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P68701

- ATPL_ECO57

UniProt

P68701 - ATPL_ECO57

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Protein

ATP synthase subunit c

Gene

atpE

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

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
Complete GO annotation...

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

Topology

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

GO - Cellular componenti

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

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...

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

        10         20         30         40         50
MENLNMDLLY MAAAVMMGLA AIGAAIGIGI LGGKFLEGAA RQPDLIPLLR
60 70
TQFFIVMGLV DAIPMIAVGL GLYVMFAVA
Length:79
Mass (Da):8,256
Last modified:July 21, 1986 - v1
Checksum:i0F595A69D8AD1F9E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 29, 2014
This is version 72 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