P43716 (ATPG_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP synthase gamma chain

Alternative name(s):
ATP synthase F1 sector gamma subunit
F-ATPase gamma subunit

Gene names

Name:	atpG
Ordered Locus Names:	HI_0480

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus › Haemophilus influenzae

Protein attributes

Sequence length	289 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF0 complex By similarity. HAMAP-Rule MF_00815
Subunit structure	F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a, b and c By similarity.
Subcellular location	Cell inner membrane; Peripheral membrane protein By similarity HAMAP-Rule MF_00815.
Sequence similarities	Belongs to the ATPase gamma chain family.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(1) Cell inner membrane Cell membrane Membrane
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	plasma membrane ATP synthesis coupled proton transport Inferred from electronic annotation. Source: HAMAP
Cellular_component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell proton-transporting ATP synthase complex, catalytic core F(1) Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP proton-transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: HAMAP proton-transporting ATPase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 289	289	ATP synthase gamma chain HAMAP-Rule MF_00815		PRO_0000073292

Sequences

	Sequence		Length	Mass (Da)
	P43716 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 622CBA682F37FD00	FASTA	289	32,069
	10 20 30 40 50 60 MAGAKEIKTK IASVQSTQKI TKAMEMVATS KMRKTQDRMA ASRPYSETIR NVISHVSKAS 70 80 90 100 110 120 IGYKHPFLVE REVKKIGILV ISTDRGMCGG LNVNLFKTTL NQIKNWKEQN ISTDLGLIGS 130 140 150 160 170 180 KGISFFRSFG FNIKGQLSGL GDTPALEELI GVANTMFDAY RNGEIDAVYI AYNKFVNTMS 190 200 210 220 230 240 QKPVVQQLVP LPESKDDHLN ERQQTWDYLY EPEPKVLLDS LLVRYLESQI YQAVVDNVAS 250 260 270 280 EQAARMVAMK AATDNAGNLI NDLRLVYNKA RQASITNELN EIVAGAAAI

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42023 Genomic DNA. Translation: AAC22138.1.
PIR	E64071.
RefSeq	NP_438640.1. NC_000907.1.
3D structure databases
ProteinModelPortal	P43716.
SMR	P43716. Positions 19-250.
ModBase	Search...
Protein-protein interaction databases
STRING	71421.HI0480.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC22138; AAC22138; HI_0480.
GeneID	949567.
KEGG	hin:HI0480.
PATRIC	20189513. VBIHaeInf48452_0499.
Phylogenomic databases
eggNOG	COG0224.
KO	K02115.
OMA	AGNLIND.
ProtClustDB	PRK05621.
Family and domain databases
HAMAP	MF_00815. ATP_synth_gamma_bact.
InterPro	IPR000131. ATPase_F1-cplx_gsu. IPR023632. ATPase_F1_gsu_CS. IPR023633. ATPase_F1_gsu_dom. [Graphical view]
PANTHER	PTHR11693. PTHR11693. 1 hit.
Pfam	PF00231. ATP-synt. 1 hit. [Graphical view]
PRINTS	PR00126. ATPASEGAMMA.
SUPFAM	SSF52943. ATPase_gamma. 1 hit.
TIGRFAMs	TIGR01146. ATPsyn_F1gamma. 1 hit.
PROSITE	PS00153. ATPASE_GAMMA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATPG_HAEIN

Accession

Primary (citable) accession number: P43716

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program