ATPG_RHOCA
ID ATPG_RHOCA Reviewed; 290 AA.
AC P72246;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
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};
OS Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33303 / B10;
RX PubMed=9440534; DOI=10.1128/jb.180.2.416-421.1998;
RA Borghese R., Crimi M., Fava L., Melandri B.A.;
RT "The ATP synthase atpHAGDC (F1) operon from Rhodobacter capsulatus.";
RL J. Bacteriol. 180:416-421(1998).
RN [2]
RP PROTEIN SEQUENCE OF 2-9, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=GA;
RA Gabellini N., Gao Z., Eckerskorn C., Lottspeich F., Oesterhelt D.;
RT "Purification of the H+-ATPase from Rhodobacter capsulatus, identification
RT of the F1F0 components and reconstitution of the active enzyme.";
RL Biochim. Biophys. Acta 934:227-234(1988).
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.
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 four main
CC subunits: a, b, b' and c. {ECO:0000269|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Cellular chromatophore membrane
CC {ECO:0000269|Ref.2}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00815, ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the ATPase gamma chain family.
CC {ECO:0000255|HAMAP-Rule:MF_00815}.
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DR EMBL; X99599; CAA67909.1; -; Genomic_DNA.
DR AlphaFoldDB; P72246; -.
DR SMR; P72246; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0042717; C:plasma membrane-derived chromatophore 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 ATP synthesis; CF(1); Direct protein sequencing; Hydrogen ion transport;
KW Ion transport; Membrane; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 2..290
FT /note="ATP synthase gamma chain"
FT /id="PRO_0000073356"
SQ SEQUENCE 290 AA; 31243 MW; F4A3819A39F5075C CRC64;
MPSLKDLKNR IVSVKNTRKI TKAMQMVAAA NIRRAQESAE AARPYAERMN AVMSSLAGAV
GSTDGAPRLL AGTGSDKVHL LVIMTGERGL CGGFNANIAK LAKAKAMELL AQGKTVKILT
VGKKGRDALR RDLGQYYIDH IDLSDVKKLS YPVAQKISQN IIDRFEAGEY DVATIFFSVF
QSVISQVPTA KQVIPAQFET DAASASAVYD YEPGDQEILT ALLPRAVATA IFAALLENNA
SFNGAQMSAM DNATRNAGDM IDRLTIEYNR SRQAAITKEL IEIISGAEAL
