CAZyme Information: MGYG000002774_02201

Basic Information

• Species: Schleiferilactobacillus harbinensis
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Schleiferilactobacillus; Schleiferilactobacillus harbinensis
• CAZyme ID: MGYG000002774_02201
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
389	MGYG000002774_10|CGC6	42238.77	8.0124

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002774	3078759	MAG	United States	North America

• Gene Location: Start: 108948; End: 110117 Strand: +

Full Sequence      

MHSSRKKRVLLTAFLTFFVALFGFNSIAQATTYGMFADVASYQPDDVLFFKNLATNQVAG
VVVKITEGSGSGAYVNPKAANQIASAQAAGLKVSLYHYARYNGASAAKAEADFFAGQAAK
YGLGKDTVMVADVEDNSLSNPYGDTVTFQQELARLGYNNQVTYSMASWFWANKLPRNYPI
WVANYGVDKPGVDNAAAWQYTSNYNGQSVDMSYDFSGIFTTGSNTGTTTPSTGDTATINY
IPGYGIALWNGYGANRTYAGRTLLTGSKWKVLAQTYADGEYWYNLGGNQWIQGKYTYAPT
GMDGVTTINSNGSSNSKAITIKYVPGYGIALWNGYGASRKYAGRTLANASSWAVYGEKYV
DGEYWYNLGGDQWVEGQYTDSPNGLPAFQ

Enzyme Prediction     

No EC number prediction in MGYG000002774_02201.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	38	205	1.2e-34	0.9661016949152542

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06522	GH25_AtlA-like	1.69e-46	36	215	3	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	9.30e-28	38	205	2	176	Glycosyl hydrolases family 25.
cd00599	GH25_muramidase	3.07e-21	36	205	2	173	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	1.58e-20	36	210	3	190	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.
cd06523	GH25_PlyB-like	1.75e-15	35	214	1	177	PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus anthracis. PlyB has an N-terminal glycosyl hydrolase family 25 (GH25) catalytic domain and a C-terminal bacterial SH3-like domain, SH3b. Both domains are required for effective catalytic activity. Endolysins are produced by bacteriophages at the end of their life cycle and participate in lysing the bacterial cell in order to release the newly formed progeny. Endolysins (also referred to as endo-N-acetylmuramidases or peptidoglycan hydrolases) 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
QEU47539.1	8.18e-288	1	389	1	389
QFR24617.1	3.33e-287	1	389	1	389
QFR63074.1	4.73e-287	1	389	1	389
QFR62675.1	1.12e-215	1	389	1	413
QFR63075.1	6.21e-134	1	306	3	323

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	3.05e-09	50	203	34	192	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	7.48e-09	50	203	34	192	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
0.000244	0.999065	0.000181	0.000188	0.000153	0.000143

TMHMM  Annotations     

start	end
9	31