(data stored in ACNUC29543 zone)

SWISSPROT: ATPG_ACIBT

ID   ATPG_ACIBT              Reviewed;         289 AA.
AC   A3M143;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   08-MAY-2019, entry version 82.
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};
GN   OrderedLocusNames=A1S_0154;
OS   Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 /
OS   NCDC KC755 / 5377).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=400667;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX   PubMed=17344419; DOI=10.1101/gad.1510307;
RA   Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA   Gerstein M., Snyder M.;
RT   "New insights into Acinetobacter baumannii pathogenesis revealed by
RT   high-density pyrosequencing and transposon mutagenesis.";
RL   Genes Dev. 21:601-614(2007).
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. {ECO:0000255|HAMAP-Rule:MF_00815}.
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. {ECO:0000255|HAMAP-
CC       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}.
DR   EMBL; CP000521; ABO10637.2; -; Genomic_DNA.
DR   SMR; A3M143; -.
DR   EnsemblBacteria; ABO10637; ABO10637; A1S_0154.
DR   KEGG; acb:A1S_0154; -.
DR   HOGENOM; HOG000215912; -.
DR   KO; K02115; -.
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:plasma membrane ATP synthesis coupled proton transport; 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   3: Inferred from homology;
DR   PRODOM; A3M143.
DR   SWISS-2DPAGE; A3M143.
KW   ATP synthesis; Cell inner membrane; Cell membrane; CF(1);
KW   Hydrogen ion transport; Ion transport; Membrane; Transport.
FT   CHAIN         1    289       ATP synthase gamma chain.
FT                                /FTId=PRO_1000134096.
SQ   SEQUENCE   289 AA;  32096 MW;  DFCDFC58E07EDBE5 CRC64;
     MANLKEIRAK VASIKSTQKI TRAMQMVAAS KMRRAQERMA QGRPYADNMR RVIAHLVQAN
     PEYKHRYMVD RPVKRVGYII VSSDRGLAGG LNINLFKKVV QHVKAQQEQS IEVQFALIGQ
     KAVSFFKNYG GKVLGATTQI GDAPSLEQLT GSVQVMLDAF DKGELDRIYL VSNGFVNAMT
     QKPKVEQLVP LAPAEEGDDL NRTYGWDYIY EPEAEELLNG LLVRYIESMV YQGVIENVAC
     EQSARMVAMK AATDNAGQLI KDLQLIYNKL RQAAITQEIS EIVGGAAAV
//

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