CAZyme Information: MGYG000002542_00513

Basic Information

• Species: Lentilactobacillus parafarraginis
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Lentilactobacillus; Lentilactobacillus parafarraginis
• CAZyme ID: MGYG000002542_00513
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
238	MGYG000002542_26|CGC1	26207.46	9.8362

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002542	2852137	Isolate	not provided	not provided

• Gene Location: Start: 35769; End: 36485 Strand: -

Full Sequence      

MKKFASLKLTALTLAAFGLLAFSATSLPVQANTFSANHPNADMVDISAYQGAQTNLGLQN
MKDAGVQAMTIKATEGTYYTNPLLAQQTQTAQSAGLSINFYHYANFTTKAQAKREAKYFV
KHVEAVTSQRDVVMAIDFEASKLANLPIATNDRNIKAFNKVVQKAGFTKTDIYTNANWVD
SYVSMNSKNLGWLANYPNNPTGKKYAAANAWQWTSNFKFSGTGRTDVSQLNNDYYLND

Enzyme Prediction     

No EC number prediction in MGYG000002542_00513.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	44	221	8.7e-38	0.9887005649717514

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06522	GH25_AtlA-like	1.45e-48	42	229	2	190	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	1.36e-36	44	221	1	179	Glycosyl hydrolases family 25.
cd00599	GH25_muramidase	6.87e-25	43	233	2	182	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	8.56e-20	44	216	3	169	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	8.67e-19	44	228	4	188	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
QHB50839.1	4.87e-136	1	238	1	239
QIR08200.1	2.01e-112	1	238	1	210
QIR08201.1	1.58e-73	35	237	14	217
QHB50840.1	2.86e-73	35	237	35	238
ANZ60387.1	8.79e-71	33	236	33	237

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	1.26e-12	40	223	19	193	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	3.37e-12	40	223	19	193	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]
5A6S_A	5.80e-08	43	234	24	205	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
1JFX_A	8.53e-06	44	231	8	203	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
P26836	9.56e-12	37	142	5	106	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P34020	6.37e-07	43	196	1	146	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

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
0.000255	0.999035	0.000176	0.000194	0.000171	0.000144

TMHMM  Annotations     

start	end
7	29