ID   CE05_ECOLX              Reviewed;         490 AA.
AC   Q47500;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Colicin-5;
GN   Name=cfa;
OS   Escherichia coli.
OG   Plasmid.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35324 / ECOR 5;
RX   PubMed=7592492; DOI=10.1128/jb.177.23.6966-6972.1995;
RA   Pilsl H., Braun V.;
RT   "Evidence that the immunity protein inactivates colicin 5 immediately prior
RT   to the formation of the transmembrane channel.";
RL   J. Bacteriol. 177:6966-6972(1995).
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.
CC   -!- FUNCTION: Colicins are polypeptide toxins produced by and active
CC       against E.coli and closely related bacteria.
CC   -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the channel forming colicin family.
CC       {ECO:0000305}.
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DR   EMBL; X87835; CAA61102.1; -; Genomic_DNA.
DR   RefSeq; WP_000362089.1; NZ_VRXO01000078.1.
DR   AlphaFoldDB; Q47500; -.
DR   SMR; Q47500; -.
DR   IntAct; Q47500; 2.
DR   PATRIC; fig|562.7401.peg.3224; -.
DR   GO; GO:0033644; C:host cell 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: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   3: Inferred from homology;
KW   Antibiotic; Antimicrobial; Bacteriocin; Host membrane; Membrane; Plasmid;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..490
FT                   /note="Colicin-5"
FT                   /id="PRO_0000218672"
FT   TRANSMEM        447..467
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          146..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   490 AA;  53138 MW;  187614D103B953E2 CRC64;
     MDKVTDNSPD VESTESTEGS FPTVGVDTGD TITATLATGT ENVGGGGGAF GGASESSAAI
     HATAKWSTAQ LKKHQAEQAA RAAAAEAALA KAKSQRDALT QRLKDIVNDA LRANAARSPS
     VTDLAHANNM AMQAEAERLR LAKAEQKARE EAEAAEKALR EAERQRDEIA RQQAETAHLL
     AMAEAAEAEK NRQDSLDEEH RAVEVAEKKL AEAKAELAKA ESDVQSKQAI VSRVAGELEN
     AQKSVDVKVT GFPGWRDVQK KLERQLQDKK NEYSSVTNAL NSAVSIRDAK KTDVQNAEIK
     LKEAKDALEK SQVKDSVDTM VGFYQYITEQ YGEKYSRIAQ DLAEKAKGSK FSSVDEALAA
     FEKYKNVLDK KISKVDRDAI FNALESVNYD ELSKNLTKIS KSLKITSRVS FLYDVGSDFK
     NAIETGNWRP LFVTLEKSAV DVGVAKIVAL MFSFIVGVPL GFWGIAIVTG IVSSYIGDDE
     LNKLNELLGI