CEIB_ECOLX
ID CEIB_ECOLX Reviewed; 626 AA.
AC P04479;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Colicin-Ib;
GN Name=cib;
OS Escherichia coli.
OG Plasmid IncI1 ColIb-P9.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
RX PubMed=6204975; DOI=10.1016/s0021-9258(17)47219-x;
RA Mankovich J.A., Lai P.H., Gokul N., Konisky J.;
RT "Organization of the colicin Ib gene. Promoter structure and immunity
RT domain.";
RL J. Biol. Chem. 259:8764-8768(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6091036; DOI=10.1093/nar/12.17.6727;
RA Varley J.M., Boulnois G.J.;
RT "Analysis of a cloned colicin Ib gene: complete nucleotide sequence and
RT implications for regulation of expression.";
RL Nucleic Acids Res. 12:6727-6739(1984).
RN [4]
RP ERRATUM OF PUBMED:6091036.
RA Varley J.M., Boulnois G.J.;
RL Nucleic Acids Res. 12:8748-8748(1984).
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; K02071; AAA92225.1; -; Genomic_DNA.
DR EMBL; X01009; CAA25505.1; -; Genomic_DNA.
DR EMBL; M13820; AAA23188.1; -; Genomic_DNA.
DR PIR; A93533; IKECB.
DR AlphaFoldDB; P04479; -.
DR SMR; P04479; -.
DR TCDB; 1.C.1.1.2; 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 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 3: Inferred from homology;
KW Antibiotic; Antimicrobial; Bacteriocin; Host membrane; Membrane; Plasmid;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..626
FT /note="Colicin-Ib"
FT /id="PRO_0000218676"
FT TRANSMEM 588..612
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 276..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 626 AA; 69924 MW; 1BE67D6F7C08A528 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 TESLKTARNA LTRAEQQLTQ QKNTPDGKTI VSPEKFPGRS
STNHSIVVSG DPRFAGTIKI TTSAVIDNRA NLNYLLTHSG LDYKRNILND RNPVVTEDVE
GDKKIYNAEV AEWDKLRQRL LDARNKITSA ESAINSARNN VSARTNEQKH ANDALNALLK
EKENIRSQLA DINQKIAEEK RKRDEINMVK DAIKLTSDFY RTIYDEFGKQ ASELAKELAS
VSQGKQIKSV DDALNAFDKF RNNLNKKYNI QDRMAISKAL EAINQVHMAE NFKLFSKAFG
FTGKVIERYD VAVELQKAVK TDNWRPFFVK LESLAAGRAA SAVTAWAFSV MLGTPVGILG
FAIIMAAVSA LVNDKFIEQV NKLIGI