CAZyme Information: MGYG000000843_01058

Basic Information

• Species: Lacticaseibacillus sp900540605
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Lacticaseibacillus; Lacticaseibacillus sp900540605
• CAZyme ID: MGYG000000843_01058
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
929	MGYG000000843_10|CGC1	103063.52	8.9193

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000843	2470970	MAG	China	Asia

• Gene Location: Start: 1331; End: 4120 Strand: -

Full Sequence      

MQSRSYSKSRFASIVILGLGLFALAQAPGFIVKANDDVPNQVMGNVFSQQPHLVDSTTGI
MPVLGKGVPRTTLAKSVLAQARTAVVQNQPDVITIGDTNRPKVDAVDVASYQSWMQQSDY
NKLKSLGVQTVVVKVSQGNGYQKTAYFNSVSVNSIKYAQKAGLNVAVYDYATFNSAAAAK
SEADNTAYAMQKLGLSKDMLVFADMEDTKCNVAYLADYWSQLSVHGYHNQAVYTGGGYSG
AQQAVETVGASRTWWAQYPYSPKANSLWNTNYGAWQFSSTARIPGGSTSSLIDVSHDYKG
LLTTTVLPQGPKYADDRYVTVTSKNYITYNAFSFVGFLTNAQVYQRTFHSTGQYHHINGN
TYLSLYDNAGKWAGYINEKAVTVGKGHQGAWLSANKYATLTQANQKLLPAFDATTFSSTS
PYLNNTYHVTGEYHDINGDVYYSLYDQNSRWLGYIKSTAVTVTSQAQGPWQSDNRYVTVT
DSNYMTYSSFDFFGKMTNAQVYHRTFRSTGQYHHANGQTYLSLYDVSGGWAGYINARAVS
VGKGHQGAWLPADKYATLTQPNQKLLAGFDTAAMGSTSTYLNNTYHVTGEYHDINGDVFY
SIYDSTDHWLGYVKAAWVATSEQAQGIWQTKDGYVAPTKKGTIWASFDFLSGVSDQQYPL
LQVKGLYHHANGRVYYSVYDLKGKWIGYLDASLTKTQDQGLKQADDRYVTVTSQNYITYN
GFDFYGLLNNTQVYQHTFYSSGMYHHANGSTYLSIYDGAGKWAGYINEKAVTVGKGHQGA
WLPADKYATLTQPNQKLLAGFDTATMGSTSSHLDNTYHITGKYHDIDGRTFFSLYDTVGR
WLGYVQSDWVAVSSQPQGVWLQVDRTVQVVDQSYTIWASFDFLSGQKAAWYKTLKVKGEY
HHFNGSIFLSVYNPVTGAWIGYLNAKAVK

Enzyme Prediction     

No EC number prediction in MGYG000000843_01058.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	106	285	1.1e-22	0.9887005649717514

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06522	GH25_AtlA-like	1.20e-52	103	298	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	1.42e-14	106	285	1	179	Glycosyl hydrolases family 25.
cd00599	GH25_muramidase	9.36e-13	106	287	3	178	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	2.41e-09	106	285	4	180	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.
cd06525	GH25_Lyc-like	7.77e-08	106	285	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QIL47388.1	1.11e-127	93	773	129	819
AYW50604.1	2.26e-127	90	770	147	843
AYY10113.1	1.54e-107	93	771	138	815
QFG47130.1	3.15e-106	248	775	54	584
QDR75798.1	5.24e-106	97	691	40	645

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
0.000369	0.998831	0.000254	0.000185	0.000178	0.000161

TMHMM  Annotations     

start	end
13	32