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Gene Review

kpsT  -  KpsT protein

Escherichia coli CFT073

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Disease relevance of kpsT


High impact information on kpsT

  • The derivatization of KpsT by this reagent is inhibited by cold ATP or ATP gamma S. Furthermore, the protein seems to require a membrane environment for efficient photolabeling, but does not require any other kps gene products [1].
  • Results obtained from saturation mutagenesis of the ATP-binding consensus sequence of KpsT and the phenotypes of strains with defined mutations in the chromosomal gene, are consistent with the view that ATP-binding by KpsT is required for transport of polymer across the inner membrane [1].
  • RfbD and RfbE were similar to capsular polysaccharide export proteins, e.g. KpsM and KpsT of Escherichia coli [3].
  • We propose that the KpsT protein acts as an energizer, coupling ATP hydrolysis to the transport process mediated by the KpsM protein [2].
  • Evidence that KpsT, the ATP-binding component of an ATP-binding cassette transporter, is exposed to the periplasm and associates with polymer during translocation of the polysialic acid capsule of Escherichia coli K1 [4].

Anatomical context of kpsT

  • We propose that KpsM and KpsT constitute a system for transport of polysialic acid across the cytoplasmic membrane [5].

Associations of kpsT with chemical compounds

  • The KpsC, KpsS, and KpsT proteins involved in polysaccharide transport were associated with the inner membrane and this membrane association occurred in the absence of any other capsule-related proteins [6].
  • All mutations mapped to the same glutamic acid residue at position 150, adjacent to Walker motif B of KpsT [7].

Other interactions of kpsT

  • The KfiA and KfiC, together with the KpsC, KpsS and KpsT proteins, were purified and polyclonal antisera to each protein generated [6].

Analytical, diagnostic and therapeutic context of kpsT

  • Results of site-directed mutagenesis of the putative ATP-binding domain of KpsT are consistent with the view that KpsT is a nucleotide-binding protein [5].


  1. Characterization of KpsT, the ATP-binding component of the ABC-transporter involved with the export of capsular polysialic acid in Escherichia coli K1. Pavelka, M.S., Hayes, S.F., Silver, R.P. J. Biol. Chem. (1994) [Pubmed]
  2. Molecular analysis of the Escherichia coli K5 kps locus: identification and characterization of an inner-membrane capsular polysaccharide transport system. Smith, A.N., Boulnois, G.J., Roberts, I.S. Mol. Microbiol. (1990) [Pubmed]
  3. Genetic organization and sequence of the rfb gene cluster of Yersinia enterocolitica serotype O:3: similarities to the dTDP-L-rhamnose biosynthesis pathway of Salmonella and to the bacterial polysaccharide transport systems. Zhang, L., al-Hendy, A., Toivanen, P., Skurnik, M. Mol. Microbiol. (1993) [Pubmed]
  4. Evidence that KpsT, the ATP-binding component of an ATP-binding cassette transporter, is exposed to the periplasm and associates with polymer during translocation of the polysialic acid capsule of Escherichia coli K1. Bliss, J.M., Silver, R.P. J. Bacteriol. (1997) [Pubmed]
  5. Identification of two genes, kpsM and kpsT, in region 3 of the polysialic acid gene cluster of Escherichia coli K1. Pavelka, M.S., Wright, L.F., Silver, R.P. J. Bacteriol. (1991) [Pubmed]
  6. The localization of KpsC, S and T, and KfiA, C and D proteins involved in the biosynthesis of the Escherichia coli K5 capsular polysaccharide: evidence for a membrane-bound complex. Rigg, G.P., Barrett, B., Roberts, I.S. Microbiology (Reading, Engl.) (1998) [Pubmed]
  7. Polysialic acid export in Escherichia coli K1: the role of KpsT, the ATP-binding component of an ABC transporter, in chain translocation. Bliss, J.M., Garon, C.F., Silver, R.P. Glycobiology (1996) [Pubmed]
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