CAZyme Information: MGYG000001293_01977

Basic Information

• Species: Lacticaseibacillus rhamnosus
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Lacticaseibacillus; Lacticaseibacillus rhamnosus
• CAZyme ID: MGYG000001293_01977
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
392	MGYG000001293_1|CGC25	42571.9	6.301

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001293	3010111	Isolate	not provided	not provided

• Gene Location: Start: 2047790; End: 2048968 Strand: -

Full Sequence      

MTQNDYTQLHNLGIKGVVVKVTEGTYYTNGIAANQIKFARNAGMVVSAYHYATFDSASAA
VAEANYFANRLDSLNVGKNVTVVADIESDAVSGDIAGNLKAFWQTMTQRGYQNHVAYTMR
YYKHLDALTSTTGKDRTWIAQYPYTPSANSLWDQDFGAWQFSSTGHLPGHSQNLDVSIDY
QGLFTRENGAASTSTAPSSVSYDPIVSQKTVSYSGSLDQSVRADGLYASAPFYTSAATSV
GNTAAKAYNGAHFTALQEETTAKGTFVQIRFNNGSVYWIDKRALAIEQYDTVTSKTPVSY
TGSLDQNSRADGLYTAGPFFTSVATAIGNTNAKALNGQHFTALEEDTTAKGTFVEIKLND
GKIYWVDKRALAIDRYDKVISTTAVSYTGSFD

Enzyme Prediction     

No EC number prediction in MGYG000001293_01977.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	5	169	4.2e-34	0.9322033898305084

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06522	GH25_AtlA-like	1.22e-87	1	180	13	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	1.24e-28	5	170	11	180	Glycosyl hydrolases family 25.
cd00599	GH25_muramidase	4.47e-25	13	178	21	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.
cd06415	GH25_Cpl1-like	6.76e-16	5	176	13	195	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.
cd06414	GH25_LytC-like	4.77e-14	5	180	14	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
AZZ23551.1	6.01e-284	1	392	26	417
AON63595.1	6.01e-284	1	392	26	417
CAR87896.1	6.01e-284	1	392	26	417
AQY35141.1	6.01e-284	1	392	26	417
AXI94880.1	6.01e-284	1	392	26	417

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5JQC_A	1.62e-10	202	387	14	190	Crystalstructure putative autolysin from Listeria monocytogenes [Listeria monocytogenes EGD-e]
4KRU_A	2.79e-10	5	184	33	212	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	7.56e-10	5	184	33	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]
1JFX_A	1.92e-06	5	175	18	198	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P34020	2.68e-09	5	183	14	184	Autolytic lysozyme OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=lyc PE=1 SV=1
P26836	2.96e-06	5	177	22	194	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2

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
1.000051	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001293_01977.