P43721 (ATPL_HAEIN) 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:	HI_0484

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	84 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 inner membrane; Multi-pass membrane protein By similarity HAMAP MF_01396.
Miscellaneous	Dicyclohexylcarbodiimide (DCDD) binding to the active aspartate 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 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 – 84	84	ATP synthase subunit c HAMAP MF_01396		PRO_0000112148
Regions
	Transmembrane	9 – 29	21	Helical; Potential
	Transmembrane	54 – 74	21	Helical; Potential
Sites
	Site	60	1	Reversibly protonated during proton transport By similarity

Sequences

	Sequence		Length	Mass (Da)
	P43721 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: E57C8B223498ED02	FASTA	84	8,641
	10 20 30 40 50 60 METVITATII GASILLAFAA LGTAIGFAIL GGKFLESSAR QPELASSLQT KMFIVAGLLD 70 80 AIAMIAVGIS LLFIFANPFI GLLN

References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

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Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42023 Genomic DNA. Translation: AAC22142.1.
PIR	I64071.
RefSeq	NP_438644.1. NC_000907.1.
3D structure databases
ProteinModelPortal	P43721.
SMR	P43721. Positions 7-76.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	949568.
GenomeReviews	Gene locus HI_0484 in contig L42023_GR.
KEGG	hin:HI0484.
PATRIC	20189521. VBIHaeInf48452_0503.
TIGR	HI_0484.
Phylogenomic databases
HOGENOM	HBG753983.
OMA	IALYMLF.
ProtClustDB	PRK06876.
Enzyme and pathway databases
BioCyc	HINF71421:HI_0484-MONOMER.
Family and domain databases
HAMAP	MF_01396. ATP_synth_c_bact. [Tree]
InterPro	IPR000454. ATPase_F0-cplx_csu. IPR005953. ATPase_F0-cplx_csu_bac/chlpt. 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.
TIGRFAMs	TIGR01260. ATP_synt_c. 1 hit.
PROSITE	PS00605. ATPASE_C. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATPL_HAEIN

Accession

Primary (citable) accession number: P43721

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	January 25, 2012
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program