ATPG_RICRS
ID ATPG_RICRS Reviewed; 323 AA.
AC A8GTS7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=A1G_06765;
OS Rickettsia rickettsii (strain Sheila Smith).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=392021;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sheila Smith;
RA Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Dasch G., Eremeeva M.;
RT "Complete genome sequence of Rickettsia rickettsii.";
RL Submitted (SEP-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; CP000848; ABV76802.1; -; Genomic_DNA.
DR RefSeq; WP_012151344.1; NC_009882.1.
DR AlphaFoldDB; A8GTS7; -.
DR SMR; A8GTS7; -.
DR EnsemblBacteria; ABV76802; ABV76802; A1G_06765.
DR GeneID; 45539714; -.
DR KEGG; rri:A1G_06765; -.
DR HOGENOM; CLU_050669_0_1_5; -.
DR OMA; MQITSAM; -.
DR Proteomes; UP000006832; 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 InterPro; IPR022436; RPE2.
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.
DR TIGRFAMs; TIGR03774; RPE2; 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..323
FT /note="ATP synthase gamma chain"
FT /id="PRO_1000053316"
SQ SEQUENCE 323 AA; 36636 MW; 27A2C0FD66497BCD CRC64;
MSNLKQLRTR IKSVKSTQKI TKAMQLVSAS KMAKIKSQIA NSNFYIEAVS KMMSAILSID
MYELSIEEQK FFNTVPNKAN LLIVMTSQRG LCGTFNYSII QQVKNDIKEL ENKGEQIKLI
IIGKKGYEAL KRQYVNYIDS YFELPKIHDE NLMLQVKQKI MSAVENLEVS NCVIYFNKFK
NAMTQIMTRQ QILPVAKYQD DSMIDNPIVN LVGFGYKERG AKPINNRSAT SDIVGESKSI
DYNYEYEGEN LISNLINLYV NSQINYALLQ SRASEEGARM TAMENATNNA NDLISKLVLK
LNRSRQAIIT TELIEIIAGS EAV
