ID   CEA_CITFR               Reviewed;         592 AA.
AC   P04480; Q51599;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Colicin-A;
GN   Name=caa;
OS   Citrobacter freundii.
OG   Plasmid ColA-CA31.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX   NCBI_TaxID=546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6313941; DOI=10.1016/s0022-2836(83)80148-x;
RA   Morlon J., Lloubes R., Varenne S., Chartier M., Lazdunski C.;
RT   "Complete nucleotide sequence of the structural gene for colicin A, a gene
RT   translated at non-uniform rate.";
RL   J. Mol. Biol. 170:271-285(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2832701; DOI=10.1007/bf00330599;
RA   Morlon J., Chartier M., Bidaud M., Lazdunski C.;
RT   "The complete nucleotide sequence of the colicinogenic plasmid ColA. High
RT   extent of homology with ColE1.";
RL   Mol. Gen. Genet. 211:231-243(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-70.
RX   PubMed=6641715; DOI=10.1002/j.1460-2075.1983.tb01501.x;
RA   Morlon J., Lloubes R., Chartier M., Bonicel J., Lazdunski C.;
RT   "Nucleotide sequence of promoter, operator and amino-terminal region of
RT   caa, the structural gene of colicin A.";
RL   EMBO J. 2:787-789(1983).
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   -!- INTERACTION:
CC       P04480; P19934: tolA; Xeno; NbExp=6; IntAct=EBI-6559916, EBI-1120026;
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; X01008; CAA25503.1; -; Genomic_DNA.
DR   EMBL; M37402; AAA72879.1; -; Genomic_DNA.
DR   EMBL; M26369; AAA98057.1; -; Genomic_DNA.
DR   PIR; I40784; IKEBCA.
DR   RefSeq; WP_008323639.1; NZ_MDCX01000274.1.
DR   PDB; 3IAX; X-ray; 2.60 A; B=1-107.
DR   PDB; 3QDR; X-ray; 2.65 A; B=53-107.
DR   PDBsum; 3IAX; -.
DR   PDBsum; 3QDR; -.
DR   AlphaFoldDB; P04480; -.
DR   BMRB; P04480; -.
DR   SMR; P04480; -.
DR   IntAct; P04480; 2.
DR   MINT; P04480; -.
DR   TCDB; 1.C.1.3.1; the channel-forming colicin (colicin) family.
DR   PRIDE; P04480; -.
DR   EvolutionaryTrace; P04480; -.
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   DisProt; DP01852; -.
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..592
FT                   /note="Colicin-A"
FT                   /id="PRO_0000218666"
FT   TRANSMEM        528..548
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        555..575
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          373..395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   STRAND          14..16
FT                   /evidence="ECO:0007829|PDB:3IAX"
FT   STRAND          58..60
FT                   /evidence="ECO:0007829|PDB:3QDR"
FT   STRAND          63..66
FT                   /evidence="ECO:0007829|PDB:3QDR"
FT   TURN            82..84
FT                   /evidence="ECO:0007829|PDB:3QDR"
FT   STRAND          86..90
FT                   /evidence="ECO:0007829|PDB:3QDR"
FT   STRAND          93..97
FT                   /evidence="ECO:0007829|PDB:3QDR"
SQ   SEQUENCE   592 AA;  62993 MW;  B80FA1F52A8CFC5D CRC64;
     MPGFNYGGKG DGTGWSSERG SGPEPGGGSH GNSGGHDRGD SSNVGNESVT VMKPGDSYNT
     PWGKVIINAA GQPTMNGTVM TADNSSMVPY GRGFTRVLNS LVNNPVSPAG QNGGKSPVQT
     AVENYLMVQS GNLPPGYWLS NGKVMTEVRE ERTSGGGGKN GNERTWTVKV PREVPQLTAS
     YNEGMRIRQE AADRARAEAN ARALAEEEAR AIASGKSKAE FDAGKRVEAA QAAINTAQLN
     VNNLSGAVSA ANQVITQKQA EMTPLKNELA AANQRVQETL KFINDPIRSR IHFNMRSGLI
     RAQHNVDTKQ NEINAAVANR DALNSQLSQA NNILQNARNE KSAADAALSA ATAQRLQAEA
     ALRAAAEAAE KARQRQAEEA ERQRQAMEVA EKAKDERELL EKTSELIAGM GDKIGEHLGD
     KYKAIAKDIA DNIKNFQGKT IRSFDDAMAS LNKITANPAM KINKADRDAL VNAWKHVDAQ
     DMANKLGNLS KAFKVADVVM KVEKVREKSI EGYETGNWGP LMLEVESWVL SGIASSVALG
     IFSATLGAYA LSLGVPAIAV GIAGILLAAV VGALIDDKFA DALNNEIIRP AH