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malG maltose ABC transporter membrane subunit MalG [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 948530, updated on 11-Apr-2024

Summary

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Gene symbol
malG
Gene description
maltose ABC transporter membrane subunit MalG
Primary source
ASAP:ABE-0013193
Locus tag
b4032
See related
ECOCYC:EG10556
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
ECK4024
Summary
The maltose transport complex MalFGK(2) also transports maltodextrin. [More information is available at EcoGene: EG10556]. MalG is an integral membrane component of the maltose ABC transporter. [More information is available at EcoCyc: EG10556].
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Genomic context

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Sequence:
NC_000913.3 (4242626..4243516, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene putative phosphate starvation-inducible protein PsiE Neighboring gene D-xylose:H(+) symporter Neighboring gene ncRNA Neighboring gene maltose ABC transporter membrane subunit MalF Neighboring gene maltose ABC transporter periplasmic binding protein

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Conformational Dynamics in the Binding-Protein-Independent Mutant of the Escherichia coli Maltose Transporter, MalG511, and Its Interaction with Maltose Binding Protein. Bajaj R, et al. Biochemistry, 2018 May 22. PMID 29637782, Free PMC Article
  2. Cellular localization of the MalG protein from the maltose transport system in Escherichia coli K12. Dassa E. Mol Gen Genet, 1990 Jun. PMID 2233678
  3. Studies of the maltose transport system reveal a mechanism for coupling ATP hydrolysis to substrate translocation without direct recognition of substrate. Gould AD, et al. J Biol Chem, 2010 Apr 9. PMID 20147285, Free PMC Article
  4. Formation of a Chloride-conducting State in the Maltose ATP-binding Cassette (ABC) Transporter. Carlson ML, et al. J Biol Chem, 2016 Jun 3. PMID 27059961, Free PMC Article
  5. Allosteric transitions of the maltose transporter studied by an elastic network model. Li CH, et al. Biopolymers, 2014 Jul. PMID 24865820

See all (161) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. the equilibrium of this mutant is shifted toward the semi-open state in its resting state and interacts with MBP with high affinity, providing an explanation for the inhibition of MalG511 by MBP at higher concentrations. In contrast, the mutant binding protein, MBPG13D, interacts with lower affinity and could restore MalG511 to a normal catalytic cycle
    Title: Conformational Dynamics in the Binding-Protein-Independent Mutant of the Escherichia coli Maltose Transporter, MalG511, and Its Interaction with Maltose Binding Protein.
  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. 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.
  5. analysis of the MalFGK2 mechanism for coupling ATP hydrolysis to substrate translocation without direct recognition of substrate
    Title: Studies of the maltose transport system reveal a mechanism for coupling ATP hydrolysis to substrate translocation without direct recognition of substrate.
  6. 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.
  7. 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.
  8. 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).
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Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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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 protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
Process Evidence Code Pubs
involved_in maltodextrin transmembrane transport IBA
Inferred from Biological aspect of Ancestor
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
  
involved_in maltose transport IBA
Inferred from Biological aspect of Ancestor
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 organic substance transport IEA
Inferred from Electronic Annotation
more info
  
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 enzyme IIA-maltose transporter complex IPI
Inferred from Physical Interaction
more info
 PubMed 
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 membrane IEA
Inferred from Electronic Annotation
more info
  
located_in plasma membrane IDA
Inferred from Direct Assay
more info
 PubMed 
located_in plasma membrane IEA
Inferred from Electronic Annotation
more info
  
located_in plasma membrane ISM
Inferred from Sequence Model
more info
 PubMed 

General protein information

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Preferred Names
maltose ABC transporter membrane subunit MalG
NP_418456.1

NCBI Reference Sequences (RefSeq)

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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
    4242626..4243516 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_418456.1 maltose ABC transporter membrane subunit MalG [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_418456.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A826YX71, A0A831GRB7
    Conserved Domains (1) summary
    PRK10998
    Location:1 → 296
    malG; maltose ABC transporter permease MalG
Nucleotide Protein
Heading Accession and Version

Gene LinkOut

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Other Literature Sources
Molecular Biology Databases
Research Materials