CAZyme Information: MGYG000000097_01830

Basic Information

• Species: Ligilactobacillus animalis
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Ligilactobacillus; Ligilactobacillus animalis
• CAZyme ID: MGYG000000097_01830
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
771	MGYG000000097_14|CGC1	88653.75	4.8162

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000097	1849821	Isolate	Canada	North America

• Gene Location: Start: 9892; End: 12207 Strand: -

Full Sequence      

MDYRRKKKALASYRKMNKRKIWLASGMTMMAISTGMYATQNVKADQVSVEAQNTQQVVTD
KDSSNVSNEQNDQTTVQLDQQVSEQKDVQNESSSTSDQAKVDLNDTAQEDNTNATDQAQN
KDELSTEDVVDDTNATQELQLTTDEKQANENVAENAQAQQLQVNKVATKMQTPDAIYIGD
SQYTRGDAIDVASYQSWLNQDDFNKLKQLGIKAVVVKLTEGQSYVNPAATKQINYAKNAG
LTVSIYHYARFNDAATGYAEGQHVVNTMENLGLGQDTLVFADMEDHSTYSNDVRGNLNSF
WNALTAAGFNNRGVYTGGGYPYYEAAIATVGRAKTWWSQYPFVPTNNGYYEQEWRNLGYG
AWQFSSTAYLPGRENMGALDLSIDFNGLFSKSDTAEKPVTQQVFKDGHWYLFDQVTGAMQ
YGFQSLSPYGQDKTVYYANNGQMQYGQQKIDGYWYNFDVVDGAMKTGLVQIPEQNKTVYY
ANNGRMQYGWQWVNNATRYFDTFNGAMVTGQQKINGHWYLFDNSGAMQRGFQNLKAYGDD
KTVYYNQDGWMLYGWQGIDNVPYYFDTFNGAMMTGERYINGHWYLFNDKGQMQRGFQKVM
ENGKEKTVYYNYDGWRLYGWQGIDNVPYYFDKSTGAMMTGERYLNGHWYLFNDKGQMQRG
FQKVMENGKEKTVYYNYDGWMLYGWQGINDVPYYFDTFNGAMMTGERYINGHWYLFNDKG
QMQRGFQKVMENGKEKTVYYNYDGWMLYGWQTINGKRYYFDTFNGALLKEE

Enzyme Prediction     

No EC number prediction in MGYG000000097_01830.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	189	372	6e-31	0.9887005649717514

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06522	GH25_AtlA-like	4.69e-59	187	385	2	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	1.98e-24	189	372	1	179	Glycosyl hydrolases family 25.
NF033930	pneumo_PspA	1.34e-22	463	720	440	640	pneumococcal surface protein A. The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.
cd00599	GH25_muramidase	4.38e-21	189	383	3	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.
NF033838	PspC_subgroup_1	9.12e-21	390	655	439	663	pneumococcal surface protein PspC, choline-binding form. The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AWZ39196.1	2.13e-101	1	390	1	423
AWZ40161.1	2.13e-101	1	390	1	423
QCQ03274.1	2.96e-100	1	390	1	423
QHQ69357.1	7.76e-99	393	767	119	512
QIA89409.1	6.93e-83	407	768	288	651

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P29336	2.24e-14	529	769	1137	1364	Glucosyltransferase-S OS=Streptococcus downei OX=1317 GN=gtfS PE=3 SV=1
P49331	2.75e-11	512	767	1121	1372	Glucosyltransferase-S OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=gtfD PE=3 SV=3
P34020	2.48e-08	189	380	4	178	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
0.061289	0.927092	0.008353	0.002488	0.000457	0.000300

TMHMM  Annotations     

start	end
21	38