(data stored in ACNUC7421 zone)

SWISSPROT: D1CDI2_THET1

ID   D1CDI2_THET1            Unreviewed;       508 AA.
AC   D1CDI2;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   16-JAN-2019, entry version 68.
DE   RecName: Full=ATP synthase subunit alpha {ECO:0000256|HAMAP-Rule:MF_01346};
DE            EC=7.1.2.2 {ECO:0000256|HAMAP-Rule:MF_01346};
DE   AltName: Full=ATP synthase F1 sector subunit alpha {ECO:0000256|HAMAP-Rule:MF_01346};
DE   AltName: Full=F-ATPase subunit alpha {ECO:0000256|HAMAP-Rule:MF_01346};
GN   Name=atpA {ECO:0000256|HAMAP-Rule:MF_01346};
GN   OrderedLocusNames=Tter_0065 {ECO:0000313|EMBL:ACZ40988.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ40988.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ40988.1, 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 alpha chain is a regulatory
CC       subunit. {ECO:0000256|HAMAP-Rule:MF_01346}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC         Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         EC=7.1.2.2; Evidence={ECO:0000256|HAMAP-Rule:MF_01346};
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(1), b(2) and c(9-12). The alpha and
CC       beta chains form an alternating ring which encloses part of the
CC       gamma chain. CF(1) is attached to CF(0) by a central stalk formed
CC       by the gamma and epsilon chains, while a peripheral stalk is
CC       formed by the delta and b chains. {ECO:0000256|HAMAP-
CC       Rule:MF_01346}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01346}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01346}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|HAMAP-Rule:MF_01346}.
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DR   EMBL; CP001825; ACZ40988.1; -; Genomic_DNA.
DR   RefSeq; WP_012874023.1; NC_013525.1.
DR   STRING; 525904.Tter_0065; -.
DR   EnsemblBacteria; ACZ40988; ACZ40988; Tter_0065.
DR   KEGG; ttr:Tter_0065; -.
DR   eggNOG; ENOG4105CDG; Bacteria.
DR   eggNOG; COG0056; LUCA.
DR   HOGENOM; HOG000130111; -.
DR   KO; K02111; -.
DR   OMA; GNAQIKS; -.
DR   OrthoDB; 837522at2; -.
DR   BioCyc; TTER525904:G1GGS-65-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:0015986; P:ATP synthesis coupled proton transport; IEA:UniProtKB-UniRule.
DR   CDD; cd01132; F1_ATPase_alpha; 1.
DR   Gene3D; 1.20.150.20; -; 1.
DR   Gene3D; 2.40.30.20; -; 1.
DR   HAMAP; MF_01346; ATP_synth_alpha_bact; 1.
DR   InterPro; IPR023366; ATP_synth_asu-like_sf.
DR   InterPro; IPR000793; ATP_synth_asu_C.
DR   InterPro; IPR038376; ATP_synth_asu_C_sf.
DR   InterPro; IPR033732; ATP_synth_F1_a.
DR   InterPro; IPR005294; ATP_synth_F1_asu.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR   InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF00306; ATP-synt_ab_C; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   PIRSF; PIRSF039088; F_ATPase_subunit_alpha; 1.
DR   SUPFAM; SSF50615; SSF50615; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00962; atpA; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1CDI2.
DR   SWISS-2DPAGE; D1CDI2.
KW   ATP synthesis {ECO:0000256|HAMAP-Rule:MF_01346};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01346};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01346};
KW   CF(1) {ECO:0000256|HAMAP-Rule:MF_01346};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
KW   Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01346};
KW   Hydrolase {ECO:0000313|EMBL:ACZ40988.1};
KW   Ion transport {ECO:0000256|HAMAP-Rule:MF_01346};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01346};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01346};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323};
KW   Translocase {ECO:0000256|HAMAP-Rule:MF_01346};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01346}.
FT   DOMAIN       24     92       ATP-synt_ab_N. {ECO:0000259|Pfam:
FT                                PF02874}.
FT   DOMAIN      149    364       ATP-synt_ab. {ECO:0000259|Pfam:PF00006}.
FT   DOMAIN      371    496       ATP-synt_ab_C. {ECO:0000259|Pfam:
FT                                PF00306}.
FT   NP_BIND     169    176       ATP. {ECO:0000256|HAMAP-Rule:MF_01346}.
FT   COILED      475    495       {ECO:0000256|SAM:Coils}.
FT   SITE        362    362       Required for activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_01346}.
SQ   SEQUENCE   508 AA;  55181 MW;  7FBE76C0013B4C13 CRC64;
     MAIKTEEIAE IIKKQIESFG QPVVTAEVGT VVEVGDGIAR AYGLSGVKAS ELVQFENGVY
     GLALNLEEDN VGIVILGPYT DIEEGQQVRS TGRVVDVPVG DELIGRVVNP LGEPIDGKGP
     INATKRRVIE RIAPGVVARK SVDTPVQTGI KAIDSMIPIG RGQRELIIGD RQTGKSAIAI
     DTIINQKGKD LICIYVAIGQ KTSKVAQVVA TLEEYGAMEH TIVVAANADD PASLQYIAPY
     AGCAMGEEFM EQGRDALVVY DDLSKHAAAY REISLLLRRP PGREAYPGDV FYLHSRLLER
     AARLNDEYGG GSLTALPIIE TQANDVSAYI PTNVISITDG QIYLESDLFY AGIRPAINVG
     LSVSRVGGAA QTKAMRQVAG KLRLDLAQFR SLAAFAQFGS DLDKATRAQL ERGQRLTEVL
     KQPQYSPVPL ERQVMIIFAA TNGYLDDIPV DSVRDFENRF YEYMDSVHPE IGQEIADKKA
     LSDELTEKLR AAIEEFKQGY TPQQSAPA
//

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