Q9PR08 (ATPL_UREPA) 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:	UU136

Organism

Ureaplasma parvum serovar 3 (strain ATCC 700970) [Complete proteome] [HAMAP]

Taxonomic identifier

273119 [NCBI]

Taxonomic lineage

Bacteria › Tenericutes › Mollicutes › Mycoplasmataceae › Ureaplasma

Protein attributes

Sequence length	109 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 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 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 membrane; Multi-pass membrane protein By similarity HAMAP MF_01396.
Miscellaneous	Dicyclohexylcarbodiimide (DCDD) binding to the active glutamate residue inhibits ATPase in vitro By similarity. HAMAP 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 membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Lipid-binding
Technical term	Complete 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 – 109	109	ATP synthase subunit c HAMAP MF_01396		PRO_0000112175
Regions
	Transmembrane	42 – 62	21	Helical; Potential
	Transmembrane	88 – 108	21	Helical; Potential
Sites
	Site	92	1	Reversibly protonated during proton transport By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9PR08 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: CD72373089564AD3	FASTA	109	11,018
	10 20 30 40 50 60 MSSFIDITNV ISSHIEANLP AIASENVGSL ANGAGIAYLG KYIGTGITML AAGAVGLMQG 70 80 90 100 FSTANAVQAV ARNPEAQPKI LSTMIVGLAL AEAVAIYALI VSILIIFVA

References

[1]	"The complete sequence of the mucosal pathogen Ureaplasma urealyticum." Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y., Cassell G.H. Nature 407:757-762(2000) [PubMed: 11048724] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700970.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF222894 Genomic DNA. Translation: AAF30542.1.
RefSeq	NP_077967.1. NC_002162.1.
3D structure databases
ProteinModelPortal	Q9PR08.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	875901.
GenomeReviews	Gene locus UU136 in contig AF222894_GR.
KEGG	uur:UU136.
PATRIC	20533808. VBIUrePar45146_0142.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG753983.
OMA	GRNPEMA.
ProtClustDB	CLSK2298783.
Enzyme and pathway databases
BioCyc	UURE95667:UU136-MONOMER.
Family and domain databases
HAMAP	MF_01396. ATP_synth_c_bact. [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.
KO	K02110.
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_UREPA

Accession

Primary (citable) accession number: Q9PR08

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 2, 2001
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program