(data stored in ACNUC7421 zone)

SWISSPROT: D1CDI4_THET1

ID   D1CDI4_THET1            Unreviewed;       175 AA.
AC   D1CDI4;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   08-MAY-2019, entry version 68.
DE   RecName: Full=ATP synthase subunit b {ECO:0000256|HAMAP-Rule:MF_01398};
DE   AltName: Full=ATP synthase F(0) sector subunit b {ECO:0000256|HAMAP-Rule:MF_01398};
DE   AltName: Full=ATPase subunit I {ECO:0000256|HAMAP-Rule:MF_01398};
DE   AltName: Full=F-type ATPase subunit b {ECO:0000256|HAMAP-Rule:MF_01398};
DE            Short=F-ATPase subunit b {ECO:0000256|HAMAP-Rule:MF_01398};
GN   Name=atpF {ECO:0000256|HAMAP-Rule:MF_01398};
GN   OrderedLocusNames=Tter_0067 {ECO:0000313|EMBL:ACZ40990.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ40990.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ40990.1, 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: Component of the F(0) channel, it forms part of the
CC       peripheral stalk, linking F(1) to F(0). {ECO:0000256|HAMAP-
CC       Rule:MF_01398, ECO:0000256|SAAS:SAAS00535352}.
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_01398,
CC       ECO:0000256|SAAS:SAAS00002149}.
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_01398}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01398}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01398}.
CC   -!- SIMILARITY: Belongs to the ATPase B chain family.
CC       {ECO:0000256|HAMAP-Rule:MF_01398, ECO:0000256|RuleBase:RU003848,
CC       ECO:0000256|SAAS:SAAS00535426}.
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DR   EMBL; CP001825; ACZ40990.1; -; Genomic_DNA.
DR   RefSeq; WP_012874025.1; NC_013525.1.
DR   STRING; 525904.Tter_0067; -.
DR   EnsemblBacteria; ACZ40990; ACZ40990; Tter_0067.
DR   KEGG; ttr:Tter_0067; -.
DR   eggNOG; ENOG4108KJP; Bacteria.
DR   eggNOG; COG0711; LUCA.
DR   HOGENOM; HOG000015377; -.
DR   KO; K02109; -.
DR   OMA; KFAWKPI; -.
DR   OrthoDB; 1999641at2; -.
DR   BioCyc; TTER525904:G1GGS-67-MONOMER; -.
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   HAMAP; MF_01398; ATP_synth_b_bprime; 1.
DR   InterPro; IPR028987; ATP_synth_B-like_membr_sf.
DR   InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt.
DR   InterPro; IPR005864; ATP_synth_F0_bsu_bac.
DR   Pfam; PF00430; ATP-synt_B; 1.
DR   SUPFAM; SSF81573; SSF81573; 1.
DR   TIGRFAMs; TIGR01144; ATP_synt_b; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1CDI4.
DR   SWISS-2DPAGE; D1CDI4.
KW   ATP synthesis {ECO:0000256|HAMAP-Rule:MF_01398,
KW   ECO:0000256|SAAS:SAAS00416301};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01398,
KW   ECO:0000256|SAAS:SAAS00999632};
KW   CF(0) {ECO:0000256|HAMAP-Rule:MF_01398, ECO:0000256|RuleBase:RU003848,
KW   ECO:0000256|SAAS:SAAS00002111}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
KW   Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01398,
KW   ECO:0000256|RuleBase:RU003848, ECO:0000256|SAAS:SAAS00002281};
KW   Ion transport {ECO:0000256|HAMAP-Rule:MF_01398,
KW   ECO:0000256|RuleBase:RU003848, ECO:0000256|SAAS:SAAS00416306};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01398,
KW   ECO:0000256|SAAS:SAAS00983388};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01398,
KW   ECO:0000256|RuleBase:RU003848, ECO:0000256|SAAS:SAAS00983359};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01398,
KW   ECO:0000256|SAAS:SAAS00983391};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01398,
KW   ECO:0000256|RuleBase:RU003848, ECO:0000256|SAAS:SAAS00416370}.
FT   TRANSMEM     12     29       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01398}.
FT   COILED       48    130       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   175 AA;  19981 MW;  98BFC992DD27A21C CRC64;
     MSAVLENLGL QLWPFIWQLV AFLILVYVLK RFAFGPVTRI LDERAARVRE SIETAERIQR
     EAAEQEQRTK QMLEDARRQA QAILQQAQQA AERIQSTAQD NAREQANQII QRAQEDIDRM
     KAEAIDELRR QVADLAIAAA SRIIRKELDP ATHRALINEV LAESVDQFRG GRPVA
//

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