U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

Links from GEO Profiles

    • Showing Current items.

    malK maltose ABC transporter ATP binding subunit [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 948537, updated on 17-Dec-2024

    Summary

    Go to the top of the page Help
    Official Symbol
    malK
    Official Full Name
    maltose ABC transporter ATP binding subunit
    Primary source
    ECOCYC:EG10558
    Locus tag
    b4035
    See related
    ASAP:ABE-0013216
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
    Lineage
    Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
    Also known as
    ECK4027; malB
    Summary
    The inactive, ATP-bound form of MalK directly antagonizes the mal regulon activator MalT. [More information is available at EcoGene: EG10558]. MalK is the ATP-binding component of the maltose ABC transporter. [More information is available at EcoCyc: EG10558].
    NEW
    Try the new Gene table
    Try the new Transcript table

    Genomic context

    Go to the top of the page Help
    Sequence:
    NC_000913.3 (4246784..4247899)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene maltose ABC transporter membrane subunit MalF Neighboring gene maltose ABC transporter periplasmic binding protein Neighboring gene maltose outer membrane channel/phage lambda receptor protein Neighboring gene maltose regulon periplasmic protein

    Genomic regions, transcripts, and products

    Go to the top of the page Help
    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

    Go to the top of the pageHelp

    Related articles in PubMed

    1. Vanadate-catalyzed photocleavage of the signature motif of an ATP-binding cassette (ABC) transporter. Fetsch EE, et al. Proc Natl Acad Sci U S A, 2002 Jul 23. PMID 12093921, Free PMC Article
    2. Characterization of site-directed mutations in conserved domains of MalK, a bacterial member of the ATP-binding cassette (ABC) family [corrected]. Walter C, et al. FEBS Lett, 1992 May 25. PMID 1592114
    3. The role of ATP as the energy source for maltose transport in Escherichia coli. Dean DA, et al. Res Microbiol, 1990 Mar-Apr. PMID 2177914
    4. Stabilization of translationally active mRNA by prokaryotic REP sequences. Newbury SF, et al. Cell, 1987 Jan 30. PMID 2433046
    5. A network of dynamically conserved residues deciphers the motions of maltose transporter. Lukman S, et al. Proteins, 2009 Aug 15. PMID 19274733

    See all (174) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Coupling between ATP hydrolysis and protein conformational change in maltose transporter MalK has been described.
      Title: Coupling between ATP hydrolysis and protein conformational change in maltose transporter.
    2. Data indicate that MalFGK2 transporter is comprised of two membrane proteins, MalF and MalG, and the nucleotide-binding domain, which controls the conformation of MalFG, is composed of the homodimeric MalK subunit.
      Title: Formation of a Chloride-conducting State in the Maltose ATP-binding Cassette (ABC) Transporter.
    3. Data suggest that the binding and conformational change of maltose transporter (MalFGK2) may provide some insights into the understanding of the mechanism of ABC transporters.
      Title: Allosteric transitions of the maltose transporter studied by an elastic network model.
    4. The water-mediated entropic force is important for ATP-induced conformational changes of nucleotide-binding domains in MalK.
      Title: ATP-induced conformational changes of nucleotide-binding domains in an ABC transporter. Importance of the water-mediated entropic force.
    5. Escherichia coli maltose binding protein has inhibitory effects on beta-amyloid aggregation and cytotoxicity
      Title: The inhibitory effects of Escherichia coli maltose binding protein on β-amyloid aggregation and cytotoxicity.
    6. The molecular entity that interacts with MalT is not free MalK, but the maltose transporter, MalFGK(2) , which sequesters MalT to the membrane.
      Title: The ABC transporter MalFGK(2) sequesters the MalT transcription factor at the membrane in the absence of cognate substrate.
    7. using x-ray crystallography, study captured the maltose transporter in an intermediate step between the inward- and outward-facing states
      Title: Crystal structure of the maltose transporter in a pretranslocation intermediate state.
    8. substrate availability is communicated from MalE to the MalK dimer via extracytoplasmic loops of MalFG
      Title: Maltose binding protein (MalE) interacts with periplasmic loops P2 and P1 respectively of the MalFG subunits of the maltose ATP binding cassette transporter (MalFGK(2)) from Escherichia coli/Salmonella during the transport cycle.
    9. 2.8-A crystal structure of the intact maltose transporter in complex with the maltose-binding protein, maltose and ATP
      Title: Crystal structure of a catalytic intermediate of the maltose transporter.
    10. ATP-driven MalK dimer closure and reopening are crucial steps in the translocation cycle of the intact maltose transporter MalFGK2
      Title: ATP-driven MalK dimer closure and reopening and conformational changes of the "EAA" motifs are crucial for function of the maltose ATP-binding cassette transporter (MalFGK2).
    Submit: New GeneRIF Correction See all GeneRIFs (11)

    Interactions

    Go to the top of the page Help
    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Go to the top of the page Help

    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables ABC-type maltose transporter activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables ABC-type maltose transporter activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables ABC-type maltose transporter activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ABC-type transporter activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ATP binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables ATP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ATP binding IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables ATP hydrolysis activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables DNA-binding transcription factor binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in carbohydrate transport IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within maltodextrin transmembrane transport IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in maltodextrin transmembrane transport IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in maltose transmembrane transport IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within maltose transport IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in negative regulation of maltose transport NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    involved_in negative regulation of transmembrane transport NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    involved_in transmembrane transport IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    part_of ATP-binding cassette (ABC) transporter complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of ATP-binding cassette (ABC) transporter complex IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    part_of enzyme IIA-maltose transporter complex IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    part_of maltose transport complex IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    part_of maltose transport complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of maltose transport complex IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    located_in membrane IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in plasma membrane IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

    Go to the top of the page Help
    Preferred Names
    maltose ABC transporter ATP binding subunit
    NP_418459.1

    NCBI Reference Sequences (RefSeq)

    Go to the top of the page Help

    NEW Try the new Transcript table

    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_000913.3 Reference assembly

      Range
      4246784..4247899
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_418459.1 maltose ABC transporter ATP binding subunit [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_418459.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A8S7I4J8, A0A8T6BIJ2
      Conserved Domains (1) summary
      PRK11000
      Location:1 → 371
      PRK11000; maltose/maltodextrin ABC transporter ATP-binding protein MalK
    Nucleotide Protein
    Heading Accession and Version

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.