CAZyme Information: MGYG000004046_01515

Basic Information

• Species: Limosilactobacillus vaginalis
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Limosilactobacillus; Limosilactobacillus vaginalis
• CAZyme ID: MGYG000004046_01515
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
375	MGYG000004046_43|CGC1	42747.4	4.7823

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004046	1731903	MAG	United Kingdom	Europe

• Gene Location: Start: 1188; End: 2315 Strand: +

Full Sequence      

MALYTVDVYSGSSDSIIRDSHADGVIVKATQGTSYVNPRCNHQWDLAGQLGKLRGLYHYA
GGGNPESEAQYFINNIKNYVGQGILILDWESYQNSSWGDASWSLRFVTEVHRLTGVWPLI
YVQESALWQVANCAQYCGGWVAKYASMTWNSWTLPNMSVSASAFGALTGWQFTGGDMDRS
IFYLTKEAWMKIANPSGSKDGWQGSGDTWQYFENGSAVKNDWRKVDNRWYYLDESGNTVT
GWRKINNRWYYFDVNHDGTFGAALTGWQQINDHWYYMDSDNTWCLTGWQEINGKKYYFDP
DNAWMLTGRQEIDGKLYVFGDDGALQTPIENQPADLKPSKTETETKLTAVDREVIENDLK
PYIQSIIKAEIAKEK

Enzyme Prediction     

No EC number prediction in MGYG000004046_01515.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	16	174	3.1e-30	0.8813559322033898

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06417	GH25_LysA-like	7.54e-60	6	189	4	195	LysA is a cell wall endolysin produced by Lactobacillus fermentum, which degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. The N-terminal glycosyl hydrolase family 25 (GH25) domain of LysA has sequence similarity with other murein hydrolase catalytic domains while the C-terminal domain has sequence similarity with putative bacterial cell wall-binding SH3b domains. This domain family also includes LysL of Lactococcus lactis.
cd00599	GH25_muramidase	4.71e-28	6	182	3	186	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.
NF033930	pneumo_PspA	4.06e-24	168	327	463	603	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.
NF033838	PspC_subgroup_1	3.75e-22	191	327	477	606	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.
NF033840	PspC_relate_1	7.64e-22	187	310	497	619	PspC-related protein choline-binding protein 1. Members of this family share C-terminal homology to the choline-binding form of the pneumococcal surface antigen PspC, but not to its allelic LPXTG-anchored forms because they lack the choline-binding repeat region. Members of this family should not be confused with PspC itself, whose identity and function reflect regions N-terminal to the choline-binding region. See Iannelli, et al. (PMID: 11891047) for information about the different allelic forms of PspC.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AIY32273.1	2.07e-122	1	199	1	199
QKT15002.1	1.56e-117	2	198	3	199
AEI58326.1	9.95e-116	1	198	1	198
ATP34759.1	3.13e-112	1	195	1	195
QLL72790.1	4.44e-112	1	195	1	195

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6ZM8_A	1.99e-12	25	176	27	190	ChainA, muramidase [Sodiomyces alcalophilus]
6ZMV_A	3.27e-08	19	178	21	191	ChainA, muramidase [Trichobolus zukalii],6ZMV_B Chain B, muramidase [Trichobolus zukalii]
2X8R_A	3.39e-08	22	154	26	181	Thestructure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_B The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_C The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_D The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_E The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_F The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P00721	4.18e-08	25	125	27	142	N,O-diacetylmuramidase OS=Chalaropsis sp. OX=36534 PE=1 SV=1

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
1.000027	0.000007	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004046_01515.