LAN15_STAEP
ID LAN15_STAEP Reviewed; 55 AA.
AC P86047; I6YXA9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-AUG-2020, sequence version 2.
DT 25-MAY-2022, entry version 24.
DE RecName: Full=Lantibiotic epilancin 15X {ECO:0000303|PubMed:15792796};
DE Flags: Precursor;
GN Name=elxA {ECO:0000303|PubMed:21802007};
OS Staphylococcus epidermidis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1282;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=15X154;
RX PubMed=21802007; DOI=10.1016/j.chembiol.2011.05.007;
RA Velasquez J.E., Zhang X., van der Donk W.A.;
RT "Biosynthesis of the antimicrobial peptide epilancin 15X and its N-terminal
RT lactate.";
RL Chem. Biol. 18:857-867(2011).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 25-55, STRUCTURE BY NMR OF 25-55, MASS SPECTROMETRY,
RP FUNCTION, DEHYDRATION AT SER-27; THR-31; THR-32 AND THR-52, AND LANTHIONINE
RP AND METHYLLANTHIONINE CROSS-LINKS.
RC STRAIN=15X154;
RX PubMed=15792796; DOI=10.1016/j.febslet.2005.01.083;
RA Ekkelenkamp M.B., Hanssen M., Danny Hsu S.-T., de Jong A., Milatovic D.,
RA Verhoef J., van Nuland N.A.J.;
RT "Isolation and structural characterization of epilancin 15X, a novel
RT lantibiotic from a clinical strain of Staphylococcus epidermidis.";
RL FEBS Lett. 579:1917-1922(2005).
CC -!- FUNCTION: Lanthionine-containing peptide antibiotic (lantibiotic)
CC active on Gram-positive bacteria such as staphylococci, enterococci and
CC streptococci. The bactericidal activity of lantibiotics is based on
CC depolarization of energized bacterial cytoplasmic membranes, initiated
CC by the formation of aqueous transmembrane pores.
CC {ECO:0000269|PubMed:15792796}.
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 (Probable)
CC (PubMed:15792796). The next steps are cleavage of the leader peptide by
CC ElxP and membrane translocation by ElxT (Probable). The leader peptide
CC may be removed before membrane translocation, in contrast to other
CC lantibiotics for which the cleavage occur after translocation
CC (Probable). This is suggested by the probable cytoplasmic localization
CC of the serine protease ElxP that cleaves the leader peptide (Probable).
CC {ECO:0000269|PubMed:15792796, ECO:0000305|PubMed:21802007}.
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 (PubMed:21802007). This hydrolysis may occur
CC spontaneously (By similarity). The pyruvate group thus formed is
CC reduced to D-lactate by the NADPH-dependent oxidoreductase ElxO
CC (PubMed:21802007). This N-terminal D-lactate protects the lantibiotic
CC against degradation against aminopeptidase (PubMed:21802007).
CC {ECO:0000250|UniProtKB:Q57312, ECO:0000269|PubMed:21802007}.
CC -!- PTM: It is not established whether the 2,3-didehydrobutyrines are the
CC E- or Z-isomers. {ECO:0000269|PubMed:15792796}.
CC -!- MASS SPECTROMETRY: Mass=3172.75; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15792796};
CC -!- SIMILARITY: Belongs to the type A lantibiotic family. {ECO:0000255}.
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DR EMBL; JQ979180; AFN69432.1; -; Genomic_DNA.
DR PDB; 1W9N; NMR; -; A=25-55.
DR PDBsum; 1W9N; -.
DR AlphaFoldDB; P86047; -.
DR SMR; P86047; -.
DR EvolutionaryTrace; P86047; -.
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.
DR InterPro; IPR012519; Lantibiotic_typ-A_Pep5.
DR Pfam; PF08130; Antimicrobial18; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 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:0000269|PubMed:15792796,
FT ECO:0000269|PubMed:21802007"
FT /id="PRO_0000450387"
FT PEPTIDE 25..55
FT /note="Lantibiotic epilancin 15X"
FT /evidence="ECO:0000269|PubMed:15792796"
FT /id="PRO_0000379930"
FT MOD_RES 25
FT /note="D-lactate; by the dehydratase ElxB and the
FT dehydrogenase ElxO"
FT /evidence="ECO:0000269|PubMed:15792796,
FT ECO:0000269|PubMed:21802007"
FT MOD_RES 27
FT /note="2,3-didehydroalanine (Ser); by the dehydratase ElxB"
FT /evidence="ECO:0000269|PubMed:15792796,
FT ECO:0000305|PubMed:21802007"
FT MOD_RES 31
FT /note="2,3-didehydrobutyrine; by the dehydratase ElxB"
FT /evidence="ECO:0000269|PubMed:15792796,
FT ECO:0000305|PubMed:21802007"
FT MOD_RES 32
FT /note="2,3-didehydrobutyrine; by the dehydratase ElxB"
FT /evidence="ECO:0000269|PubMed:15792796,
FT ECO:0000305|PubMed:21802007"
FT MOD_RES 52
FT /note="2,3-didehydrobutyrine; by the dehydratase ElxB"
FT /evidence="ECO:0000269|PubMed:15792796,
FT ECO:0000305|PubMed:21802007"
FT CROSSLNK 36..40
FT /note="Lanthionine (Ser-Cys); by the dehydratase ElxB and
FT the cyclase ElxC"
FT /evidence="ECO:0000269|PubMed:15792796,
FT ECO:0000305|PubMed:21802007"
FT CROSSLNK 44..47
FT /note="Beta-methyllanthionine (Thr-Cys); by the dehydratase
FT ElxB and the cyclase ElxC"
FT /evidence="ECO:0000269|PubMed:15792796,
FT ECO:0000305|PubMed:21802007"
FT CROSSLNK 46..49
FT /note="Beta-methyllanthionine (Thr-Cys); by the dehydratase
FT ElxB and the cyclase ElxC"
FT /evidence="ECO:0000269|PubMed:15792796,
FT ECO:0000305|PubMed:21802007"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:1W9N"
SQ SEQUENCE 55 AA; 6130 MW; 9340248456813712 CRC64;
MKKELFDLNL NKDIEAQKSD LNPQSASIVK TTIKASKKLC RGFTLTCGCH FTGKK
