CEA1_ECOLX
ID CEA1_ECOLX Reviewed; 522 AA.
AC P02978;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Colicin-E1;
GN Name=cea;
OS Escherichia coli.
OG Plasmid ColE1, Plasmid ColE1-EC71, and Plasmid pAO3.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=ColE1;
RX PubMed=6953432; DOI=10.1073/pnas.79.9.2827;
RA Yamada M., Ebina Y., Miyata T., Nakazawa T., Nakazawa A.;
RT "Nucleotide sequence of the structural gene for colicin E1 and predicted
RT structure of the protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:2827-2831(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=ColE1-EC71;
RX PubMed=7972047; DOI=10.1073/pnas.91.23.11276;
RA Riley M.A., Tan Y., Wang J.;
RT "Nucleotide polymorphism in colicin E1 and Ia plasmids from natural
RT isolates of Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:11276-11280(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-71.
RC PLASMID=ColE1;
RX PubMed=6271636; DOI=10.1016/0378-1119(81)90121-9;
RA Ebina Y., Kishi F., Miki T., Kagamiyama H., Nakazawa T., Nakazawa A.;
RT "The nucleotide sequence surrounding the promoter region of colicin E1
RT gene.";
RL Gene 15:119-126(1981).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 480-522.
RC PLASMID=pAO3;
RX PubMed=384144; DOI=10.1007/bf00268276;
RA Oka A., Nomura N., Morita M., Sugisaki H., Sugimoto K., Takanami M.;
RT "Nucleotide sequence of small ColE1 derivatives: structure of the regions
RT essential for autonomous replication and colicin E1 immunity.";
RL Mol. Gen. Genet. 172:151-159(1979).
RN [5]
RP STRUCTURE BY NMR OF 345-522.
RX PubMed=2199197; DOI=10.1111/j.1432-1033.1990.tb19105.x;
RA Wormald M.R., Merril A.R., Cramer W.A., Williams R.J.P.;
RT "Solution NMR studies of colicin E1 C-terminal thermolytic peptide.
RT Structural comparison with colicin A and the effects of pH changes.";
RL Eur. J. Biochem. 191:155-161(1990).
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 -!- MISCELLANEOUS: Plasmid PAO3 is a small colicin E1 derivative.
CC -!- SIMILARITY: Belongs to the channel forming colicin family.
CC {ECO:0000305}.
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DR EMBL; J01563; AAA87379.1; -; Genomic_DNA.
DR EMBL; U15633; AAA59418.1; -; Genomic_DNA.
DR PIR; A93913; IKEC1.
DR PDB; 2I88; X-ray; 2.50 A; A=332-522.
DR PDB; 6WXH; EM; 3.09 A; D=1-190.
DR PDBsum; 2I88; -.
DR PDBsum; 6WXH; -.
DR AlphaFoldDB; P02978; -.
DR SMR; P02978; -.
DR TCDB; 1.C.1.2.2; the channel-forming colicin (colicin) family.
DR EvolutionaryTrace; P02978; -.
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:0044325; F:transmembrane transporter binding; IPI:CAFA.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:InterPro.
DR GO; GO:0032413; P:negative regulation of ion transmembrane transporter activity; IDA:CAFA.
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..522
FT /note="Colicin-E1"
FT /id="PRO_0000218668"
FT TRANSMEM 471..487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..510
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 26..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 47..105
FT /evidence="ECO:0007829|PDB:6WXH"
FT HELIX 112..130
FT /evidence="ECO:0007829|PDB:6WXH"
FT HELIX 346..362
FT /evidence="ECO:0007829|PDB:2I88"
FT HELIX 365..378
FT /evidence="ECO:0007829|PDB:2I88"
FT HELIX 386..402
FT /evidence="ECO:0007829|PDB:2I88"
FT HELIX 406..416
FT /evidence="ECO:0007829|PDB:2I88"
FT HELIX 422..425
FT /evidence="ECO:0007829|PDB:2I88"
FT HELIX 428..434
FT /evidence="ECO:0007829|PDB:2I88"
FT HELIX 447..457
FT /evidence="ECO:0007829|PDB:2I88"
FT HELIX 461..471
FT /evidence="ECO:0007829|PDB:2I88"
FT HELIX 472..475
FT /evidence="ECO:0007829|PDB:2I88"
FT HELIX 476..488
FT /evidence="ECO:0007829|PDB:2I88"
FT HELIX 494..507
FT /evidence="ECO:0007829|PDB:2I88"
FT HELIX 513..515
FT /evidence="ECO:0007829|PDB:2I88"
FT HELIX 516..520
FT /evidence="ECO:0007829|PDB:2I88"
SQ SEQUENCE 522 AA; 57280 MW; A77C351BBC1AB7C1 CRC64;
METAVAYYKD GVPYDDKGQV IITLLNGTPD GSGSGGGGGK GGSKSESSAA IHATAKWSTA
QLKKTQAEQA ARAKAAAEAQ AKAKANRDAL TQRLKDIVNE ALRHNASRTP SATELAHANN
AAMQAEDERL RLAKAEEKAR KEAEAAEKAF QEAEQRRKEI EREKAETERQ LKLAEAEEKR
LAALSEEAKA VEIAQKKLSA AQSEVVKMDG EIKTLNSRLS SSIHARDAEM KTLAGKRNEL
AQASAKYKEL DELVKKLSPR ANDPLQNRPF FEATRRRVGA GKIREEKQKQ VTASETRINR
INADITQIQK AISQVSNNRN AGIARVHEAE ENLKKAQNNL LNSQIKDAVD ATVSFYQTLT
EKYGEKYSKM AQELADKSKG KKIGNVNEAL AAFEKYKDVL NKKFSKADRD AIFNALASVK
YDDWAKHLDQ FAKYLKITGH VSFGYDVVSD ILKIKDTGDW KPLFLTLEKK AADAGVSYVV
ALLFSLLAGT TLGIWGIAIV TGILCSYIDK NKLNTINEVL GI
