CAZyme Information: MGYG000000155_00583

Basic Information

• Species: Weissella confusa
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Weissella; Weissella confusa
• CAZyme ID: MGYG000000155_00583
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
873		98167.26	5.1959

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000155	2346100	Isolate	China	Asia

• Gene Location: Start: 146581; End: 149202 Strand: -

Full Sequence      

MLGQQDFEWGAYHYSTYSTTSEATAEANYFVDTAQSLGLSDTTYMVDDLEAESTKTSNTT
QLAETFKRQVNNRGYGKTLLYTYASYTQQQGLKFNAWDDKNVWMASYPAKPSKDNLWYTN
YGMWQWNSKTNFPGITGTYDVSIDYDNLSASGDYVTTQRDVNYFGTFNQSNRNDGLYPDY
PWNTGGDQYVGSATQYNGQQVVITKEAVTNKGTTWAGFYLNGRLIWVDKAALSNVSTGIS
INKRAMFIQKNRNDGLFTNAPYGMINPSGIGSVSATGNDRKAVTVERQITVNGVLWYGGY
IDGIMTWFDAQAVVQDDTAPVDKNYVATINENGRNDSIYEDKPWEYRSKSLGLANQLSGR
TILVTGEWTTPDGVTWVRFSWNGKTVWVDKQAVSQSSISDVQSIQKRALFEQNGRNDSFY
SNAPYGVLGASGAGMVGTSNQHKSITVEKKVVVNGVLWYGGYIDGKFLWFDSKAVIEDNS
APKPVKYSMEITQSKRNDSLYLEKPWEYRSDYYKAAKEFEGQVVQVRNEWKTPDGVTWIN
FTVDNRNVWMDKSGASTVDAADVHQRAMFIQNDRNDGLYLNAPYGSKGAQYVGSVKSTGN
DRKSITVEKSVIKNNVTWYGGNLDGKFYWFDSAAVVEDNSNPVAVNKQMVISQFNRNDGI
YEGKPWEYRSNYVQSATQLNNKTVTVTQEWTTPDGVTWSGFQLNGRLVWIDSQGITNSIS
KRALFIQNGRNDGLYKDAPYGLQGAHYIGSVDSTNNTRHSITVEREVVLNGVTWYGGYLN
GELYWFDSLAVVEDNSSAVAANYDAVVRQDGRNDGLYRDKPWEYRTQWISSAQKLAGQKI
HVVSEWQTPDGVTWVGFNWNNQLVWLDKAGIAQ

Enzyme Prediction     

No EC number prediction in MGYG000000155_00583.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	5	135	9.6e-23	0.7288135593220338

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06522	GH25_AtlA-like	1.85e-35	10	145	59	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	6.79e-20	10	135	53	180	Glycosyl hydrolases family 25.
cd00599	GH25_muramidase	1.71e-14	9	143	54	185	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	4.06e-14	9	145	58	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.
cd06523	GH25_PlyB-like	6.50e-10	10	142	56	175	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
QYU58648.1	5.48e-217	10	873	102	977
QYU58650.1	1.13e-111	152	635	189	673
AIM64427.1	1.74e-108	10	635	99	736
AIM63028.1	1.74e-108	10	635	99	736
AIG65712.1	1.74e-108	10	635	99	736

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000064	0.000002	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000155_00583.