ID   ATPG_UREPA              Reviewed;         286 AA.
AC   Q9PR14;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=UU130;
OS   Ureaplasma parvum serovar 3 (strain ATCC 700970).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX   NCBI_TaxID=273119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700970;
RX   PubMed=11048724; DOI=10.1038/35037619;
RA   Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y.,
RA   Cassell G.H.;
RT   "The complete sequence of the mucosal pathogen Ureaplasma urealyticum.";
RL   Nature 407:757-762(2000).
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 membrane {ECO:0000255|HAMAP-Rule:MF_00815};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-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; AF222894; AAF30536.1; -; Genomic_DNA.
DR   RefSeq; WP_006688922.1; NC_002162.1.
DR   AlphaFoldDB; Q9PR14; -.
DR   SMR; Q9PR14; -.
DR   STRING; 273119.UU130; -.
DR   EnsemblBacteria; AAF30536; AAF30536; UU130.
DR   GeneID; 29672729; -.
DR   KEGG; uur:UU130; -.
DR   eggNOG; COG0224; Bacteria.
DR   HOGENOM; CLU_050669_0_1_14; -.
DR   OMA; MQITSAM; -.
DR   Proteomes; UP000000423; 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; 1.
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 membrane; CF(1); Hydrogen ion transport; Ion transport;
KW   Membrane; Reference proteome; Transport.
FT   CHAIN           1..286
FT                   /note="ATP synthase gamma chain"
FT                   /id="PRO_0000073409"
SQ   SEQUENCE   286 AA;  32295 MW;  C9AE278976AAE4F5 CRC64;
     MSLDAMKRKI NSVQTTAKIT NAMKLVATAK LKRQRDRLAA IKEYCHDYYD VIGLLLSVVD
     DVEFLKIPNA KDRTLYITIN STMGLAGSYN YNVNKLISKI VNETDITFTI GKKGHDFMRL
     SGRVDQVNTY LNLNDNDLTF DMSLQIAREA LELYSQGEVN KICIIYTKFI NAITFEVSVI
     DVLPFDKTAL IKDHLAETIE LAKDNIIFKP NKFELVKKIL PTYIATVLYG SLIESKISEN
     ASRRNAMDAA TKNAKALAEN YKLIYNTLRQ GKITREITEI VAGSDD