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atpG ATP synthase F1 complex subunit gamma [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 948243, updated on 2-May-2024

Summary

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Gene symbol
atpG
Gene description
ATP synthase F1 complex subunit gamma
Primary source
ASAP:ABE-0012211
Locus tag
b3733
See related
ECOCYC:EG10104
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
ECK3726; papC; uncG
Summary
HT_Cmplx10_Mem: [More information is available at EcoGene: EG10104]. The gamma subunit appears to play an important role in coupling the catalytic site events with proton translocation in association with the epsilon subunit. [More information is available at EcoCyc: EG10104].
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Genomic context

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Sequence:
NC_000913.3 (3917402..3918265, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene ATP synthase F1 complex subunit epsilon Neighboring gene ATP synthase F1 complex subunit beta Neighboring gene ATP synthase F1 complex subunit alpha Neighboring gene ATP synthase F1 complex subunit delta

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. Anatomy of F1-ATPase powered rotation. Martin JL, et al. Proc Natl Acad Sci U S A, 2014 Mar 11. PMID 24567403, Free PMC Article
  2. Temperature dependence of single molecule rotation of the Escherichia coli ATP synthase F1 sector reveals the importance of gamma-beta subunit interactions in the catalytic dwell. Sekiya M, et al. J Biol Chem, 2009 Aug 14. PMID 19502237, Free PMC Article
  3. Inhibition of ATPase activity of Escherichia coli ATP synthase by polyphenols. Dadi PK, et al. Int J Biol Macromol, 2009 Jul 1. PMID 19375450
  4. Reduced diversity and increased virulence-gene carriage in intestinal enterobacteria of coeliac children. Sánchez E, et al. BMC Gastroenterol, 2008 Nov 4. PMID 18983674, Free PMC Article
  5. A rotor-stator cross-link in the F1-ATPase blocks the rate-limiting step of rotational catalysis. Scanlon JA, et al. J Biol Chem, 2008 Sep 19. PMID 18628203, Free PMC Article

See all (85) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. A series of angular accelerations and decelerations occur during the power stroke of the F!-ATPase molecular motor.
    Title: Anatomy of F1-ATPase powered rotation.
  2. The catalytic activity of PapC is required to initiate pilus biogenesis.
    Title: Function of the usher N-terminus in catalysing pilus assembly.
  3. analysis of epsilon and gamma subunits roles in inhibited and active states of Escherichia coli ATP synthase F1 rotation
    Title: Single molecule behavior of inhibited and active states of Escherichia coli ATP synthase F1 rotation.
  4. The P pilus usher PapC R652 is important for high-affinity binding to the adhesin whereas F21 is important for limiting affinity for the PapA major rod subunit.
    Title: The differential affinity of the usher for chaperone-subunit complexes is required for assembly of complete pili.
  5. The PapC usher domain structure reveals a beta-sandwich fold very similar to that of the plug domain, a domain of PapC obstructing its translocation domain.
    Title: Structural homology between the C-terminal domain of the PapC usher and its plug.
  6. the temperature dependence of single molecule rotation of the Escherichia coli ATP synthase F1 sector reveals the importance of gamma-beta subunit interactions in the catalytic dwell
    Title: Temperature dependence of single molecule rotation of the Escherichia coli ATP synthase F1 sector reveals the importance of gamma-beta subunit interactions in the catalytic dwell.
  7. Prevalence of P fimbriae (papC), capsule K5 (sfaD/E) and haemolysin (hlyA) genes was higher in E. coli isolated from active and non-active coeliac children than in those from control subjects [papC; sfaD/E; hlyA].
    Title: Reduced diversity and increased virulence-gene carriage in intestinal enterobacteria of coeliac children.
  8. PapC and FimD of Uropathogenic E coli are ushers bound to a translocating type 1 pilus assembly intermediate; they capture the secretion of a virulence factor across the outer membrane.
    Title: Fiber formation across the bacterial outer membrane by the chaperone/usher pathway.
  9. N-terminus verified by Edman degradation on mature peptide
    Title: Structure of the gamma subunit of Escherichia coli F1 ATPase probed in trypsin digestion and biotin-avidin binding studies.
  10. overall molecular size (11 nm), pore size (2 nm), and twin-pore configuration of PapC resemble that of the Tom40 complex, a mitochondrial outer membrane protein translocase
    Title: The outer membrane usher forms a twin-pore secretion complex.
Submit: New GeneRIF Correction See all GeneRIFs (11)

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 ATP binding IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
contributes_to proton-transporting ATP synthase activity, rotational mechanism IBA
Inferred from Biological aspect of Ancestor
more info
  
contributes_to proton-transporting ATP synthase activity, rotational mechanism IDA
Inferred from Direct Assay
more info
 PubMed 
enables proton-transporting ATP synthase activity, rotational mechanism IDA
Inferred from Direct Assay
more info
 PubMed 
enables proton-transporting ATP synthase activity, rotational mechanism IEA
Inferred from Electronic Annotation
more info
  
enables proton-transporting ATPase activity, rotational mechanism IDA
Inferred from Direct Assay
more info
 PubMed 
Process Evidence Code Pubs
involved_in ATP biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
involved_in proton motive force-driven ATP synthesis IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in proton motive force-driven ATP synthesis IEA
Inferred from Electronic Annotation
more info
  
involved_in proton motive force-driven plasma membrane ATP synthesis IEA
Inferred from Electronic Annotation
more info
  
involved_in proton motive force-driven plasma membrane ATP synthesis IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in proton transmembrane transport IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
located_in membrane HDA PubMed 
located_in plasma membrane IEA
Inferred from Electronic Annotation
more info
  
located_in plasma membrane NAS
Non-traceable Author Statement
more info
 PubMed 
part_of proton-transporting ATP synthase complex IPI
Inferred from Physical Interaction
more info
 PubMed 
part_of proton-transporting ATP synthase complex, catalytic core F(1) IBA
Inferred from Biological aspect of Ancestor
more info
  
part_of proton-transporting ATP synthase complex, catalytic core F(1) IEA
Inferred from Electronic Annotation
more info
  
part_of proton-transporting ATP synthase complex, catalytic core F(1) IMP
Inferred from Mutant Phenotype
more info
 PubMed 

General protein information

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Preferred Names
ATP synthase F1 complex subunit gamma
NP_418189.1

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
    3917402..3918265 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_418189.1 ATP synthase F1 complex subunit gamma [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_418189.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A7A6MM84
    Conserved Domains (1) summary
    PRK05621
    Location:1 → 287
    PRK05621; F0F1 ATP synthase subunit gamma; Validated
Nucleotide Protein
Heading Accession and Version

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Other Literature Sources
Molecular Biology Databases
Research Materials