CAZyme Information: MGYG000000021_01837

Basic Information

• Species: Limosilactobacillus vaginalis_A
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Limosilactobacillus; Limosilactobacillus vaginalis_A
• CAZyme ID: MGYG000000021_01837
• CAZy Family: GH23
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
712		79334.79	4.4528

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000021	1945993	Isolate	United Kingdom	Europe

• Gene Location: Start: 15586; End: 17724 Strand: +

Full Sequence      

MSDLYSMVYIESADGKHAFRVDWNDLYNSFKRNFQLNSNYEISFTLTYTEQYRDVFNIAK
EKCWVWYDGQWFNIQQREVDSDENGFATLQITCTHTLIDSMKNVRLDKSQPTEDNPEISG
GDSSSNDSSDDSSDNQQAGTVIKETDNKQTTSLDACLHNFLDNNDQNIKYELHGNFPQAA
VECTGSLYDWLGQNLSLFSAYYVPDNYTLKIYDLDSLKHQTGKQFRYLHNMTNVDLQTDV
VDLVNDCEVYGGKMEKDITTASGNGATEPQNGDWTPVIQNAAGLVGEHLSQNDINLILAQ
INLESSGQEDAKGGDDGLSDGIAKGLLQFKQSTFDYYSRPPYTDIWHGLDQLVALMNVPN
WRNQITGHSGWSPQGAPISKATIQVQTGGNWGWPFPSVGEGSFSSGQLFGVQPGGGFRTN
GFHDGLDFGSVDHPGSEVHAIHGGTVTSIAWGGSEIKWYIVITDETGLNVEYQEAFSSRN
NFSVVMNQHVNTGDVIGYRDTDHLHIGITRHNIQEAFNHAFLNDGTWLDPLETIKNGGAS
GGSNEGGTTTTTEVYYLLHFHYQDEDSIKKYHLHRGAPIIQDSIYDMDALKQYVENTVQH
KPKAALTINGYSGNPGNLGDVWKLIAPELQLNMDVTLMGIQGNDEYFHPNGDQELSLNNT
GLAMKDAINAIWSDIREVNKNISVLDSFSGTGSRREDHFANENNKPGRDNNR

Enzyme Prediction     

No EC number prediction in MGYG000000021_01837.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam06605	Prophage_tail	4.87e-17	140	260	7	129	Prophage endopeptidase tail. This family is of prophage tail proteins that are probably acting as endopeptidases.
cd13402	LT_TF-like	6.36e-15	294	376	1	84	lytic transglycosylase-like domain of tail fiber-like proteins and similar domains. These tail fiber-like proteins are multi-domain proteins that include a lytic transglycosylase (LT) domain. Members of the LT family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, and the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL). LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.
pfam18994	Prophage_tailD1	8.50e-14	25	95	15	84	Prophage endopeptidase tail N-terminal domain. This domain represents the N-terminal domain of prophage tail proteins that are probably acting as endopeptidases. This domain has a RIFT related fold.
pfam06605	Prophage_tail	3.24e-10	562	666	137	246	Prophage endopeptidase tail. This family is of prophage tail proteins that are probably acting as endopeptidases.
cd12797	M23_peptidase	1.19e-09	423	508	1	85	M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins. This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QFS34324.1	3.33e-286	20	703	23	708
AKP01089.1	1.47e-270	18	701	19	715
QPB66444.1	1.47e-270	18	701	19	715
QBE45500.1	1.47e-270	18	701	19	715
AYN56739.1	1.63e-270	18	701	22	718

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5GT1_A	5.87e-56	391	539	25	172	ChainA, Choline binding protein A [Ligilactobacillus salivarius str. Ren]

Swiss-Prot Hits     

has no Swissprot hit.

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
1.000037	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000021_01837.