ID E6YJA6_BARC7 Unreviewed; 303 AA.
AC E6YJA6;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 29-MAY-2013, entry version 15.
DE RecName: Full=ATP synthase gamma chain;
DE AltName: Full=ATP synthase F1 sector gamma subunit;
DE AltName: Full=F-ATPase gamma subunit;
GN Name=atpG; OrderedLocusNames=BARCL_1272;
OS Bartonella clarridgeiae (strain CIP 104772 / 73).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=696125;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 104772 / 73;
RA Engel P., Salzburger W., Marius L., Chao-Chin C., Soichi M.,
RA Christa L., Alexandra C., Aurelie L., Claudine M., Stephan S.C.,
RA Christoph D.;
RT "Genome sequencing of Bartonella species and comparative genomics.";
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton
CC gradient across the membrane. The gamma chain is believed to be
CC important in regulating ATPase activity and the flow of protons
CC through the CF(0) complex (By similarity).
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
CC core - and CF(0) - the membrane proton channel. CF(1) has five
CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0)
CC has three main subunits: a, b and c (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane
CC protein (By similarity).
CC -!- SIMILARITY: Belongs to the ATPase gamma chain family.
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DR EMBL; FN645454; CBI76944.1; -; Genomic_DNA.
DR RefSeq; YP_004159509.1; NC_014932.1.
DR EnsemblBacteria; CBI76944; CBI76944; BARCL_1272.
DR GeneID; 10137999; -.
DR KEGG; bcd:BARCL_1272; -.
DR PATRIC; 45180059; VBIBarCla149360_1216.
DR HOGENOM; HOG000215911; -.
DR KO; K02115; -.
DR OMA; QQRGMAT; -.
DR BioCyc; BCLA696125:GC2L-1324-MONOMER; -.
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:HAMAP.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:HAMAP.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:HAMAP.
DR HAMAP; MF_00815; ATP_synth_gamma_bact; 1; -.
DR InterPro; IPR000131; ATPase_F1-cplx_gsu.
DR InterPro; IPR023632; ATPase_F1_gsu_CS.
DR InterPro; IPR023633; ATPase_F1_gsu_dom.
DR PANTHER; PTHR11693; PTHR11693; 1.
DR Pfam; PF00231; ATP-synt; 1.
DR PRINTS; PR00126; ATPASEGAMMA.
DR SUPFAM; SSF52943; ATPase_gamma; 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 Complete proteome; Hydrogen ion transport; Hydrolase; Ion transport;
KW Membrane; Transport.
SQ SEQUENCE 303 AA; 33394 MW; 1619B45B7FBC5B88 CRC64;
MASLKDLRDR IASVKATQKI TKAMQMVAAA KLHRAQEAAE SARPYAQRMA ALLARVFADI
DPVDAPPLMC GTGRDDKHLL VVCTAERGLC GAFNTQIVRH ARERINGLLS RGKTVKILTV
GKKGADILLR DFKALMVDHV DLRSVKQITF AEAEKISKCI IDLFNEGVFD VCTLFYSEFV
SVINQCPKTV NLIPVVAQKE FPDEVGGIKK EKKSRVVQSA VYDYEPDAAF LVDELVPRNL
SVQIFRALLE NVAGEMGAKM SAMDNASRNA GEMINKLTVT YNRQRQAQIT TELIEIIAGA
EAL
//
