ID   SAKA_LATCU              Reviewed;          59 AA.
AC   P0A311; P35619; P80097;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Bacteriocin curvacin-A;
DE   Flags: Precursor;
GN   Name=curA;
OS   Latilactobacillus curvatus (Lactobacillus curvatus).
OG   Plasmid 60 kb.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Latilactobacillus.
OX   NCBI_TaxID=28038;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LTH1174;
RX   PubMed=7694558; DOI=10.1007/bf00292077;
RA   Tichaczek P.S., Vogel R.F., Hammes W.P.;
RT   "Cloning and sequencing of curA encoding curvacin A, the bacteriocin
RT   produced by Lactobacillus curvatus LTH1174.";
RL   Arch. Microbiol. 160:279-283(1993).
RN   [2]
RP   PRELIMINARY PROTEIN SEQUENCE OF 19-59.
RC   STRAIN=LTH1174;
RA   Tichaczek P.S., Nissen-Meyer J., Nes I.F., Vogel R.F., Hammes W.P.;
RT   "Characterization of the bacteriocins curvacin A from Lactobacillus
RT   curvatus LTH1174 and sakacin P from L. sake LTH673.";
RL   Syst. Appl. Microbiol. 15:460-465(1992).
RN   [3]
RP   STRUCTURE BY NMR OF 19-59, AND DISULFIDE BOND.
RX   PubMed=16331975; DOI=10.1021/bi051215u;
RA   Haugen H.S., Fimland G., Nissen-Meyer J., Kristiansen P.E.;
RT   "Three-dimensional structure in lipid micelles of the pediocin-like
RT   antimicrobial peptide curvacin A.";
RL   Biochemistry 44:16149-16157(2005).
CC   -!- FUNCTION: Bactericidal activity; inhibits closely related Lactobacilli,
CC       Listeria monocytogenes and ivanovvi, Enterococcus faecalis,
CC       Carnobacterium sp and Brocothrix thermosphacta.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the bacteriocin class IIA/YGNGV family.
CC       {ECO:0000305}.
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DR   EMBL; S67323; AAB28845.1; -; Genomic_DNA.
DR   EMBL; X72223; CAA51023.1; -; Genomic_DNA.
DR   PDB; 2A2B; NMR; -; A=19-59.
DR   PDBsum; 2A2B; -.
DR   AlphaFoldDB; P0A311; -.
DR   SMR; P0A311; -.
DR   EvolutionaryTrace; P0A311; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.5.130; -; 1.
DR   InterPro; IPR002633; Bacteriocin_IIa.
DR   InterPro; IPR023384; Bacteriocin_IIa_CS.
DR   InterPro; IPR023388; Bacteriocin_IIa_dom_sf.
DR   InterPro; IPR010133; Bacteriocin_signal_seq.
DR   Pfam; PF01721; Bacteriocin_II; 1.
DR   TIGRFAMs; TIGR01847; bacteriocin_sig; 1.
DR   PROSITE; PS60030; BACTERIOCIN_IIA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic; Antimicrobial; Bacteriocin;
KW   Direct protein sequencing; Disulfide bond; Plasmid; Secreted.
FT   PROPEP          1..18
FT                   /id="PRO_0000002747"
FT   CHAIN           19..59
FT                   /note="Bacteriocin curvacin-A"
FT                   /id="PRO_0000002748"
FT   DISULFID        28..33
FT                   /evidence="ECO:0000269|PubMed:16331975"
FT   CONFLICT        20
FT                   /note="R -> C (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        33
FT                   /note="C -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          22..24
FT                   /evidence="ECO:0007829|PDB:2A2B"
FT   STRAND          29..32
FT                   /evidence="ECO:0007829|PDB:2A2B"
FT   HELIX           37..42
FT                   /evidence="ECO:0007829|PDB:2A2B"
FT   HELIX           47..57
FT                   /evidence="ECO:0007829|PDB:2A2B"
SQ   SEQUENCE   59 AA;  6257 MW;  CEE4B0EB5470574A CRC64;
     MNNVKELSMT ELQTITGGAR SYGNGVYCNN KKCWVNRGEA TQSIIGGMIS GWASGLAGM