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Q9ZEC2 (ATPL_RICPR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:RP022
OrganismRickettsia prowazekii (strain Madrid E) [Reference proteome] [HAMAP]
Taxonomic identifier272947 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group

Protein attributes

Sequence length74 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.

Sequence similarities

Belongs to the ATPase C chain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7474ATP synthase subunit c HAMAP-Rule MF_01396
PRO_0000112161

Regions

Transmembrane8 – 2821Helical; Potential
Transmembrane52 – 7221Helical; Potential

Sites

Site581Reversibly protonated during proton transport By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ZEC2 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 7AA5D0812840067A

FASTA747,686
        10         20         30         40         50         60 
MDIVSLKFIG IGFMAIGMYG AALGVSNIFS SLLSAIARNP SAAENLQRMA LIGAGLAEAM 

        70 
GLFSFVIAML LIFS 

« Hide

References

[1]"The genome sequence of Rickettsia prowazekii and the origin of mitochondria."
Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., Kurland C.G.
Nature 396:133-140(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Madrid E.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ235270 Genomic DNA. Translation: CAA14493.1.
PIRF71709.
RefSeqNP_220416.1. NC_000963.1.

3D structure databases

ProteinModelPortalQ9ZEC2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272947.RP022.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAA14493; CAA14493; CAA14493.
GeneID883547.
KEGGrpr:RP022.
PATRIC17900776. VBIRicPro72556_0022.

Phylogenomic databases

eggNOGCOG0636.
HOGENOMHOG000235245.
KOK02110.
OMAGIACLGM.
OrthoDBEOG68H8G3.
ProtClustDBPRK07558.

Family and domain databases

Gene3D1.20.20.10. 1 hit.
HAMAPMF_01396. ATP_synth_c_bact.
InterProIPR000454. ATPase_F0-cplx_csu.
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.
PROSITEPS00605. ATPASE_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameATPL_RICPR
AccessionPrimary (citable) accession number: Q9ZEC2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: February 19, 2014
This is version 85 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

Rickettsia prowazekii

Rickettsia prowazekii (strain Madrid E): entries and gene names