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Gene Review

malK  -  maltose ABC transportor ATPase

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK4027, JW3995
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Disease relevance of malK

  • The structure and expression of the distal part of the malK-lamB operon in Escherichia coli was studied [1].
  • The malE and malK genes from Salmonella typhimurium, and the malEFG operon and a portion of malK from Enterobacter aerogenes were cloned and sequenced [2].
  • The malK gene, encoding a membrane-associated component of the maltose transport complex of Salmonella typhimurium was cloned into an expression vector downstream of the promoters lambda pR and lambda pL and a strong translation initiation region [3].
  • To demonstrate the use of this phage, we isolated lacZ fusions to the malB locus [4].

High impact information on malK

  • From maltose-negative mutants of the two categories, we isolated suppressor mutations within malK that restore transport [5].
  • We show here that one can successfully replace all of the CRP sites by the binding site of another DNA-bending protein, integration host factor, or by a sequence-directed bend without altering the process of malKp activation [6].
  • The products of the malF, malG, and malK genes form a membrane-associated complex that catalyzes the hydrolysis of ATP to provide energy for the transport event [7].
  • Three adjacent binding sites for cAMP receptor protein are involved in the activation of the divergent malEp-malKp promoters [8].
  • Six malK point mutations were isolated specifically affecting the interaction with MalT, the transcriptional regulator of the maltose system [9].

Chemical compound and disease context of malK

  • The malK gene of Salmonella typhimurium encoding the ATP-hydrolyzing subunit of the ATP-Binding Cassette (ABC) transporter for maltose was subcloned into the pRSET5d expression vector [10].

Biological context of malK


Associations of malK with chemical compounds

  • We found that when all three genes were present or when malF and malK were present together, the corresponding antigens were detected easily on Western immunoblots and were soluble in the non-ionic detergent, Triton X-100 [16].
  • To this end, single cysteine residues were introduced into each subunit at several positions and the respective malF and malG alleles were individually co-expressed with each of the malK alleles [17].
  • The third class of malK mutations resulted in resistance to the enzyme IIIGlc-mediated inhibitory effects of alpha-methylglucoside [18].

Other interactions of malK


Analytical, diagnostic and therapeutic context of malK

  • For a better insight into the role of DT3 in signal integration, we PCR mutagenized the DT3-encoding region and screened for gain of function mutations in a malK+ strain in the absence of repression by MalY or Aes [21].


  1. malM, a new gene of the maltose regulon in Escherichia coli K12. I. malM is the last gene of the malK-lamB operon and encodes a periplasmic protein. Gilson, E., Rousset, J.P., Charbit, A., Perrin, D., Hofnung, M. J. Mol. Biol. (1986) [Pubmed]
  2. Comparison of sequences from the malB regions of Salmonella typhimurium and Enterobacter aerogenes with Escherichia coli K12: a potential new regulatory site in the interoperonic region. Dahl, M.K., Francoz, E., Saurin, W., Boos, W., Manson, M.D., Hofnung, M. Mol. Gen. Genet. (1989) [Pubmed]
  3. Large scale purification, nucleotide binding properties, and ATPase activity of the MalK subunit of Salmonella typhimurium maltose transport complex. Walter, C., Höner zu Bentrup, K., Schneider, E. J. Biol. Chem. (1992) [Pubmed]
  4. Lambda placMu: a transposable derivative of bacteriophage lambda for creating lacZ protein fusions in a single step. Bremer, E., Silhavy, T.J., Weisemann, J.M., Weinstock, G.M. J. Bacteriol. (1984) [Pubmed]
  5. Subunit interactions in ABC transporters: a conserved sequence in hydrophobic membrane proteins of periplasmic permeases defines an important site of interaction with the ATPase subunits. Mourez, M., Hofnung, M., Dassa, E. EMBO J. (1997) [Pubmed]
  6. CRP induces the repositioning of MalT at the Escherichia coli malKp promoter primarily through DNA bending. Richet, E., Søgaard-Andersen, L. EMBO J. (1994) [Pubmed]
  7. Mechanism of maltose transport in Escherichia coli: transmembrane signaling by periplasmic binding proteins. Davidson, A.L., Shuman, H.A., Nikaido, H. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  8. Three adjacent binding sites for cAMP receptor protein are involved in the activation of the divergent malEp-malKp promoters. Vidal-Ingigliardi, D., Raibaud, O. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  9. Structural model of MalK, the ABC subunit of the maltose transporter of Escherichia coli: implications for mal gene regulation, inducer exclusion, and subunit assembly. Böhm, A., Diez, J., Diederichs, K., Welte, W., Boos, W. J. Biol. Chem. (2002) [Pubmed]
  10. Functional purification of a bacterial ATP-binding cassette transporter protein (MalK) from the cytoplasmic fraction of an overproducing strain. Schneider, E., Linde, M., Tebbe, S. Protein Expr. Purif. (1995) [Pubmed]
  11. A DNA sequence containing the control regions of the malEFG and malK-lamB operons in Escherichia coli K12. Bedouelle, H., Hofnung, M. Mol. Gen. Genet. (1982) [Pubmed]
  12. Mutations in the promoter regions of the malEFG and malK-lamB operons of Escherichia coli K12. Bedouelle, H. J. Mol. Biol. (1983) [Pubmed]
  13. Large-scale purification, dissociation and functional reassembly of the maltose ATP-binding cassette transporter (MalFGK(2)) of Salmonella typhimurium. Landmesser, H., Stein, A., Blüschke, B., Brinkmann, M., Hunke, S., Schneider, E. Biochim. Biophys. Acta (2002) [Pubmed]
  14. A putative helical domain in the MalK subunit of the ATP-binding-cassette transport system for maltose of Salmonella typhimurium (MalFGK2) is crucial for interaction with MalF and MalG. A study using the LacK protein of Agrobacterium radiobacter as a tool. Wilken, S., Schmees, G., Schneider, E. Mol. Microbiol. (1996) [Pubmed]
  15. Molecular evolution of the ATPase subunit of three archaeal sugar ABC transporters. Imamura, H., Jeon, B.S., Wakagi, T. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  16. Characterization of the structural requirements for assembly and nucleotide binding of an ATP-binding cassette transporter. The maltose transport system of Escherichia coli. Panagiotidis, C.H., Reyes, M., Sievertsen, A., Boos, W., Shuman, H.A. J. Biol. Chem. (1993) [Pubmed]
  17. ATP modulates subunit-subunit interactions in an ATP-binding cassette transporter (MalFGK2) determined by site-directed chemical cross-linking. Hunke, S., Mourez, M., Jehanno, M., Dassa, E., Schneider, E. J. Biol. Chem. (2000) [Pubmed]
  18. The activities of the Escherichia coli MalK protein in maltose transport, regulation, and inducer exclusion can be separated by mutations. Kühnau, S., Reyes, M., Sievertsen, A., Shuman, H.A., Boos, W. J. Bacteriol. (1991) [Pubmed]
  19. MalI, a novel protein involved in regulation of the maltose system of Escherichia coli, is highly homologous to the repressor proteins GalR, CytR, and LacI. Reidl, J., Römisch, K., Ehrmann, M., Boos, W. J. Bacteriol. (1989) [Pubmed]
  20. Reconstitution of maltose transport in malB and malA mutants of Escherichia coli. Brass, J.M. Ann. Microbiol. (Paris) (1982) [Pubmed]
  21. Two domains of MalT, the activator of the Escherichia coli maltose regulon, bear determinants essential for anti-activation by MalK. Richet, E., Joly, N., Danot, O. J. Mol. Biol. (2005) [Pubmed]
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