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P68701 (ATPL_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP synthase subunit c
Alternative name(s):
ATP synthase F(0) sector subunit c
F-type ATPase subunit c
Short name=F-ATPase subunit c
Lipid-binding protein
Gene names
Name:atpE
Ordered Locus Names:Z5235, ECs4679
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length79 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_01396

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 By similarity. HAMAP-Rule MF_01396

Subunit structure

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 By similarity.

Subcellular location

Cell inner membrane; Multi-pass membrane protein By similarity HAMAP-Rule MF_01396.

Miscellaneous

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

Sequence similarities

Belongs to the ATPase C chain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7979ATP synthase subunit c HAMAP-Rule MF_01396
PRO_0000112146

Regions

Transmembrane11 – 3121Helical; By similarity
Transmembrane53 – 7321Helical; By similarity

Sites

Site611Reversibly protonated during proton transport By similarity

Amino acid modifications

Modified residue11N-formylmethionine By similarity

Sequences

Sequence LengthMass (Da)Tools
P68701 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 0F595A69D8AD1F9E

FASTA798,256
        10         20         30         40         50         60 
MENLNMDLLY MAAAVMMGLA AIGAAIGIGI LGGKFLEGAA RQPDLIPLLR TQFFIVMGLV 

        70 
DAIPMIAVGL GLYVMFAVA 

« Hide

References

[1]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG58940.1.
BA000007 Genomic DNA. Translation: BAB38102.1.
PIRG91213.
H86059.
RefSeqNP_290376.1. NC_002655.2.
NP_312706.1. NC_002695.1.

3D structure databases

ProteinModelPortalP68701.
SMRP68701. Positions 1-79.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING155864.Z5235.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG58940; AAG58940; Z5235.
BAB38102; BAB38102; BAB38102.
GeneID915336.
960436.
KEGGece:Z5235.
ecs:ECs4679.
PATRIC18358955. VBIEscCol44059_4642.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0636.
HOGENOMHOG000235244.
KOK02110.
OMAELHIVPE.
OrthoDBEOG68H8G3.

Enzyme and pathway databases

BioCycECOL386585:GJFA-4647-MONOMER.
ECOO157:ATPE-MONOMER.

Family and domain databases

Gene3D1.20.20.10. 1 hit.
HAMAPMF_01396. ATP_synth_c_bact.
InterProIPR000454. 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]
PfamPF00137. ATP-synt_C. 1 hit.
[Graphical view]
PRINTSPR00124. ATPASEC.
SUPFAMSSF81333. SSF81333. 1 hit.
TIGRFAMsTIGR01260. ATP_synt_c. 1 hit.
PROSITEPS00605. ATPASE_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameATPL_ECO57
AccessionPrimary (citable) accession number: P68701
Secondary accession number(s): P00844
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 14, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families