LANEL_STAEP
ID LANEL_STAEP Reviewed; 55 AA.
AC Q57312;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 41.
DE RecName: Full=Lantibiotic epilancin;
DE Flags: Precursor;
GN Name=elkA;
OS Staphylococcus epidermidis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1282;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 25-55, AND
RP DEHYDRATION AT SER-27; THR-31; SER-32 AND THR-52.
RC STRAIN=K7;
RX PubMed=7607233; DOI=10.1111/j.1432-1033.1995.tb20600.x;
RA Van de Kamp M., Van den Hooven H.W., Konings R.N.H., Bierbaum G.,
RA Sahl H.-G., Kuipers O.P., Siezen R.J., de Vos W.M., Hilbers C.W.,
RA Van de Ven F.J.M.;
RT "Elucidation of the primary structure of the lantibiotic epilancin K7 from
RT Staphylococcus epidermidis K7. Cloning and characterisation of the
RT epilancin-K7-encoding gene and NMR analysis of mature epilancin K7.";
RL Eur. J. Biochem. 230:587-600(1995).
CC -!- FUNCTION: Lanthionine-containing peptide antibiotic (lantibiotic)
CC active on Gram-positive bacteria such as staphylococci, enterococci and
CC streptococci (By similarity). The bactericidal activity of lantibiotics
CC is based on depolarization of energized bacterial cytoplasmic
CC membranes, initiated by the formation of aqueous transmembrane pores
CC (By similarity). {ECO:0000250|UniProtKB:P86047}.
CC -!- PTM: Maturation of this lantibiotic involves the enzymatic conversion
CC of Thr, and Ser into dehydrated AA by ElxB and the formation of
CC thioether bonds with cysteine by the cyclase ElxC (By similarity). The
CC next steps are cleavage of the leader peptide by ElxP and membrane
CC translocation by ElxT (By similarity). The leader peptide may be
CC removed before membrane translocation, in contrast to other
CC lantibiotics for which the cleavage occur after translocation (By
CC similarity). This is suggested by the probable cytoplasmic localization
CC of the serine protease ElxP that cleaves the leader peptide (By
CC similarity). {ECO:0000250|UniProtKB:P86047}.
CC -!- PTM: It is not established whether the 2,3-didehydrobutyrine is the
CC E- or Z-isomer. {ECO:0000269|PubMed:7607233}.
CC -!- PTM: The N-terminal D-lactate is probably produced by dehydration of
CC Ser-25 by ElxB, followed by proteolytic removal of the leader peptide
CC by the serine protease ElxP and hydrolysis of the resulting new N-
CC terminal dehydroalanine (By similarity). This hydrolysis may occur
CC spontaneously (Probable). The pyruvate group thus formed is reduced to
CC D-lactate by the NADPH-dependent oxidoreductase ElxO (By similarity).
CC This N-terminal D-lactate protects the lantibiotic against degradation
CC against aminopeptidase (By similarity). {ECO:0000250|UniProtKB:P86047,
CC ECO:0000305|PubMed:7607233}.
CC -!- SIMILARITY: Belongs to the type A lantibiotic family. {ECO:0000305}.
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DR EMBL; X87412; CAA60860.1; -; Genomic_DNA.
DR EMBL; U20348; AAA79236.1; -; Genomic_DNA.
DR PIR; S65681; S65681.
DR AlphaFoldDB; Q57312; -.
DR TCDB; 1.C.20.1.7; the nisin (nisin) family.
DR GO; GO:0005102; F:signaling receptor binding; IEA:UniProtKB-KW.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Bacteriocin; D-amino acid;
KW Direct protein sequencing; Lantibiotic; Thioether bond.
FT PROPEP 1..24
FT /note="Cleaved by ElxP"
FT /evidence="ECO:0000250|UniProtKB:P86047,
FT ECO:0000269|PubMed:7607233"
FT /id="PRO_0000275927"
FT PEPTIDE 25..55
FT /note="Lantibiotic epilancin"
FT /evidence="ECO:0000269|PubMed:7607233"
FT /id="PRO_0000275928"
FT MOD_RES 25
FT /note="D-lactate; by the dehydratase ElxB and the
FT dehydrogenase ElxO"
FT /evidence="ECO:0000250|UniProtKB:P86047,
FT ECO:0000269|PubMed:7607233"
FT MOD_RES 27
FT /note="2,3-didehydroalanine (Ser); by the dehydratase ElxB"
FT /evidence="ECO:0000250|UniProtKB:P86047,
FT ECO:0000269|PubMed:7607233"
FT MOD_RES 31
FT /note="2,3-didehydrobutyrine; by the dehydratase ElxB"
FT /evidence="ECO:0000250|UniProtKB:P86047,
FT ECO:0000269|PubMed:7607233"
FT MOD_RES 32
FT /note="2,3-didehydroalanine (Ser); by the dehydratase ElxB"
FT /evidence="ECO:0000250|UniProtKB:P86047,
FT ECO:0000269|PubMed:7607233"
FT MOD_RES 52
FT /note="2,3-didehydrobutyrine; by the dehydratase ElxB"
FT /evidence="ECO:0000250|UniProtKB:P86047,
FT ECO:0000269|PubMed:7607233"
FT CROSSLNK 36..40
FT /note="Lanthionine (Ser-Cys); by the dehydratase ElxB and
FT the cyclase ElxC"
FT /evidence="ECO:0000250|UniProtKB:P86047,
FT ECO:0000269|PubMed:7607233"
FT CROSSLNK 44..47
FT /note="Beta-methyllanthionine (Thr-Cys); by the dehydratase
FT ElxB and the cyclase ElxC"
FT /evidence="ECO:0000250|UniProtKB:P86047,
FT ECO:0000269|PubMed:7607233"
FT CROSSLNK 46..49
FT /note="Beta-methyllanthionine (Thr-Cys); by the dehydratase
FT ElxB and the cyclase ElxC"
FT /evidence="ECO:0000250|UniProtKB:P86047,
FT ECO:0000269|PubMed:7607233"
SQ SEQUENCE 55 AA; 5851 MW; 28311B7C49951D7C CRC64;
MNNSLFDLNL NKGVETQKSD LSPQSASVLK TSIKVSKKYC KGVTLTCGCN ITGGK
