View bacteriocin : Colicin-Ia

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Accession BAC172
Name Colicin-Ia
Related Entries Colicin-V (Microcin-V)Colicin-E1Colicin-10Colicin-NColicin-M

Colicin-Ib
Gene cia
Class Unclassified
Producer Organism Escherichia coli [Gram-negative]
Taxonomy BacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Target organisms Unavailable data
Swiss-Prot Entry P06716
PDB Entry 1CII resolved by X-ray 2HDI resolved by X-ray
Other databases EMBL M13819EMBL U15622PIR C25035SMR P06716TCDB 1.C.1.1.1

GO GO:0016021GO GO:0005886GO GO:0005102GO GO:0019835GO GO:0050829

InterPro IPR000293InterPro IPR014740InterPro IPR014739Gene3D G3DSA:1.10.490.30Gene3D G3DSA:3.30.305.10

Gene3D G3DSA:1.20.250.10Pfam PF01024PRINTS PR00280ProDom PD002657PROSITE PS00276
Description This colicin is a channel-forming colicin. This class of transmembrane toxins depolarize the cytoplasmic membrane, leading to dissipation of cellular energy.

Colicins are polypeptide toxins produced by and active against Escherichia coli and closely related bacteria.
[Ref. 1] | View abstract | Export citation
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 23-624.PLASMID=ColIa-CA53
MEDLINE=97162210;PubMed=9009197;DOI=10.1038/385461a0
Wiener M., Freymann D., Ghosh P., Stroud R.M.
"Crystal structure of colicin Ia.", Nature 385:461-464(1997)

[Ref. 2] | View abstract | Export citation
NUCLEOTIDE SEQUENCE [GENOMIC DNA].PLASMID=ColIa-EC28
MEDLINE=95062249;PubMed=7972047;DOI=10.1073/pnas.91.23.11276
Riley M.A., Tan Y., Wang J.
"Nucleotide polymorphism in colicin E1 and Ia plasmids from naturalisolates of Escherichia coli", Proc. Natl. Acad. Sci. U.S.A. 91:11276-11280(1994)

[Ref. 3]
SEQUENCE REVISION TO 304

Konisky J.
"", Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.

[Ref. 4] | View abstract | Export citation
NUCLEOTIDE SEQUENCE [GENOMIC DNA].PLASMID=ColIa-CA53
MEDLINE=87008385;PubMed=3531169;
Mankovich J.A., Hsu C.-H., Konisky J.
"DNA and amino acid sequence analysis of structural and immunity genesof colicins Ia and Ib", J. Bacteriol. 168:228-236(1986)

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Sequence
 ........10 ........20 ........30 ........40 ........50 ........60 ........70 ........80 
          |          |          |          |          |          |          |          | 
 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
Structure
Composition
Formula C3019 H4909 N901 O963 S6
Absent amino acids C
Common amino acids A
Mass (Da) 69457.7
Net charge +15
Isoelectric point 9.72
Basic residues 103
Acidic residues 88
Hydrophobic residues 219
Polar residues 174
Aliphatic residues 120
Tiny residues 155
Boman Index -1515.11
Hydropathy Index -0.64
Aliphatic Index 82.91
Instability Index 34 (stable)
Half Life Mammalian : 30 hour
Yeast : >20 hour
E. coli : >10 hour
Extinction Coefficient 59360 M-1 cm-1
Absorbance 280nm 94.98
Red solid plot : values according to the hydrophobicity scale of Kyte and Doolittle (reference paper).


Yellow dashed plot : Experimentally determined hydrophobicity scale for proteins at membrane interfaces(reference paper).


Green dotted-dashed plot : prediction of transmembrane helices (reference paper). In this scale (unlike the others), more negative values reflect greater hydrophobicity.

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