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

    Gene ID: 948243, updated on 3-Dec-2024

    Summary

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    Official Symbol
    atpG
    Official Full Name
    ATP synthase F1 complex subunit gamma
    Primary source
    ECOCYC:EG10104
    Locus tag
    b3733
    See related
    ASAP:ABE-0012211
    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. The regulatory region of the L-arabinose operon: a physical, genetic and physiological study. Schleif R, et al. J Mol Biol, 1975 Jul 5. PMID 168391
    3. H(+)-ATPase gamma subunit of Escherichia coli. Role of the conserved carboxyl-terminal region. Iwamoto A, et al. J Biol Chem, 1990 Mar 25. PMID 2138624
    4. Structure of the gamma subunit of Escherichia coli F1 ATPase probed in trypsin digestion and biotin-avidin binding studies. Tang C, et al. J Biol Chem, 1994 Feb 11. PMID 7508444
    5. Topology of the outer membrane usher PapC determined by site-directed fluorescence labeling. Henderson NS, et al. J Biol Chem, 2004 Dec 17. PMID 15485883

    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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    Homology

    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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