Entry sw:ATPG_STRSA

ID   ATPG_STRSA              Reviewed;         293 AA.
AC   Q9ZJ02;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   30-NOV-2016, entry version 66.
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   Streptococcus sanguinis.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=10904;
RX   PubMed=12591869; DOI=10.1128/JB.185.5.1525-1533.2003;
RA   Kuhnert W.L., Quivey R.G. Jr.;
RT   "Genetic and biochemical characterization of the F-ATPase operon from
RT   Streptococcus sanguis 10904.";
RL   J. Bacteriol. 185:1525-1533(2003).
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 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; AF001955; AAD00917.1; -; Genomic_DNA.
DR   RefSeq; WP_002895995.1; NZ_LAYH01000003.1.
DR   ProteinModelPortal; Q9ZJ02; -.
DR   STRING; 388919.SSA_0787; -.
DR   eggNOG; ENOG4105J80; Bacteria.
DR   eggNOG; COG0224; LUCA.
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-HAMAP.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-HAMAP.
DR   GO; GO:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:UniProtKB-HAMAP.
DR   CDD; cd12151; F1-ATPase_gamma; 1.
DR   HAMAP; MF_00815; ATP_synth_gamma_bact; 1.
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;
KW   ATP synthesis; Cell membrane; CF(1); Hydrogen ion transport;
KW   Ion transport; Membrane; Transport.
FT   CHAIN         1    293       ATP synthase gamma chain.
FT                                /FTId=PRO_0000073394.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT         4    292       ipfam:ATP-synt [T]
FT   MYHIT         2    292       ihamap:ATP_synth_gamma_bact [T]
FT   MYHIT       278    291       ipat:ATPASE_GAMMA [T]
SQ   SEQUENCE   293 AA;  32541 MW;  546D2F7A86898485 CRC64;
     MAVSLNDIKN KIASTKNTSQ ITNAMQMVSA AKLGKSEEAA KNFQVYAQKV RKLVTDMLHG
     HEAENARHHS MLISRPVKKS AYIVITSDRG LVGGYNATIL KALMELKAEY HPTGEDFEVI
     CIGSVGADFF RARGIQPVYE LRGLADQPSF DEVRKIISKT IEMYQNELFD ELYVCYNHHV
     NSLTSQMRVE QMLPIIDLDP NEADEDYTLN LELESSRDSI LDQLLPQFAE SMIYGAIIDA
     KTAENAAGMT AMQTATDNAK KVISDLTIQY NRARQAAITQ EITEIVAGAS ALE
//