View bacteriocin : Colicin-Ib

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Accession BAC173
Name Colicin-Ib
Related Entries Colicin-V (Microcin-V)Colicin-E1Colicin-10Colicin-NColicin-M

Colicin-Ia
Gene cib
Class Unclassified
Producer Organism Escherichia coli [Gram-negative]
Taxonomy BacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Target organisms Unavailable data
Swiss-Prot Entry P04479
PDB Entry Unknown
Other databases EMBL K02071EMBL X01009EMBL M13820PIR A93533HSSP P06716

SMR P04479TCDB 1.C.1.1.2GO GO:0016021GO GO:0005102GO GO:0019835

GO GO:0050829InterPro IPR000293InterPro IPR014740InterPro IPR014739Gene3D G3DSA:1.10.490.30

Gene3D G3DSA:3.30.305.10Gene3D G3DSA:1.20.250.10Pfam PF01024PRINTS PR00280ProDom PD002657

PROSITE 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]
ERRATUM.
Varley J.M., Boulnois G.J.
"", Nucleic Acids Res. 12:8748-8748(1984)

[Ref. 2] | View abstract | Export citation
[3]NUCLEOTIDE SEQUENCE [GENOMIC DNA]
MEDLINE=85014128;PubMed=6091036;DOI=10.1093/nar/12.17.6727
Varley J.M., Boulnois G.J.
"Analysis of a cloned colicin Ib gene: complete nucleotide sequence and implications for regulation of expression.", Nucleic Acids Res. 12:6727-6739(1984)

[Ref. 3] | View abstract | Export citation
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40
MEDLINE=84264487;PubMed=6204975;
Mankovich J.A., Lai P.H., Gokul N., Konisky J.
"Organization of the colicin Ib gene. Promoter structure and immunitydomain.", J. Biol. Chem. 259:8764-8768(1984)

[Ref. 4] | View abstract | Export citation
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 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
Composition
Formula C3049 H4935 N903 O962 S9
Absent amino acids C
Common amino acids A
Mass (Da) 69952.45
Net charge +14
Isoelectric point 9.6
Basic residues 103
Acidic residues 89
Hydrophobic residues 223
Polar residues 161
Aliphatic residues 122
Tiny residues 146
Boman Index -1512.06
Hydropathy Index -0.61
Aliphatic Index 82.88
Instability Index 37.17 (stable)
Half Life Mammalian : 30 hour
Yeast : >20 hour
E. coli : >10 hour
Extinction Coefficient 52370 M-1 cm-1
Absorbance 280nm 83.79
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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