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ATPG_PARDP
ID   ATPG_PARDP              Reviewed;         290 AA.
AC   A1B8N9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=Pden_3817;
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA   Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 2 of Paracoccus denitrificans PD1222.";
RL   Submitted (DEC-2006) 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; CP000490; ABL71883.1; -; Genomic_DNA.
DR   RefSeq; WP_011750052.1; NC_008687.1.
DR   PDB; 5DN6; X-ray; 3.98 A; G=1-290.
DR   PDBsum; 5DN6; -.
DR   AlphaFoldDB; A1B8N9; -.
DR   SMR; A1B8N9; -.
DR   STRING; 318586.Pden_3817; -.
DR   TCDB; 3.A.2.1.7; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR   PRIDE; A1B8N9; -.
DR   EnsemblBacteria; ABL71883; ABL71883; Pden_3817.
DR   KEGG; pde:Pden_3817; -.
DR   eggNOG; COG0224; Bacteria.
DR   HOGENOM; CLU_050669_0_1_5; -.
DR   OMA; MQITSAM; -.
DR   Proteomes; UP000000361; Chromosome 2.
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   1: Evidence at protein level;
KW   3D-structure; ATP synthesis; Cell inner membrane; Cell membrane; CF(1);
KW   Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW   Transport.
FT   CHAIN           1..290
FT                   /note="ATP synthase gamma chain"
FT                   /id="PRO_1000053277"
SQ   SEQUENCE   290 AA;  31599 MW;  622A5B7BEE74FA7F CRC64;
     MPSLKDLKNR IGSVKNTRKI TKAMQMVAAA KLRRAQEAAE AARPYADRMA AVMAGLTAAA
     AGSDMAPRLL AGTGEDRRHL LVVMTSERGL AGGFNSSIVK LARLRLQELQ AQGKQVSILT
     VGKKGREQLK REYGDLFVNH VDLSEVKRIG YDNARAIADE ILDRFDNGEF DVATLFYNRF
     ESVISQVPTA RQVIPAVIEE GEAGASSLYD YEPDENAILN DLLPRSVATQ VFAALLENAA
     SEQGARMTAM DNATRNAGDM IDRLTTVYNR SRQAAITKEL IEIISGAEAL
 
 
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