CAZyme Information: MGYG000002386_03081

Basic Information

• Species: Lactiplantibacillus plantarum
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Lactiplantibacillus; Lactiplantibacillus plantarum
• CAZyme ID: MGYG000002386_03081
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
899	MGYG000002386_1|CGC42	99154.42	9.5758

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002386	3412302	Isolate	China	Asia

• Gene Location: Start: 3190721; End: 3193420 Strand: +

Full Sequence      

MNFKTHNHINAKTTKRFKLYKSGKLWLVAGVTFCSFVGSAIINDQIAHADTVTVAKTATT
VTRTTVSADSKTSNDSASSDTVSTTANKVANTASNIAHQPNSATTNLNTSQAATATSSTT
TKAASSILSQADSETANSNTSQAVTATSSAATEAVSSAANQTGQKVSSSNNKSHEATAHT
TSAASGSINQVSSTAIKSATSTENTNKATSVASNAAKHQATTTKKADLNLTTVTASTPET
DVWTIGDTTRPRVDVVDVASYQSAMTQSDYNKLKAAGVKTVIIKTTEGTGYTNPVALAQA
KMANAAGLNVDFYHYATFNTADTAQMEATNMANFLVKNNVSKKVLLFADMEDAKTYTVNA
TANLNTFWSVLNALGYTNHGVYTSNTYLYRDAVIKTVGQSRVWRAQYPYTPSANNLWNTE
GGAWQFSSTALLPSGSDYTGYIDVSICYNGLTEDSAGTNTFSTPNEFVNQYHWEGNKLYF
YGSNGQPITGFRHYGNNKLEYYGSDHAQYRNRYLTAANNQLYYFGSNGDAITGLRHYANN
KLEYYGTDHIQYRNRYATVGNNKLYYFGSNGDAISGLRHYGNNKLEFYGTDHIQYRNRYY
TAAKNKLYYFGGNGDAITGLRHYGHNKLEYYGNDHVQYRNRYYTAAKNRLYYFGSNGDAI
SGLRHYGNNKLEFYGTDHIQYRNRYYTAAKNKLYYFGDNGDAITGLRHYGNNKLEYYGAD
HVQYRNRYATVNNQLYYFGSNGDAITGLRHYGNNKLEYYGADHVQYRNRYYTAAKNKLYY
FGGNGDAITGLRHYGNNKLEFYGTDHIQYRNRYVTVGNHRYYFGSNGDAVSTNQPQTEAD
IIGSMRVAQKAQQIVTVVQNGGSTATLKLWQKQGNTWRNLLTSSSRIGNGGIGNSHEGN

Enzyme Prediction     

No EC number prediction in MGYG000002386_03081.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	256	432	1.7e-31	0.9774011299435028

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06522	GH25_AtlA-like	1.13e-71	253	448	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	8.78e-23	256	433	1	178	Glycosyl hydrolases family 25.
cd00599	GH25_muramidase	1.35e-17	255	446	2	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.
cd06525	GH25_Lyc-like	5.24e-14	256	434	3	174	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.
cd06414	GH25_LytC-like	5.18e-13	255	448	3	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
AYA98179.1	4.14e-291	1	899	27	925
AYG33503.1	4.14e-291	1	899	27	925
ALV16002.1	4.14e-291	1	899	27	925
QTL10694.1	1.34e-289	1	899	27	925
ADO00167.1	1.34e-289	1	899	27	925

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
0.065997	0.909480	0.023019	0.000598	0.000404	0.000504

TMHMM  Annotations     

start	end
25	42