ID   CEAK_ECOLX              Reviewed;         548 AA.
AC   Q47502; P75615;
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-K;
GN   Name=cka;
OS   Escherichia coli.
OG   Plasmid ColK-K235.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K49;
RX   PubMed=7592493; DOI=10.1128/jb.177.23.6973-6977.1995;
RA   Pilsl H., Braun V.;
RT   "Strong function-related homology between the pore-forming colicins K and
RT   5.";
RL   J. Bacteriol. 177:6973-6977(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Izard J., Chartier M., Baty D.;
RL   Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
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; X87834; CAA61099.1; -; Genomic_DNA.
DR   EMBL; U27452; AAB41288.1; -; Genomic_DNA.
DR   RefSeq; WP_011264160.1; NZ_SNQD01000078.1.
DR   RefSeq; YP_214172.1; NC_006881.1.
DR   AlphaFoldDB; Q47502; -.
DR   SMR; Q47502; -.
DR   TCDB; 1.C.1.2.1; 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..548
FT                   /note="Colicin-K"
FT                   /id="PRO_0000218671"
FT   TRANSMEM        505..525
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        155
FT                   /note="S -> G (in Ref. 2; AAB41288)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   548 AA;  59662 MW;  2E67689D088CCF86 CRC64;
     MAKELSGYGP TAGESMGGTG ANLNQQGGNN NSNSGVHWGG GSGHGNNGGQ GNSNSSGSTS
     TVMKTGESYL TPWGDVVINN DGLPVMNGIV MTEENSTLVD NPFGGVSRVL NSLISDMPSL
     FAESSGNNNN NTASVNTAPT NAQVSDMDKS SKVVSNVINE KQKQKNKIAT QISEKQKKIE
     EMKKVFKHHS YHGITDLERD VDELQKKSNQ LDADISKLNS YKNTLQSKIG DVNKQKEAEE
     KARENAEVAE HETLNEEKQA VAEAEKRLAE AKAELAKAES DVQSKQATVS RVAGELENAQ
     KSVDVKVTGF PGWRDVQKKL QRQLEAKQAE YSAVENELKN AVSFRDGKAA EVKEAEQKLK
     EAQDALEKSQ IKDAVDTMVG FYQYITEQYG EKYAKIAQDL AEKSKGKKIQ GVDEALAAFE
     KYKNVLDKKF SKVDRDAIFN ALESVNYDEL SKNLTKISKS LKITSRVSFL YDVGSDFKNA
     IETGNWRPLF VTLEKSAVDV GVAKIVALMF SFIVGVPLGF WGIAIVTGIV SSYIGDDELS
     KLNELLGI