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)

P68701

- ATPL_ECO57

UniProt

P68701 - ATPL_ECO57

Protein

ATP synthase subunit c

Gene

atpE

Organism
Escherichia coli O157:H7
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
  1. Functioni

    F1F0 ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F1 containing the extramembraneous catalytic core and F0 containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation.UniRule annotation
    Key component of the F0 channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F1 delta and epsilon subunits.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei61 – 611Reversibly protonated during proton transportUniRule annotation

    GO - Molecular functioni

    1. hydrogen ion transmembrane transporter activity Source: InterPro
    2. lipid binding Source: UniProtKB-KW

    GO - Biological processi

    1. ATP hydrolysis coupled proton transport Source: InterPro
    2. ATP synthesis coupled proton transport Source: InterPro

    Keywords - Biological processi

    ATP synthesis, Hydrogen ion transport, Ion transport, Transport

    Keywords - Ligandi

    Lipid-binding

    Enzyme and pathway databases

    BioCyciECOL386585:GJFA-4647-MONOMER.
    ECOO157:ATPE-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP synthase subunit cUniRule annotation
    Alternative name(s):
    ATP synthase F(0) sector subunit cUniRule annotation
    F-type ATPase subunit cUniRule annotation
    Short name:
    F-ATPase subunit cUniRule annotation
    Lipid-binding proteinUniRule annotation
    Gene namesi
    Name:atpEUniRule annotation
    Ordered Locus Names:Z5235, ECs4679
    OrganismiEscherichia coli O157:H7
    Taxonomic identifieri83334 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000558: Chromosome, UP000002519: Chromosome

    Subcellular locationi

    Cell inner membrane UniRule annotation; Multi-pass membrane protein UniRule annotation

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell
    3. proton-transporting ATP synthase complex, coupling factor F(o) Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, CF(0), Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 7979ATP synthase subunit cPRO_0000112146Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-formylmethionineBy similarity

    Keywords - PTMi

    Formylation

    Interactioni

    Subunit structurei

    F-type ATPases have 2 components, F1 - the catalytic core - and F0 - the membrane proton channel. F1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. F0 has three main subunits: a1, b2 and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F1 is attached to F0 by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains.UniRule annotation

    Protein-protein interaction databases

    STRINGi155864.Z5235.

    Structurei

    3D structure databases

    ProteinModelPortaliP68701.
    SMRiP68701. Positions 1-79.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei11 – 3121HelicalUniRule annotationAdd
    BLAST
    Transmembranei53 – 7321HelicalUniRule annotationAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATPase C chain family.UniRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0636.
    HOGENOMiHOG000235244.
    KOiK02110.
    OMAiELHIVPE.
    OrthoDBiEOG68H8G3.

    Family and domain databases

    Gene3Di1.20.20.10. 1 hit.
    HAMAPiMF_01396. ATP_synth_c_bact.
    InterProiIPR000454. ATPase_F0-cplx_csu.
    IPR005953. ATPase_F0-cplx_csu_bac/chlpt.
    IPR020537. ATPase_F0-cplx_csu_DDCD_BS.
    IPR002379. ATPase_proteolipid_c_like_dom.
    [Graphical view]
    PfamiPF00137. ATP-synt_C. 1 hit.
    [Graphical view]
    PRINTSiPR00124. ATPASEC.
    SUPFAMiSSF81333. SSF81333. 1 hit.
    TIGRFAMsiTIGR01260. ATP_synt_c. 1 hit.
    PROSITEiPS00605. ATPASE_C. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P68701-1 [UniParc]FASTAAdd to Basket

    « Hide

    MENLNMDLLY MAAAVMMGLA AIGAAIGIGI LGGKFLEGAA RQPDLIPLLR   50
    TQFFIVMGLV DAIPMIAVGL GLYVMFAVA 79
    Length:79
    Mass (Da):8,256
    Last modified:July 21, 1986 - v1
    Checksum:i0F595A69D8AD1F9E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005174 Genomic DNA. Translation: AAG58940.1.
    BA000007 Genomic DNA. Translation: BAB38102.1.
    PIRiG91213.
    H86059.
    RefSeqiNP_290376.1. NC_002655.2.
    NP_312706.1. NC_002695.1.

    Genome annotation databases

    EnsemblBacteriaiAAG58940; AAG58940; Z5235.
    BAB38102; BAB38102; BAB38102.
    GeneIDi915336.
    960436.
    KEGGiece:Z5235.
    ecs:ECs4679.
    PATRICi18358955. VBIEscCol44059_4642.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005174 Genomic DNA. Translation: AAG58940.1 .
    BA000007 Genomic DNA. Translation: BAB38102.1 .
    PIRi G91213.
    H86059.
    RefSeqi NP_290376.1. NC_002655.2.
    NP_312706.1. NC_002695.1.

    3D structure databases

    ProteinModelPortali P68701.
    SMRi P68701. Positions 1-79.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 155864.Z5235.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAG58940 ; AAG58940 ; Z5235 .
    BAB38102 ; BAB38102 ; BAB38102 .
    GeneIDi 915336.
    960436.
    KEGGi ece:Z5235.
    ecs:ECs4679.
    PATRICi 18358955. VBIEscCol44059_4642.

    Phylogenomic databases

    eggNOGi COG0636.
    HOGENOMi HOG000235244.
    KOi K02110.
    OMAi ELHIVPE.
    OrthoDBi EOG68H8G3.

    Enzyme and pathway databases

    BioCyci ECOL386585:GJFA-4647-MONOMER.
    ECOO157:ATPE-MONOMER.

    Family and domain databases

    Gene3Di 1.20.20.10. 1 hit.
    HAMAPi MF_01396. ATP_synth_c_bact.
    InterProi IPR000454. ATPase_F0-cplx_csu.
    IPR005953. ATPase_F0-cplx_csu_bac/chlpt.
    IPR020537. ATPase_F0-cplx_csu_DDCD_BS.
    IPR002379. ATPase_proteolipid_c_like_dom.
    [Graphical view ]
    Pfami PF00137. ATP-synt_C. 1 hit.
    [Graphical view ]
    PRINTSi PR00124. ATPASEC.
    SUPFAMi SSF81333. SSF81333. 1 hit.
    TIGRFAMsi TIGR01260. ATP_synt_c. 1 hit.
    PROSITEi PS00605. ATPASE_C. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
    2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
      Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
      , Kuhara S., Shiba T., Hattori M., Shinagawa H.
      DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

    Entry informationi

    Entry nameiATPL_ECO57
    AccessioniPrimary (citable) accession number: P68701
    Secondary accession number(s): P00844
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 71 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Dicyclohexylcarbodiimide (DCDD) binding to the active aspartate residue inhibits ATPase in vitro.By similarity

    Keywords - Technical termi

    Complete proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3