Reviewed, UniProtKB/Swiss-Prot Q68XQ0 (ATPL_RICTY)

Names and origin

Protein names

Recommended 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:	RT0106

Organism

Rickettsia typhi [Complete proteome] [HAMAP]

Taxonomic identifier

785 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › typhus group

Protein attributes

Sequence length	74 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred 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. 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.
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.
Sequence similarities	Belongs to the ATPase C chain family.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(0) Cell inner membrane Cell membrane Membrane
Domain	Transmembrane
Ligand	Lipid-binding
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ATP synthesis coupled proton transport Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW proton-transporting ATP synthase complex, coupling factor F(o) Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	hydrogen ion transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: HAMAP lipid binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 74	74	ATP synthase subunit c HAMAP MF_01396		PRO_0000288730
Regions
	Transmembrane	8 – 28	21	Potential
	Transmembrane	52 – 72	21	Potential
Sites
	Site	58	1	Reversibly protonated during proton transport By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q68XQ0-1 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 7AA5C65B2840067A	FASTA	74	7,670
	10 20 30 40 50 60 MDIVSLKFIG IGFMAIGMYG AALGVSNIFS SLLSAIARNP SAAENLQRMA LIGAGLAEAM 70 GLFAFVIAML LIFS

References

[1]

"Complete genome sequence of Rickettsia typhi and comparison with sequences of other Rickettsiae." McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E., McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E., Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A. , Hong C., Yu X.-J., Walker D.H., Weinstock G.M. J. Bacteriol. 186:5842-5855(2004) [PubMed: 15317790] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC VR-144 / Wilmington.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE017197 Genomic DNA. Translation: AAU03592.1.
RefSeq	YP_067074.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2958528.
GenomeReviews	Gene locus RT0106 in contig AE017197_GR.
KEGG	rty:RT0106.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q68XQ0.
OMA	MAIGMYG
Enzyme and pathway databases
BioCyc	RTYP257363:RT0106-MON.
BRENDA	3.6.3.14. 281221.
Family and domain databases
HAMAP	MF_01396. [Tree]
InterPro	IPR000454. ATPase_F0-cplx_csu. IPR020537. ATPase_F0-cplx_csu_DDCD_BS. IPR002379. ATPase_F0/V0-cplx_csu. [Graphical view]
Gene3D	G3DSA:1.20.20.10. ATPase_F0/V0_c. 1 hit.
Pfam	PF00137. ATP-synt_C. 1 hit. [Graphical view]
PRINTS	PR00124. ATPASEC.
PROSITE	PS00605. ATPASE_C. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATPL_RICTY

Accession

Primary (citable) accession number: Q68XQ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	October 11, 2004
Last modified:	November 24, 2009
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)