CEIA_ECOLX
ID CEIA_ECOLX Reviewed; 626 AA.
AC P06716;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 24-OCT-2003, sequence version 2.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Colicin-Ia;
GN Name=cia;
OS Escherichia coli.
OG Plasmid ColIa-CA53, and Plasmid ColIa-EC28.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=ColIa-CA53;
RX PubMed=3531169; DOI=10.1128/jb.168.1.228-236.1986;
RA Mankovich J.A., Hsu C.-H., Konisky J.;
RT "DNA and amino acid sequence analysis of structural and immunity genes of
RT colicins Ia and Ib.";
RL J. Bacteriol. 168:228-236(1986).
RN [2]
RP SEQUENCE REVISION TO 304.
RA Konisky J.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=ColIa-EC28;
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 [4]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 23-624.
RC PLASMID=ColIa-CA53;
RX PubMed=9009197; DOI=10.1038/385461a0;
RA Wiener M., Freymann D., Ghosh P., Stroud R.M.;
RT "Crystal structure of colicin Ia.";
RL Nature 385:461-464(1997).
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; M13819; AAA23182.2; -; Genomic_DNA.
DR EMBL; U15622; AAA59396.1; -; Genomic_DNA.
DR PIR; C25035; C25035.
DR RefSeq; WP_001582575.1; NZ_WSVS01000050.1.
DR PDB; 1CII; X-ray; 3.00 A; A=23-624.
DR PDB; 2HDI; X-ray; 2.50 A; B=282-385.
DR PDBsum; 1CII; -.
DR PDBsum; 2HDI; -.
DR AlphaFoldDB; P06716; -.
DR SMR; P06716; -.
DR IntAct; P06716; 1.
DR MINT; P06716; -.
DR DrugBank; DB04147; Dodecyldimethylamine N-oxide.
DR TCDB; 1.C.1.1.1; the channel-forming colicin (colicin) family.
DR EvolutionaryTrace; P06716; -.
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 InterPro; IPR014740; Channel_colicin_cen.
DR InterPro; IPR014739; Channel_colicin_N_sf.
DR Pfam; PF01024; Colicin; 1.
DR Pfam; PF11504; Colicin_Ia; 1.
DR PRINTS; PR00280; CHANLCOLICIN.
DR SUPFAM; SSF58096; SSF58096; 1.
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..626
FT /note="Colicin-Ia"
FT /id="PRO_0000218675"
FT TRANSMEM 580..594
FT /note="Helical"
FT TRANSMEM 597..612
FT /note="Helical"
FT REGION 23..225
FT /note="Translocation (T)"
FT REGION 276..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..385
FT /note="Receptor-binding (R)"
FT REGION 450..626
FT /note="Channel (C)"
FT CONFLICT 304
FT /note="H -> D (in Ref. 3; AAA59396)"
FT /evidence="ECO:0000305"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:1CII"
FT HELIX 67..121
FT /evidence="ECO:0007829|PDB:1CII"
FT HELIX 126..168
FT /evidence="ECO:0007829|PDB:1CII"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:1CII"
FT HELIX 176..282
FT /evidence="ECO:0007829|PDB:1CII"
FT HELIX 285..291
FT /evidence="ECO:0007829|PDB:2HDI"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:2HDI"
FT STRAND 298..308
FT /evidence="ECO:0007829|PDB:2HDI"
FT TURN 312..314
FT /evidence="ECO:0007829|PDB:2HDI"
FT STRAND 316..326
FT /evidence="ECO:0007829|PDB:2HDI"
FT HELIX 329..337
FT /evidence="ECO:0007829|PDB:2HDI"
FT HELIX 340..346
FT /evidence="ECO:0007829|PDB:2HDI"
FT HELIX 359..383
FT /evidence="ECO:0007829|PDB:2HDI"
FT HELIX 470..480
FT /evidence="ECO:0007829|PDB:1CII"
FT TURN 481..484
FT /evidence="ECO:0007829|PDB:1CII"
FT HELIX 490..499
FT /evidence="ECO:0007829|PDB:1CII"
FT HELIX 501..504
FT /evidence="ECO:0007829|PDB:1CII"
FT HELIX 511..521
FT /evidence="ECO:0007829|PDB:1CII"
FT HELIX 525..539
FT /evidence="ECO:0007829|PDB:1CII"
FT HELIX 548..560
FT /evidence="ECO:0007829|PDB:1CII"
FT HELIX 565..571
FT /evidence="ECO:0007829|PDB:1CII"
FT TURN 572..574
FT /evidence="ECO:0007829|PDB:1CII"
FT HELIX 580..591
FT /evidence="ECO:0007829|PDB:1CII"
FT HELIX 597..612
FT /evidence="ECO:0007829|PDB:1CII"
FT HELIX 614..621
FT /evidence="ECO:0007829|PDB:1CII"
SQ SEQUENCE 626 AA; 69429 MW; 3DC0DF322F405D39 CRC64;
MSDPVRITNP GAESLGYDSD GHEIMAVDIY VNPPRVDVFH GTPPAWSSFG NKTIWGGNEW
VDDSPTRSDI EKRDKEITAY KNTLSAQQKE NENKRTEAGK RLSAAIAARE KDENTLKTLR
AGNADAADIT RQEFRLLQAE LREYGFRTEI AGYDALRLHT ESRMLFADAD SLRISPREAR
SLIEQAEKRQ KDAQNADKKA ADMLAEYERR KGILDTRLSE LEKNGGAALA VLDAQQARLL
GQQTRNDRAI SEARNKLSSV TESLNTARNA LTRAEQQLTQ QKNTPDGKTI VSPEKFPGRS
STNHSIVVSG DPRFAGTIKI TTSAVIDNRA NLNYLLSHSG LDYKRNILND RNPVVTEDVE
GDKKIYNAEV AEWDKLRQRL LDARNKITSA ESAVNSARNN LSARTNEQKH ANDALNALLK
EKENIRNQLS GINQKIAEEK RKQDELKATK DAINFTTEFL KSVSEKYGAK AEQLAREMAG
QAKGKKIRNV EEALKTYEKY RADINKKINA KDRAAIAAAL ESVKLSDISS NLNRFSRGLG
YAGKFTSLAD WITEFGKAVR TENWRPLFVK TETIIAGNAA TALVALVFSI LTGSALGIIG
YGLLMAVTGA LIDESLVEKA NKFWGI
