ATPG_RICCN
ID ATPG_RICCN Reviewed; 323 AA.
AC Q92G87;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=RC1236;
OS Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=272944;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-613 / Malish 7;
RX PubMed=11557893; DOI=10.1126/science.1061471;
RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL Science 293:2093-2098(2001).
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; AE006914; AAL03774.1; -; Genomic_DNA.
DR PIR; D97854; D97854.
DR RefSeq; WP_010977801.1; NC_003103.1.
DR AlphaFoldDB; Q92G87; -.
DR SMR; Q92G87; -.
DR EnsemblBacteria; AAL03774; AAL03774; RC1236.
DR KEGG; rco:RC1236; -.
DR PATRIC; fig|272944.4.peg.1417; -.
DR HOGENOM; CLU_050669_0_1_5; -.
DR OMA; MQITSAM; -.
DR Proteomes; UP000000816; 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_0000244532"
FT REGION 206..240
FT /note="Insert"
SQ SEQUENCE 323 AA; 36735 MW; C953AFB0A986AC7C CRC64;
MSNLKQLRTR IKSVKSTQKI TKAMQLVSAS KMAKIKSQIA NSNFYIEAVS KMMSAILSID
MYELSIEEQK FFNTVPNKAN LLIVMTSQRG LCGTFNYSII KQVKNDIKEL ENKGEQIKLI
IIGKKGYEAL KRQYVNYIDS YFELPKIHDE NLMLQVKQKI MSAVENLEVS NCVIYFNKFK
NAMTQIMTRQ QILPVAKYQD DSMIDNPIVN LVGFGYKERG VKPINNRRAT SDIVGESKSI
DYNYEYEGES LISNLINLYV NSQINYALLQ SRASEEGARM TAMENATNNA NDLISKLVLK
LNRSRQAIIT TELIEIIAGS EVV
