Q9ZEC2 (ATPL_RICPR) Reviewed, UniProtKB/Swiss-Prot

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:	RP022

Organism

Rickettsia prowazekii (strain Madrid E) [Reference proteome] [HAMAP]

Taxonomic identifier

272947 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › typhus group › Rickettsia prowazekii

Protein attributes

Sequence length	74 AA.
Sequence status	Complete.
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. 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.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(0) Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Lipid-binding
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: InterPro ATP synthesis coupled proton transport Inferred from electronic annotation. Source: InterPro
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell proton-transporting ATP synthase complex, coupling factor F(o) Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	hydrogen ion transmembrane transporter activity Inferred from electronic annotation. Source: InterPro 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-Rule MF_01396		PRO_0000112161
Regions
	Transmembrane	8 – 28	21	Helical; Potential
	Transmembrane	52 – 72	21	Helical; Potential
Sites
	Site	58	1	Reversibly protonated during proton transport By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9ZEC2 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 7AA5D0812840067A	FASTA	74	7,686
	10 20 30 40 50 60 MDIVSLKFIG IGFMAIGMYG AALGVSNIFS SLLSAIARNP SAAENLQRMA LIGAGLAEAM 70 GLFSFVIAML LIFS

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.
PIR	F71709.
RefSeq	NP_220416.1. NC_000963.1.
3D structure databases
ProteinModelPortal	Q9ZEC2.
ModBase	Search...
Protein-protein interaction databases
STRING	272947.RP022.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAA14493; CAA14493; CAA14493.
GeneID	883547.
KEGG	rpr:RP022.
PATRIC	17900776. VBIRicPro72556_0022.
Phylogenomic databases
eggNOG	COG0636.
HOGENOM	HOG000235245.
KO	K02110.
OMA	GIACLGM.
ProtClustDB	PRK07558.
Family and domain databases
Gene3D	1.20.20.10. 1 hit.
HAMAP	MF_01396. ATP_synth_c_bact.
InterPro	IPR000454. ATPase_F0-cplx_csu. IPR020537. ATPase_F0-cplx_csu_DDCD_BS. IPR002379. ATPase_proteolipid_c_like_dom. [Graphical view]
Pfam	PF00137. ATP-synt_C. 1 hit. [Graphical view]
PRINTS	PR00124. ATPASEC.
SUPFAM	SSF81333. ATPase_F0/V0_c. 1 hit.
PROSITE	PS00605. ATPASE_C. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATPL_RICPR

Accession

Primary (citable) accession number: Q9ZEC2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program