ID   CEA1_SHISO              Reviewed;         521 AA.
AC   P21178;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Colicin-E1*;
GN   Name=cea;
OS   Shigella sonnei.
OG   Plasmid pKY-1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=624;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Higashi M., Hata M., Hase T., Yamaguchi K., Masamune Y.;
RT   "The nucleotide sequence of cea and the region of origin of plasmid pKY-
RT   1.";
RL   J. Gen. Appl. Microbiol. 32:433-442(1986).
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: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the channel forming colicin family.
CC       {ECO:0000305}.
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DR   EMBL; M37218; AAA98156.1; -; Genomic_DNA.
DR   PIR; S06218; S06218.
DR   AlphaFoldDB; P21178; -.
DR   SMR; P21178; -.
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   3: Inferred from homology;
KW   Antibiotic; Antimicrobial; Bacteriocin; Cell membrane; Membrane; Plasmid;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..521
FT                   /note="Colicin-E1*"
FT                   /id="PRO_0000218669"
FT   TRANSMEM        470..486
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        493..509
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          26..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          127..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..163
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   521 AA;  57670 MW;  8051419A7FA4D36D CRC64;
     METAVAYYKD GVPYDDKGEV IITLLNGNPD GSGSGGGGGT GGSKSESSAA IHATAKWSTA
     QLKKTQAEQA ARAKAAAEAQ AKAKANRDAL TQHLKDIVNE ALRHNSTHPE VIDLLMPIMQ
     RCRQKQSGCA LQKQKKKPVK KRKRAEKSFQ EAEQRRKEIE KEQAETERQL KLAEDEEKRL
     AALSEEARAV EVAQKNLAAA QSELAKVDEE INTLNTRLSS SIHARDAETN TLSGKRNELD
     QASAKYKELD ERVKLLSPRA NDPLQSRPFF EATRLRARRG DEMEEKQKQV TATETRLNQI
     SSEINGIQEA ISQANNKRST AVSRIHDAED NLKTAQTNLL NSQIKDAVDA TVSFYQTLSE
     KYGEKYSKMA QELADKSKGK KISNVNEALA AFEKYKDVLN KKFSKADRDA IFNALEAVKY
     EDWAKHLDQF AKYLKITGHV SFGYDVVSDI LKIKDTGDWK PLFLTLEKKA VDAGVSYVVV
     LLFSVLAGTT LGIWGIAIVT GILCAFIDKN KLNTINEVLG I