1	3.82e-231	1	334	1	334
ALI33786.1	7.72e-231	1	334	1	334
AWF95387.1	1.39e-218	1	334	1	334
ALI33060.1	6.32e-215	1	334	1	334

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	5.25e-12	36	226	23	212	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	1.54e-11	36	226	23	212	X-raystructure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101],4KRT_B X-ray structure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]

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
0.000210	0.999143	0.000175	0.000175	0.000164	0.000145

TMHMM  Annotations     

start	end
7	26