B1Y3T2 (ATPL_LEPCP) 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:	Lcho_3531

Organism

Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix discophora (strain SP-6)) [Complete proteome] [HAMAP]

Taxonomic identifier

395495 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › unclassified Burkholderiales › Burkholderiales Genera incertae sedis › Leptothrix › Leptothrix cholodnii

Protein attributes

Sequence length	82 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
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 – 82	82	ATP synthase subunit c HAMAP-Rule MF_01396		PRO_1000184409
Regions
	Transmembrane	7 – 27	21	Helical; Potential
	Transmembrane	53 – 73	21	Helical; Potential
Sites
	Site	60	1	Reversibly protonated during proton transport By similarity

Sequences

	Sequence		Length	Mass (Da)
	B1Y3T2 [UniParc]. Last modified May 20, 2008. Version 1. Checksum: F1AF5CD226B3A537	FASTA	82	8,483
	10 20 30 40 50 60 MENVLGLVAL ACGIIIGLGA IGACIGIALM GGKYLEASAR QPELMNELQT KMFLLAGLID 70 80 AAFLIGVGIA MLFAFANPFV LK

References

[1]

"Complete sequence of Leptothrix cholodnii SP-6." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. , Kyrpides N., Lykidis A., Emerson D., Richardson P. Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51168 / LMG 8142 / SP-6.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001013 Genomic DNA. Translation: ACB35785.1.
RefSeq	YP_001792550.1. NC_010524.1.
3D structure databases
ProteinModelPortal	B1Y3T2.
ModBase	Search...
Protein-protein interaction databases
STRING	395495.Lcho_3531.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACB35785; ACB35785; Lcho_3531.
GeneID	6161271.
KEGG	lch:Lcho_3531.
PATRIC	22397485. VBILepCho83238_3563.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0636.
HOGENOM	HOG000235244.
KO	K02110.
OMA	IDASFII.
ProtClustDB	PRK06876.
Enzyme and pathway databases
BioCyc	LCHO395495:GHYL-3579-MONOMER.
Family and domain databases
Gene3D	1.20.20.10. 1 hit.
HAMAP	MF_01396. ATP_synth_c_bact.
InterPro	IPR000454. 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]
Pfam	PF00137. ATP-synt_C. 1 hit. [Graphical view]
PRINTS	PR00124. ATPASEC.
SUPFAM	SSF81333. ATPase_F0/V0_c. 1 hit.
TIGRFAMs	TIGR01260. ATP_synt_c. 1 hit.
PROSITE	PS00605. ATPASE_C. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATPL_LEPCP

Accession

Primary (citable) accession number: B1Y3T2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	May 20, 2008
Last modified:	May 1, 2013
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program