View bacteriocin : Colicin-V (Microcin-V) Bookmark and Share

Accession BAC120
Name Colicin-V (Microcin-V)
Related Entries Colicin-E1Colicin-10Colicin-NColicin-MColicin-Ia

Colicin-Ib
Gene cvaC
Class Unclassified
Producer Organism Escherichia coli [Gram-negative]
Taxonomy BacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Target organisms active against Escherichia coli (also closely related bacteria) - Enterobacteriaceae
Swiss-Prot Entry P22522
PDB Entry Unknown
Other databases EMBL X57525EMBL AF062844EMBL AF062845EMBL AF062846EMBL AF062847

EMBL AF062848EMBL AF062849EMBL AF062850EMBL AF062851EMBL AF062852

EMBL AF062853EMBL AF062854EMBL AF062855EMBL AF062856EMBL AF062857

EMBL AF062858EMBL AJ223631PIR S12274
Description Mode of action:
Colicin V kills sensitive cells by disrupting the membrane potential.
Colicins are polypeptide toxins. export system.
[Ref. 1] | View abstract | Export citation
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
MEDLINE=91065315;PubMed=2249654;
Gilson L., Mahanty H.K., Kolter R.
"Genetic analysis of an MDR-like export system: the secretion of colicin V.", EMBO J. 9:3875-3884(1990).

[Ref. 2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], STRAIN=Various strains

Pinou T., Riley M.A.
"", Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.

[Ref. 3] | View abstract | Export citation
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
MEDLINE=98416173;PubMed=9743528;DOI=10.1084/jem.188.6.1091
Otto B.R., van Dooren S.J.M., Nuijens J.H., Luirink J., Oudega B.
"Characterization of a hemoglobin protease secreted by the pathogenic Escherichia coli strain EB1.", J. Exp. Med. 188:1091-1103(1998).

[Ref. 4] | View abstract | Export citation
PROTEIN SEQUENCE OF 16-62, AND DISULFIDE BOND.
MEDLINE=95039899;PubMed=7952189;
Havarstein L.S., Holo H., Nes I.F.
"The leader peptide of colicin V shares consensus sequences with leader peptides that are common among peptide bacteriocins produced by Gram-positive bacteria.", Microbiology 140:2383-2389(1994).

[Ref. 5] | View abstract | Export citation
PROTEIN SEQUENCE OF 16-28, AND SUBCELLULAR LOCATION.
PubMed=8204625;
Fath M.J., Zhang L.H., Rush J., Kolter R.
"Purification and characterization of colicin V from Escherichia coli culture supernatants.", Biochemistry 33:6911-6917(1994).

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Sequence
........10........20........30........40........50........60........70........80
| | | | | | | |
ASGRDIAMAIGTLSGQFVAGGIGAAAGGVAGGAIYDYASTHKPNPAMSPSGLGGTIKQKPEGIPSEAWNYAAGRLCNWSP
NNLSDVCL
Wheel representation
Composition
AA N° %

AA N° %

AA N° %
Ala 14 15.91%

Ile 6 6.82%

Arg 2 2.27%
Cys 2 2.27%

Lys 3 3.41%

Ser 8 9.09%
Asp 3 3.41%

Leu 5 5.68%

Thr 3 3.41%
Glu 2 2.27%

Met 2 2.27%

Val 3 3.41%
Phe 1 1.14%

Asn 5 5.68%

Trp 2 2.27%
Gly 15 17.05%

Pro 6 6.82%

Tyr 3 3.41%
His 1 1.14%

Gln 2 2.27%
Total 88
Formula C381 H594 N108 O120 S4
Absent amino acids
Common amino acids GA
Mass (Da) 8755.32
Net charge +1
Isoelectric point 7.25
Basic residues 6
Acidic residues 5
Hydrophobic residues 31
Polar residues 36
Aliphatic residues 14
Tiny residues 37
Boman Index -49.96
Hydropathy Index 0
Aliphatic Index 74.55
Instability Index 48.5 (unstable)
Half Life Mammalian : 4.4 hour
Yeast : >20 hour
E. coli : >10 hour
Extinction Coefficient 15595 M-1 cm-1
Absorbance 280nm 179.25
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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