ID   ATPG_PSEMY              Reviewed;         287 AA.
AC   A4Y188;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=Pmen_4608;
OS   Pseudomonas mendocina (strain ymp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=399739;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ymp;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Hersman L., Dubois J., Maurice P., Richardson P.;
RT   "Complete sequence of Pseudomonas mendocina ymp.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000680; ABP87354.1; -; Genomic_DNA.
DR   RefSeq; WP_012020332.1; NC_009439.1.
DR   AlphaFoldDB; A4Y188; -.
DR   SMR; A4Y188; -.
DR   STRING; 399739.Pmen_4608; -.
DR   EnsemblBacteria; ABP87354; ABP87354; Pmen_4608.
DR   KEGG; pmy:Pmen_4608; -.
DR   PATRIC; fig|399739.8.peg.4673; -.
DR   eggNOG; COG0224; Bacteria.
DR   HOGENOM; CLU_050669_0_1_6; -.
DR   OMA; MQITSAM; -.
DR   OrthoDB; 1701531at2; -.
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   InterPro; IPR023632; ATP_synth_F1_gsu_CS.
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.
DR   PROSITE; PS00153; ATPASE_GAMMA; 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..287
FT                   /note="ATP synthase gamma chain"
FT                   /id="PRO_1000053294"
SQ   SEQUENCE   287 AA;  31528 MW;  6581339B98ED4711 CRC64;
     MAGAKEIRSK IASIKSTQKI TSAMEKVAVS KMRKAQQRMA AGRPYAERIR QVIGHLAKAN
     PEYRHSFMVE RDVKRVGYIV VTSDRGLCGG LNINLFKALL KSLKEWRDQK VEADFCVVGT
     KGASFFRSNG GNVVAAISKL GEEPSINDLI GSVKVVLDAY AEGRIDRLYL VSNKFVNTMT
     QKPEVQQLLP LAASDAQGVQ KGLWDYVYEP DAQQLLDALL VRYIESQVYQ SVVENSACEQ
     AARMIAMKNA TDNAGDLIKD LQLVYNKARQ AAITQEISEI VGGAAAV