| IED ID |
IndEnz0002016216 |
| Enzyme Type ID |
protease016216 |
| Protein Name |
Lantibiotic epilancin
|
| Gene Name |
elkA |
| Organism |
Staphylococcus epidermidis |
| Taxonomic Lineage |
cellular organisms
Bacteria
Terrabacteria group
Firmicutes
Bacilli
Bacillales
Staphylococcaceae
Staphylococcus
Staphylococcus epidermidis
|
| Enzyme Sequence |
MNNSLFDLNLNKGVETQKSDLSPQSASVLKTSIKVSKKYCKGVTLTCGCNITGGK |
| Enzyme Length |
55 |
| Uniprot Accession Number |
Q57312 |
| Absorption |
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| Active Site |
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| Activity Regulation |
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| Binding Site |
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| Calcium Binding |
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| catalytic Activity |
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| DNA Binding |
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| EC Number |
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| Enzyme Function |
FUNCTION: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria such as staphylococci, enterococci and streptococci (By similarity). The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores (By similarity). {ECO:0000250|UniProtKB:P86047}. |
| Temperature Dependency |
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| PH Dependency |
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| Pathway |
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| nucleotide Binding |
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| Features |
Cross-link (3); Modified residue (5); Peptide (1); Propeptide (1) |
| Keywords |
Antibiotic;Antimicrobial;Bacteriocin;D-amino acid;Direct protein sequencing;Lantibiotic;Thioether bond |
| Interact With |
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| Induction |
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| Subcellular Location |
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| Modified Residue |
MOD_RES 25; /note="D-lactate; by the dehydratase ElxB and the dehydrogenase ElxO"; /evidence="ECO:0000250|UniProtKB:P86047, ECO:0000269|PubMed:7607233"; MOD_RES 27; /note="2,3-didehydroalanine (Ser); by the dehydratase ElxB"; /evidence="ECO:0000250|UniProtKB:P86047, ECO:0000269|PubMed:7607233"; MOD_RES 31; /note="2,3-didehydrobutyrine; by the dehydratase ElxB"; /evidence="ECO:0000250|UniProtKB:P86047, ECO:0000269|PubMed:7607233"; MOD_RES 32; /note="2,3-didehydroalanine (Ser); by the dehydratase ElxB"; /evidence="ECO:0000250|UniProtKB:P86047, ECO:0000269|PubMed:7607233"; MOD_RES 52; /note="2,3-didehydrobutyrine; by the dehydratase ElxB"; /evidence="ECO:0000250|UniProtKB:P86047, ECO:0000269|PubMed:7607233" |
| Post Translational Modification |
PTM: Maturation of this lantibiotic involves the enzymatic conversion of Thr, and Ser into dehydrated AA by ElxB and the formation of thioether bonds with cysteine by the cyclase ElxC (By similarity). The next steps are cleavage of the leader peptide by ElxP and membrane translocation by ElxT (By similarity). The leader peptide may be removed before membrane translocation, in contrast to other lantibiotics for which the cleavage occur after translocation (By similarity). This is suggested by the probable cytoplasmic localization of the serine protease ElxP that cleaves the leader peptide (By similarity). {ECO:0000250|UniProtKB:P86047}.; PTM: It is not established whether the 2,3-didehydrobutyrine is the E- or Z-isomer. {ECO:0000269|PubMed:7607233}.; PTM: The N-terminal D-lactate is probably produced by dehydration of Ser-25 by ElxB, followed by proteolytic removal of the leader peptide by the serine protease ElxP and hydrolysis of the resulting new N-terminal dehydroalanine (By similarity). This hydrolysis may occur spontaneously (Probable). The pyruvate group thus formed is reduced to D-lactate by the NADPH-dependent oxidoreductase ElxO (By similarity). This N-terminal D-lactate protects the lantibiotic against degradation against aminopeptidase (By similarity). {ECO:0000250|UniProtKB:P86047, ECO:0000305|PubMed:7607233}. |
| Signal Peptide |
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| Structure 3D |
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| Cross Reference PDB |
- |
| Mapped Pubmed ID |
- |
| Motif |
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| Gene Encoded By |
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| Mass |
5,851 |
| Kinetics |
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| Metal Binding |
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| Rhea ID |
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| Cross Reference Brenda |
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