(data stored in SCRATCH zone)

SWISSPROT: D1CDI1_THET1

ID   D1CDI1_THET1            Unreviewed;       291 AA.
AC   D1CDI1;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   16-JAN-2019, entry version 57.
DE   RecName: Full=ATP synthase gamma chain {ECO:0000256|HAMAP-Rule:MF_00815};
DE   AltName: Full=ATP synthase F1 sector gamma subunit {ECO:0000256|HAMAP-Rule:MF_00815};
DE   AltName: Full=F-ATPase gamma subunit {ECO:0000256|HAMAP-Rule:MF_00815};
GN   Name=atpG {ECO:0000256|HAMAP-Rule:MF_00815};
GN   OrderedLocusNames=Tter_0064 {ECO:0000313|EMBL:ACZ40987.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ40987.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ40987.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Lu M., Brettin T.,
RA   Detter J.C., Goker M., Tindall B.J., Beck B., McDermott T.R.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain
RT   (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA   Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain
RT   (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
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:0000256|HAMAP-Rule:MF_00815,
CC       ECO:0000256|SAAS:SAAS00725627}.
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:0000256|HAMAP-
CC       Rule:MF_00815, ECO:0000256|SAAS:SAAS00725628}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00815}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00815}.
CC   -!- SIMILARITY: Belongs to the ATPase gamma chain family.
CC       {ECO:0000256|HAMAP-Rule:MF_00815, ECO:0000256|SAAS:SAAS00725641}.
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DR   EMBL; CP001825; ACZ40987.1; -; Genomic_DNA.
DR   RefSeq; WP_012874022.1; NC_013525.1.
DR   STRING; 525904.Tter_0064; -.
DR   EnsemblBacteria; ACZ40987; ACZ40987; Tter_0064.
DR   KEGG; ttr:Tter_0064; -.
DR   eggNOG; ENOG4105J80; Bacteria.
DR   eggNOG; COG0224; LUCA.
DR   HOGENOM; HOG000215912; -.
DR   KO; K02115; -.
DR   OMA; DRGMCGG; -.
DR   OrthoDB; 1701531at2; -.
DR   BioCyc; TTER525904:G1GGS-64-MONOMER; -.
DR   Proteomes; UP000000323; Chromosome 1.
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; D1CDI1.
DR   SWISS-2DPAGE; D1CDI1.
KW   ATP synthesis {ECO:0000256|HAMAP-Rule:MF_00815,
KW   ECO:0000256|SAAS:SAAS00725616};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00815};
KW   CF(1) {ECO:0000256|HAMAP-Rule:MF_00815,
KW   ECO:0000256|SAAS:SAAS00725624}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
KW   Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_00815,
KW   ECO:0000256|SAAS:SAAS00725646};
KW   Hydrolase {ECO:0000313|EMBL:ACZ40987.1};
KW   Ion transport {ECO:0000256|HAMAP-Rule:MF_00815,
KW   ECO:0000256|SAAS:SAAS00725612};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00815,
KW   ECO:0000256|SAAS:SAAS00725655};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_00815,
KW   ECO:0000256|SAAS:SAAS00725652}.
FT   COILED      253    273       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   291 AA;  32706 MW;  05E3703ECD383C58 CRC64;
     MPSTREIRRR IRSIRNTAQI TRAMEMVAAS RMRRAQQAVT ASRPFSEKIR HVLADLGAST
     GGGDSVMHPL LERRPENRVT LILMTSDRGL AGSFNTNIIR TAINFMLDRQ DQQVSVIAVG
     RKGRDYMVRR RRDLKAEFSN IGDLPGLDAI TPVAHMIIDE FTSGQTDAVY LAYTEYITTL
     NQRPTLLKIL PIEPPEVEEG RETKVPDYIF EPNPAMLLRA LLPRYVEVQL YQALLESKAS
     EHSARMVAMR NATDNANELV EELTLTYNKL RQANITKEII EIASGAAALE G
//

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