ATPG_HELAH
ID ATPG_HELAH Reviewed; 301 AA.
AC Q17Y79;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=ATP synthase gamma chain {ECO:0000255|HAMAP-Rule:MF_00815};
DE AltName: Full=ATP synthase F1 sector gamma subunit {ECO:0000255|HAMAP-Rule:MF_00815};
DE AltName: Full=F-ATPase gamma subunit {ECO:0000255|HAMAP-Rule:MF_00815};
GN Name=atpG {ECO:0000255|HAMAP-Rule:MF_00815}; OrderedLocusNames=Hac_0581;
OS Helicobacter acinonychis (strain Sheeba).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=382638;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sheeba;
RX PubMed=16789826; DOI=10.1371/journal.pgen.0020120;
RA Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G.,
RA Gressmann H., Achtman M., Schuster S.C.;
RT "Who ate whom? Adaptive Helicobacter genomic changes that accompanied a
RT host jump from early humans to large felines.";
RL PLoS Genet. 2:1097-1110(2006).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. The gamma chain is believed to be important in
CC regulating ATPase activity and the flow of protons through the CF(0)
CC complex. {ECO:0000255|HAMAP-Rule:MF_00815}.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a, b and c. {ECO:0000255|HAMAP-Rule:MF_00815}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00815}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00815}.
CC -!- SIMILARITY: Belongs to the ATPase gamma chain family.
CC {ECO:0000255|HAMAP-Rule:MF_00815}.
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DR EMBL; AM260522; CAJ99397.1; -; Genomic_DNA.
DR RefSeq; WP_011577511.1; NC_008229.1.
DR AlphaFoldDB; Q17Y79; -.
DR SMR; Q17Y79; -.
DR STRING; 382638.Hac_0581; -.
DR EnsemblBacteria; CAJ99397; CAJ99397; Hac_0581.
DR KEGG; hac:Hac_0581; -.
DR eggNOG; COG0224; Bacteria.
DR HOGENOM; CLU_050669_0_1_7; -.
DR OMA; MQITSAM; -.
DR OrthoDB; 1701531at2; -.
DR BioCyc; HACI382638:HAC_RS02570-MON; -.
DR Proteomes; UP000000775; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IEA:UniProtKB-UniRule.
DR CDD; cd12151; F1-ATPase_gamma; 1.
DR HAMAP; MF_00815; ATP_synth_gamma_bact; 1.
DR InterPro; IPR035968; ATP_synth_F1_ATPase_gsu.
DR InterPro; IPR000131; ATP_synth_F1_gsu.
DR PANTHER; PTHR11693; PTHR11693; 2.
DR Pfam; PF00231; ATP-synt; 1.
DR PRINTS; PR00126; ATPASEGAMMA.
DR SUPFAM; SSF52943; SSF52943; 1.
DR TIGRFAMs; TIGR01146; ATPsyn_F1gamma; 1.
PE 3: Inferred from homology;
KW ATP synthesis; Cell inner membrane; Cell membrane; CF(1);
KW Hydrogen ion transport; Ion transport; Membrane; Transport.
FT CHAIN 1..301
FT /note="ATP synthase gamma chain"
FT /id="PRO_1000053226"
SQ SEQUENCE 301 AA; 34050 MW; FC41DF7E9D976C03 CRC64;
MANLRDIRKK IGSVKNTQKI THAMKLVSTS KLRKAEEVAR NSRAYALKLD AVFDDVLSKM
KNQGIKDIQS KYFRELERLE IKKVDIIFIT ADKGLCGGFN ANTIKKVLAC TNEYQEKDIK
VRLRGIGKKG NEYFSFNGIE VLDKINDLSS MPNYERAQEF MQKVVEDYLN GKTDKVVIIH
NGFKNMIIQE IRVKTILPIG HHIIHQNSQP SEAQETITSE PSGSEDEILD SLAKKYVEYS
LYYALIDSLA AEHSARMQAM DTATNNAKDL VKNLTISYNK ARQEAITTEL VEINAGVEAL
K
