(data stored in SCRATCH zone)

SWISSPROT: D1CDI6_THET1

ID   D1CDI6_THET1            Unreviewed;       284 AA.
AC   D1CDI6;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   16-JAN-2019, entry version 60.
DE   RecName: Full=ATP synthase subunit a {ECO:0000256|HAMAP-Rule:MF_01393, ECO:0000256|RuleBase:RU000483};
DE   AltName: Full=ATP synthase F0 sector subunit a {ECO:0000256|HAMAP-Rule:MF_01393};
DE   AltName: Full=F-ATPase subunit 6 {ECO:0000256|HAMAP-Rule:MF_01393};
GN   Name=atpB {ECO:0000256|HAMAP-Rule:MF_01393};
GN   OrderedLocusNames=Tter_0069 {ECO:0000313|EMBL:ACZ40992.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ40992.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ40992.1, 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: Key component of the proton channel; it plays a direct
CC       role in the translocation of protons across the membrane.
CC       {ECO:0000256|HAMAP-Rule:MF_01393, ECO:0000256|RuleBase:RU000483}.
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_01393}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01393, ECO:0000256|RuleBase:RU000483}; Multi-pass membrane
CC       protein {ECO:0000256|HAMAP-Rule:MF_01393,
CC       ECO:0000256|RuleBase:RU000483}.
CC   -!- SIMILARITY: Belongs to the ATPase A chain family.
CC       {ECO:0000256|HAMAP-Rule:MF_01393, ECO:0000256|RuleBase:RU000483}.
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DR   EMBL; CP001825; ACZ40992.1; -; Genomic_DNA.
DR   STRING; 525904.Tter_0069; -.
DR   EnsemblBacteria; ACZ40992; ACZ40992; Tter_0069.
DR   KEGG; ttr:Tter_0069; -.
DR   eggNOG; ENOG4105EE4; Bacteria.
DR   eggNOG; COG0356; LUCA.
DR   HOGENOM; HOG000275409; -.
DR   KO; K02108; -.
DR   OMA; QVFLTSW; -.
DR   Proteomes; UP000000323; Chromosome 1.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); 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; 1.20.120.220; -; 1.
DR   HAMAP; MF_01393; ATP_synth_a_bact; 1.
DR   InterPro; IPR000568; ATP_synth_F0_asu.
DR   InterPro; IPR023011; ATP_synth_F0_asu_AS.
DR   InterPro; IPR035908; F0_ATP_A_sf.
DR   Pfam; PF00119; ATP-synt_A; 1.
DR   PRINTS; PR00123; ATPASEA.
DR   SUPFAM; SSF81336; SSF81336; 1.
DR   TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1.
DR   PROSITE; PS00449; ATPASE_A; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1CDI6.
DR   SWISS-2DPAGE; D1CDI6.
KW   ATP synthesis {ECO:0000256|HAMAP-Rule:MF_01393};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01393};
KW   CF(0) {ECO:0000256|HAMAP-Rule:MF_01393,
KW   ECO:0000256|RuleBase:RU000483};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
KW   Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01393,
KW   ECO:0000256|RuleBase:RU000483};
KW   Ion transport {ECO:0000256|HAMAP-Rule:MF_01393,
KW   ECO:0000256|RuleBase:RU000483};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01393};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01393,
KW   ECO:0000256|RuleBase:RU000483};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01393};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01393,
KW   ECO:0000256|RuleBase:RU000483}.
FT   TRANSMEM     53     72       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01393}.
FT   TRANSMEM    116    138       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01393}.
FT   TRANSMEM    158    179       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01393}.
FT   TRANSMEM    214    239       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01393}.
FT   TRANSMEM    245    267       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01393}.
SQ   SEQUENCE   284 AA;  30306 MW;  BBD09E3384EB1BD9 CRC64;
     MPLMLAEQRV GGLARILAQE EEHGKGLLGT PFHQPTLAPE TLFHIGPIPV TNSMLMTLIV
     VVALSIAAIW LSRGLSLVPS KRQNFLEAIV ELLDNLVQTT AGRTAGRAIL PLIGTLFIYI
     LVANWASLLP GVGTITWHTE HGDVPLLRAP NADLNMTLAM AIVTIVVVQI AGVAAHGVGG
     HFKEYLNPMH LIDELARVIS LSVRLFANVF GGEVLLTVML ALSFLGAIAI IPVVIPMAFM
     GLEMFIGLIQ ALVFSLLSLI YITLAVAGHG HPADAEDAES ATHH
//

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