ID   AMYL_LACAM              Reviewed;          65 AA.
AC   P80696; P81927; Q8GC39;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Bacteriocin amylovorin-L;
DE   AltName: Full=Amylovorin-L471;
DE   AltName: Full=Lactobin-A;
DE   Flags: Precursor;
GN   Name=amyL;
OS   Lactobacillus amylovorus.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1604;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LMG P-13139;
RX   PubMed=14672834; DOI=10.1016/s0168-1605(03)00298-8;
RA   De Vuyst L., Avonts L., Neysens P., Hoste B., Vancanneyt M., Swings J.,
RA   Callewaert R.;
RT   "The lactobin A and amylovorin L471 encoding genes are identical, and their
RT   distribution seems to be restricted to the species Lactobacillus amylovorus
RT   that is of interest for cereal fermentations.";
RL   Int. J. Food Microbiol. 90:93-106(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 16-65, AND MASS SPECTROMETRY.
RC   STRAIN=LMG P-13139;
RX   PubMed=8979334; DOI=10.1128/aem.63.1.13-20.1997;
RA   Contreras B.G.L., De Vuyst L., Devreese B., Busanyova K., Raymaeckers J.,
RA   Bosman F., Sablon E., Vandamme E.J.;
RT   "Isolation, purification, and amino acid sequence of lactobin A, one of the
RT   two bacteriocins produced by Lactobacillus amylovorus LMG P-13139.";
RL   Appl. Environ. Microbiol. 63:13-20(1997).
RN   [3]
RP   PROTEIN SEQUENCE OF 16-50.
RC   STRAIN=DCE 471;
RX   PubMed=10517609; DOI=10.1099/00221287-145-9-2559;
RA   Callewaert R., Holo H., Devreese B., Van Beeumen J., Nes I., De Vuyst L.;
RT   "Characterization and production of amylovorin L471, a bacteriocin purified
RT   from Lactobacillus amylovorus DCE 471 by a novel three-step method.";
RL   Microbiology 145:2559-2568(1999).
CC   -!- FUNCTION: This heat stable bacteriocin inhibits the growth of closely
CC       related Lactobacillus species. It may act as a pore-forming protein,
CC       creating a channel in the cell membrane. It kills Lactobacillus
CC       helveticus ATCC 15009, but displays no activity towards Listeria
CC       species.
CC   -!- SUBUNIT: Active lactobin is composed of two different peptides, one
CC       which is lactobin A.
CC   -!- SUBCELLULAR LOCATION: Secreted. Host cell membrane {ECO:0000305};
CC       Single-pass membrane protein {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=4879; Mass_error=0.69; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:8979334};
CC   -!- SIMILARITY: Belongs to the bacteriocin class IIB family. {ECO:0000305}.
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DR   EMBL; AJ301625; CAC82814.1; -; Genomic_DNA.
DR   RefSeq; WP_013642497.1; NZ_CP029754.1.
DR   AlphaFoldDB; P80696; -.
DR   TCDB; 1.C.22.1.8; the lactococcin a (lactococcin a) family.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; 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; IPR019493; Bacteriocin_IIb_lactacin-rel.
DR   InterPro; IPR010133; Bacteriocin_signal_seq.
DR   Pfam; PF10439; Bacteriocin_IIc; 1.
DR   TIGRFAMs; TIGR01847; bacteriocin_sig; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Bacteriocin; Direct protein sequencing;
KW   Host cell membrane; Host membrane; Membrane; Secreted; Transmembrane;
KW   Transmembrane helix.
FT   PROPEP          1..15
FT                   /evidence="ECO:0000269|PubMed:10517609,
FT                   ECO:0000269|PubMed:8979334"
FT                   /id="PRO_0000002757"
FT   CHAIN           16..65
FT                   /note="Bacteriocin amylovorin-L"
FT                   /id="PRO_0000002758"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   65 AA;  6537 MW;  1D91BF8509BC9276 CRC64;
     MKQLNSEQLQ NIIGGNRWTN AYSAALGCAV PGVKYGKKLG GVWGAVIGGV GGAAVCGLAG
     YVRKG