ID   CE10_ECOLX              Reviewed;         490 AA.
AC   Q47125;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Colicin-10;
GN   Name=cta;
OS   Escherichia coli.
OG   Plasmid pCol10.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PTE10;
RX   PubMed=7651137; DOI=10.1111/j.1365-2958.1995.tb02391.x;
RA   Pilsl H., Braun V.;
RT   "Novel colicin 10: assignment of four domains to TonB- and TolC-dependent
RT   uptake via the Tsx receptor and to pore formation.";
RL   Mol. Microbiol. 16:57-67(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; X82682; CAA57998.1; -; Genomic_DNA.
DR   PIR; I41024; I41024.
DR   AlphaFoldDB; Q47125; -.
DR   SMR; Q47125; -.
DR   TCDB; 1.C.1.2.3; the channel-forming colicin (colicin) family.
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-10"
FT                   /id="PRO_0000218673"
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;  53343 MW;  700E864DA3F97F5B 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 KTEVQNAEIK
     LKEAKDALEK SQVKDSVDTM VGFYQYITEQ YGEKYSRIAQ DLAEKAKGSK FNSVDEALAA
     FEKYKNVLDK KFSKVDRDDI FNALESITYD EWAKHLEKIS RALKVTGYLS FGYDVWDGTL
     KGLKTGDWKP LFVTLEKSAV DFGVAKIVAL MFSFIVGAPL GFWGIAIITG IVSSYIGDDE
     LNKLNELLGI