(data stored in ACNUC7421 zone)

SWISSPROT: D1CDI3_THET1

ID   D1CDI3_THET1            Unreviewed;       179 AA.
AC   D1CDI3;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   16-JAN-2019, entry version 62.
DE   RecName: Full=ATP synthase subunit delta {ECO:0000256|HAMAP-Rule:MF_01416};
DE   AltName: Full=ATP synthase F(1) sector subunit delta {ECO:0000256|HAMAP-Rule:MF_01416};
DE   AltName: Full=F-type ATPase subunit delta {ECO:0000256|HAMAP-Rule:MF_01416};
DE            Short=F-ATPase subunit delta {ECO:0000256|HAMAP-Rule:MF_01416};
GN   Name=atpH {ECO:0000256|HAMAP-Rule:MF_01416};
GN   OrderedLocusNames=Tter_0066 {ECO:0000313|EMBL:ACZ40989.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ40989.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ40989.1, 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: F(1)F(0) ATP synthase produces ATP from ADP in the
CC       presence of a proton or sodium gradient. F-type ATPases consist of
CC       two structural domains, F(1) containing the extramembraneous
CC       catalytic core and F(0) containing the membrane proton channel,
CC       linked together by a central stalk and a peripheral stalk. During
CC       catalysis, ATP synthesis in the catalytic domain of F(1) is
CC       coupled via a rotary mechanism of the central stalk subunits to
CC       proton translocation. {ECO:0000256|HAMAP-Rule:MF_01416}.
CC   -!- FUNCTION: This protein is part of the stalk that links CF(0) to
CC       CF(1). It either transmits conformational changes from CF(0) to
CC       CF(1) or is implicated in proton conduction. {ECO:0000256|HAMAP-
CC       Rule:MF_01416}.
CC   -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic
CC       core - and F(0) - the membrane proton channel. F(1) has five
CC       subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0)
CC       has three main subunits: a(1), b(2) and c(10-14). The alpha and
CC       beta chains form an alternating ring which encloses part of the
CC       gamma chain. F(1) is attached to F(0) by a central stalk formed by
CC       the gamma and epsilon chains, while a peripheral stalk is formed
CC       by the delta and b chains. {ECO:0000256|HAMAP-Rule:MF_01416}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01416}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01416}.
CC   -!- SIMILARITY: Belongs to the ATPase delta chain family.
CC       {ECO:0000256|HAMAP-Rule:MF_01416, ECO:0000256|SAAS:SAAS01082575}.
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DR   EMBL; CP001825; ACZ40989.1; -; Genomic_DNA.
DR   STRING; 525904.Tter_0066; -.
DR   EnsemblBacteria; ACZ40989; ACZ40989; Tter_0066.
DR   KEGG; ttr:Tter_0066; -.
DR   eggNOG; ENOG4105E3N; Bacteria.
DR   eggNOG; COG0712; LUCA.
DR   HOGENOM; HOG000075825; -.
DR   KO; K02113; -.
DR   OMA; MVDNIQD; -.
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:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.520.20; -; 1.
DR   HAMAP; MF_01416; ATP_synth_delta_bact; 1.
DR   InterPro; IPR026015; ATP_synth_OSCP/delta_N_sf.
DR   InterPro; IPR020781; ATPase_OSCP/d_CS.
DR   InterPro; IPR000711; ATPase_OSCP/dsu.
DR   PANTHER; PTHR11910; PTHR11910; 1.
DR   Pfam; PF00213; OSCP; 1.
DR   PRINTS; PR00125; ATPASEDELTA.
DR   SUPFAM; SSF47928; SSF47928; 1.
DR   TIGRFAMs; TIGR01145; ATP_synt_delta; 1.
DR   PROSITE; PS00389; ATPASE_DELTA; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1CDI3.
DR   SWISS-2DPAGE; D1CDI3.
KW   ATP synthesis {ECO:0000256|HAMAP-Rule:MF_01416,
KW   ECO:0000256|SAAS:SAAS00673570};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01416};
KW   CF(1) {ECO:0000256|HAMAP-Rule:MF_01416};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
KW   Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01416,
KW   ECO:0000256|SAAS:SAAS00673590};
KW   Ion transport {ECO:0000256|HAMAP-Rule:MF_01416,
KW   ECO:0000256|SAAS:SAAS00673577};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01416,
KW   ECO:0000256|SAAS:SAAS00673593};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01416,
KW   ECO:0000256|SAAS:SAAS00673594}.
SQ   SEQUENCE   179 AA;  19869 MW;  0013989CB3402E55 CRC64;
     MPSVGSSARR YAEAIFELAQ ESGNLDAWHA DLSLLASVFS DVSALRFFKN PRKSISEKQD
     MAKRLFEGKV QPQAMYLLQM LVDRDRVEIV PAILSRFEEL LREARGIVVA EVTTAVPVDD
     NEKQQIVEQL SQITGKQIEL HTKVDPSIIG GIVVRVGDKL VDGSVATALT QLHRSLTLR
//

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