ID   CEA_ECOLX               Reviewed;         204 AA.
AC   Q47108;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Colicin-A;
DE   Flags: Fragment;
GN   Name=caa;
OS   Escherichia coli.
OG   Plasmid pColA9.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=2434951; DOI=10.1073/pnas.84.5.1152;
RA   Baty D., Knibiehler M., Verheij H., Pattus F., Shire D., Bernadac A.,
RA   Lazdunski C.;
RT   "Site-directed mutagenesis of the COOH-terminal region of colicin A: effect
RT   on secretion and voltage-dependent channel activity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:1152-1156(1987).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX   PubMed=1373773; DOI=10.1016/0022-2836(92)90550-4;
RA   Parker M.W., Postma J.P.M., Pattus F., Tucker A.D., Tsernoglou D.;
RT   "Refined structure of the pore-forming domain of colicin A at 2.4-A
RT   resolution.";
RL   J. Mol. Biol. 224:639-657(1992).
CC   -!- FUNCTION: This colicin is a channel-forming colicin. This class of
CC       transmembrane toxins depolarize the cytoplasmic membrane, leading to
CC       dissipation of cellular energy. {ECO:0000269|PubMed:2434951}.
CC   -!- FUNCTION: Colicins are polypeptide toxins produced by and active
CC       against E.coli and closely related bacteria.
CC       {ECO:0000269|PubMed:2434951}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the channel forming colicin family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M15691; AAA23592.1; -; Genomic_DNA.
DR   PIR; I53544; I41169.
DR   PDB; 1COL; X-ray; 2.40 A; A/B=1-204.
DR   PDBsum; 1COL; -.
DR   AlphaFoldDB; Q47108; -.
DR   BMRB; Q47108; -.
DR   SMR; Q47108; -.
DR   EvolutionaryTrace; Q47108; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:InterPro.
DR   Gene3D; 1.10.490.30; -; 1.
DR   InterPro; IPR000293; Channel_colicin_C.
DR   InterPro; IPR038283; Channel_colicin_C_sf.
DR   Pfam; PF01024; Colicin; 1.
DR   PRINTS; PR00280; CHANLCOLICIN.
DR   PROSITE; PS00276; CHANNEL_COLICIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic; Antimicrobial; Bacteriocin; Cell membrane;
KW   Membrane; Plasmid; Transmembrane; Transmembrane helix.
FT   CHAIN           <1..204
FT                   /note="Colicin-A"
FT                   /id="PRO_0000218667"
FT   TRANSMEM        139..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        165..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
FT   HELIX           8..30
FT                   /evidence="ECO:0007829|PDB:1COL"
FT   HELIX           32..46
FT                   /evidence="ECO:0007829|PDB:1COL"
FT   HELIX           56..67
FT                   /evidence="ECO:0007829|PDB:1COL"
FT   HELIX           70..72
FT                   /evidence="ECO:0007829|PDB:1COL"
FT   HELIX           76..87
FT                   /evidence="ECO:0007829|PDB:1COL"
FT   HELIX           91..101
FT                   /evidence="ECO:0007829|PDB:1COL"
FT   HELIX           103..105
FT                   /evidence="ECO:0007829|PDB:1COL"
FT   HELIX           110..127
FT                   /evidence="ECO:0007829|PDB:1COL"
FT   HELIX           131..142
FT                   /evidence="ECO:0007829|PDB:1COL"
FT   HELIX           147..164
FT                   /evidence="ECO:0007829|PDB:1COL"
FT   HELIX           169..187
FT                   /evidence="ECO:0007829|PDB:1COL"
FT   HELIX           190..198
FT                   /evidence="ECO:0007829|PDB:1COL"
SQ   SEQUENCE   204 AA;  21790 MW;  F7702455E2E4E9B9 CRC64;
     VAEKAKDERE LLEKTSELIA GMGDKIGEHL GDKYKAIAKD IADNIKNFQG KTIRSFDDAM
     ASLNKITANP AMKINKADRD ALVNAWKHVD AQDMANKLGN LSKAFKVADV VMKVEKVREK
     SIEGYETGNW GPLMLEVESW VLSGIASSVA LGIFSATLGA YALSLGVPAI AVGIAGILLA
     AVVGALIDDK FADALNNEII RPAH