Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P0ABA6

- ATPG_ECOLI

UniProt

P0ABA6 - ATPG_ECOLI

Protein

ATP synthase gamma chain

Gene

atpG

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF0 complex.

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. protein binding Source: IntAct
    3. proton-transporting ATPase activity, rotational mechanism Source: EcoCyc
    4. proton-transporting ATP synthase activity, rotational mechanism Source: EcoCyc

    GO - Biological processi

    1. plasma membrane ATP synthesis coupled proton transport Source: UniProtKB-HAMAP

    Keywords - Biological processi

    ATP synthesis, Hydrogen ion transport, Ion transport, Transport

    Enzyme and pathway databases

    BioCyciEcoCyc:ATPG-MONOMER.
    ECOL316407:JW3711-MONOMER.
    MetaCyc:ATPG-MONOMER.

    Protein family/group databases

    TCDBi3.A.2.1.1. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP synthase gamma chain
    Alternative name(s):
    ATP synthase F1 sector gamma subunit
    F-ATPase gamma subunit
    Gene namesi
    Name:atpG
    Synonyms:papC, uncG
    Ordered Locus Names:b3733, JW3711
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10104. atpG.

    Subcellular locationi

    Cell inner membrane 1 Publication; Peripheral membrane protein 1 Publication

    GO - Cellular componenti

    1. membrane Source: UniProtKB
    2. plasma membrane Source: UniProtKB-SubCell
    3. proton-transporting ATP synthase complex, catalytic core F(1) Source: EcoliWiki

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, CF(1), Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 287287ATP synthase gamma chainPRO_0000073282Add
    BLAST

    Proteomic databases

    PaxDbiP0ABA6.
    PRIDEiP0ABA6.

    Expressioni

    Gene expression databases

    GenevestigatoriP0ABA6.

    Interactioni

    Subunit structurei

    F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a, b and c.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    atpCP0A6E64EBI-544306,EBI-544362

    Protein-protein interaction databases

    DIPiDIP-35938N.
    IntActiP0ABA6. 15 interactions.
    STRINGi511145.b3733.

    Structurei

    Secondary structure

    1
    287
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi20 – 5738
    Turni61 – 633
    Helixi66 – 683
    Beta strandi74 – 818
    Beta strandi84 – 863
    Helixi91 – 10818
    Beta strandi112 – 1198
    Helixi120 – 12910
    Beta strandi133 – 1375
    Helixi147 – 16115
    Beta strandi168 – 17710
    Beta strandi180 – 19011
    Turni196 – 1983
    Beta strandi207 – 2104
    Helixi212 – 24736

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1D8SX-ray4.40G1-287[»]
    1FS0X-ray2.10G19-248[»]
    3OAAX-ray3.26G/O/W/e2-287[»]
    ProteinModelPortaliP0ABA6.
    SMRiP0ABA6. Positions 2-285.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0ABA6.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATPase gamma chain family.Curated

    Phylogenomic databases

    eggNOGiCOG0224.
    HOGENOMiHOG000215912.
    KOiK02115.
    OMAiASIGYKH.
    OrthoDBiEOG6R5C97.
    PhylomeDBiP0ABA6.

    Family and domain databases

    HAMAPiMF_00815. ATP_synth_gamma_bact.
    InterProiIPR000131. ATPase_F1-cplx_gsu.
    IPR023632. ATPase_F1_gsu_CS.
    IPR023633. ATPase_F1_gsu_dom.
    [Graphical view]
    PANTHERiPTHR11693. PTHR11693. 1 hit.
    PfamiPF00231. ATP-synt. 1 hit.
    [Graphical view]
    PRINTSiPR00126. ATPASEGAMMA.
    SUPFAMiSSF52943. SSF52943. 1 hit.
    TIGRFAMsiTIGR01146. ATPsyn_F1gamma. 1 hit.
    PROSITEiPS00153. ATPASE_GAMMA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0ABA6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGAKEIRSK IASVQNTQKI TKAMEMVAAS KMRKSQDRMA ASRPYAETMR    50
    KVIGHLAHGN LEYKHPYLED RDVKRVGYLV VSTDRGLCGG LNINLFKKLL 100
    AEMKTWTDKG VQCDLAMIGS KGVSFFNSVG GNVVAQVTGM GDNPSLSELI 150
    GPVKVMLQAY DEGRLDKLYI VSNKFINTMS QVPTISQLLP LPASDDDDLK 200
    HKSWDYLYEP DPKALLDTLL RRYVESQVYQ GVVENLASEQ AARMVAMKAA 250
    TDNGGSLIKE LQLVYNKARQ ASITQELTEI VSGAAAV 287
    Length:287
    Mass (Da):31,577
    Last modified:July 21, 1986 - v1
    Checksum:i2417A4B8FBDB8EF8
    GO

    Sequence cautioni

    The sequence CAA23597.1 differs from that shown. Reason: Sequencing errors.
    The sequence CAA23597.1 differs from that shown. Reason: Frameshift at several positions.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01631 Genomic DNA. Translation: CAA25781.1.
    V00267 Genomic DNA. Translation: CAA23526.1.
    J01594 Genomic DNA. Translation: AAA24736.1. Frameshift.
    V00312 Genomic DNA. Translation: CAA23597.1. Sequence problems.
    M25464 Genomic DNA. Translation: AAA83874.1.
    L10328 Genomic DNA. Translation: AAA62085.1.
    U00096 Genomic DNA. Translation: AAC76756.1.
    AP009048 Genomic DNA. Translation: BAE77555.1.
    M34095 Genomic DNA. Translation: AAA24742.1.
    PIRiA01038. PWECG.
    RefSeqiNP_418189.1. NC_000913.3.
    YP_491696.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76756; AAC76756; b3733.
    BAE77555; BAE77555; BAE77555.
    GeneIDi12934007.
    948243.
    KEGGiecj:Y75_p3435.
    eco:b3733.
    PATRICi32122963. VBIEscCol129921_3857.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01631 Genomic DNA. Translation: CAA25781.1 .
    V00267 Genomic DNA. Translation: CAA23526.1 .
    J01594 Genomic DNA. Translation: AAA24736.1 . Frameshift.
    V00312 Genomic DNA. Translation: CAA23597.1 . Sequence problems.
    M25464 Genomic DNA. Translation: AAA83874.1 .
    L10328 Genomic DNA. Translation: AAA62085.1 .
    U00096 Genomic DNA. Translation: AAC76756.1 .
    AP009048 Genomic DNA. Translation: BAE77555.1 .
    M34095 Genomic DNA. Translation: AAA24742.1 .
    PIRi A01038. PWECG.
    RefSeqi NP_418189.1. NC_000913.3.
    YP_491696.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1D8S X-ray 4.40 G 1-287 [» ]
    1FS0 X-ray 2.10 G 19-248 [» ]
    3OAA X-ray 3.26 G/O/W/e 2-287 [» ]
    ProteinModelPortali P0ABA6.
    SMRi P0ABA6. Positions 2-285.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-35938N.
    IntActi P0ABA6. 15 interactions.
    STRINGi 511145.b3733.

    Protein family/group databases

    TCDBi 3.A.2.1.1. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

    Proteomic databases

    PaxDbi P0ABA6.
    PRIDEi P0ABA6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76756 ; AAC76756 ; b3733 .
    BAE77555 ; BAE77555 ; BAE77555 .
    GeneIDi 12934007.
    948243.
    KEGGi ecj:Y75_p3435.
    eco:b3733.
    PATRICi 32122963. VBIEscCol129921_3857.

    Organism-specific databases

    EchoBASEi EB0102.
    EcoGenei EG10104. atpG.

    Phylogenomic databases

    eggNOGi COG0224.
    HOGENOMi HOG000215912.
    KOi K02115.
    OMAi ASIGYKH.
    OrthoDBi EOG6R5C97.
    PhylomeDBi P0ABA6.

    Enzyme and pathway databases

    BioCyci EcoCyc:ATPG-MONOMER.
    ECOL316407:JW3711-MONOMER.
    MetaCyc:ATPG-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0ABA6.
    PROi P0ABA6.

    Gene expression databases

    Genevestigatori P0ABA6.

    Family and domain databases

    HAMAPi MF_00815. ATP_synth_gamma_bact.
    InterProi IPR000131. ATPase_F1-cplx_gsu.
    IPR023632. ATPase_F1_gsu_CS.
    IPR023633. ATPase_F1_gsu_dom.
    [Graphical view ]
    PANTHERi PTHR11693. PTHR11693. 1 hit.
    Pfami PF00231. ATP-synt. 1 hit.
    [Graphical view ]
    PRINTSi PR00126. ATPASEGAMMA.
    SUPFAMi SSF52943. SSF52943. 1 hit.
    TIGRFAMsi TIGR01146. ATPsyn_F1gamma. 1 hit.
    PROSITEi PS00153. ATPASE_GAMMA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "DNA sequence around the Escherichia coli unc operon. Completion of the sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS and phoS."
      Walker J.E., Gay N.J., Saraste M., Eberle A.N.
      Biochem. J. 224:799-815(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The atp operon: nucleotide sequence of the genes for the gamma, beta, and epsilon subunits of Escherichia coli ATP synthase."
      Saraste M., Gay N.J., Eberle A., Runswick M.J., Walker J.E.
      Nucleic Acids Res. 9:5287-5296(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Nucleotide sequence of the genes coding for alpha, beta and gamma subunits of the proton-translocating ATPase of Escherichia coli."
      Kanazawa H., Kayano T., Mabuchi K., Futai M.
      Biochem. Biophys. Res. Commun. 103:604-612(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Structure and function of H+-ATPase: what we have learned from Escherichia coli H+-ATPase."
      Kanazawa H., Futai M.
      Ann. N. Y. Acad. Sci. 402:45-64(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
      Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.
      Genomics 16:551-561(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    7. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    8. "Structure of the gamma subunit of Escherichia coli F1 ATPase probed in trypsin digestion and biotin-avidin binding studies."
      Tang C., Wilkens S., Capaldi R.A.
      J. Biol. Chem. 269:4467-4472(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-9; 72-81; 203-208 AND 214-220.
    9. "H(+)-ATPase gamma subunit of Escherichia coli. Role of the conserved carboxyl-terminal region."
      Iwamoto A., Miki J., Maeda M., Futai M.
      J. Biol. Chem. 265:5043-5048(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 261-287.
    10. Cited for: SUBUNIT, SUBCELLULAR LOCATION.
      Strain: BL21-DE3.
    11. "Structural features of the gamma subunit of the Escherichia coli F(1) ATPase revealed by a 4.4-A resolution map obtained by X-ray crystallography."
      Hausrath A.C., Grueber G., Matthews B.W., Capaldi R.A.
      Proc. Natl. Acad. Sci. U.S.A. 96:13697-13702(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (4.4 ANGSTROMS).

    Entry informationi

    Entry nameiATPG_ECOLI
    AccessioniPrimary (citable) accession number: P0ABA6
    Secondary accession number(s): P00837, P00838, Q2M851
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 86 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3