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ATP synthase subunit beta (EC 3.6.3.14) (ATP synthase F1 sector subunit beta) (F-ATPase subunit beta)

 ATPB_THEEB              Reviewed;         482 AA.
Q8DLG8;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
28-FEB-2018, entry version 109.
RecName: Full=ATP synthase subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
EC=3.6.3.14 {ECO:0000255|HAMAP-Rule:MF_01347};
AltName: Full=ATP synthase F1 sector subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
AltName: Full=F-ATPase subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
Name=atpD {ECO:0000255|HAMAP-Rule:MF_01347};
Synonyms=atpB {ECO:0000255|HAMAP-Rule:MF_01347};
OrderedLocusNames=tlr0525;
Thermosynechococcus elongatus (strain BP-1).
Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
Thermosynechococcus.
NCBI_TaxID=197221;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=BP-1;
PubMed=12240834; DOI=10.1093/dnares/9.4.123;
Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N.,
Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.;
"Complete genome structure of the thermophilic cyanobacterium
Thermosynechococcus elongatus BP-1.";
DNA Res. 9:123-130(2002).
[2]
FUNCTION, MASS SPECTROMETRY, SUBUNIT, AND SUBCELLULAR LOCATION.
STRAIN=BP-1;
PubMed=18206981; DOI=10.1016/j.bbamem.2007.12.017;
Suhai T., Dencher N.A., Poetsch A., Seelert H.;
"Remarkable stability of the proton translocating F1FO-ATP synthase
from the thermophilic cyanobacterium Thermosynechococcus elongatus BP-
1.";
Biochim. Biophys. Acta 1778:1131-1140(2008).
-!- FUNCTION: Produces ATP from ADP in the presence of a proton
gradient across the membrane. The catalytic sites are hosted
primarily by the beta subunits. {ECO:0000255|HAMAP-Rule:MF_01347}.
-!- FUNCTION: The complex from the organism is particularly stable to
disruption and remains functional after 6 hrs at 55 degrees
Celsius. {ECO:0000269|PubMed:18206981}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate +
H(+)(Out). {ECO:0000255|HAMAP-Rule:MF_01347}.
-!- ENZYME REGULATION: Inhibited by dicyclohexylcarbodiimide.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Temperature dependence:
Optimum temperature is 55 degrees Celsius, activity was detected
from 4 to 95 degrees Celsius.;
-!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
core - and CF(0) - the membrane proton channel. CF(1) has five
subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0)
has four main subunits: a(1), b(1), b'(1) and c(9-12).
{ECO:0000255|HAMAP-Rule:MF_01347, ECO:0000269|PubMed:18206981}.
-!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
{ECO:0000255|HAMAP-Rule:MF_01347, ECO:0000269|PubMed:18206981};
Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01347}.
-!- MASS SPECTROMETRY: Mass=51795; Method=MALDI; Range=1-482;
Evidence={ECO:0000269|PubMed:18206981};
-!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
{ECO:0000255|HAMAP-Rule:MF_01347}.
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EMBL; BA000039; BAC08077.1; -; Genomic_DNA.
RefSeq; NP_681315.1; NC_004113.1.
RefSeq; WP_011056375.1; NC_004113.1.
ProteinModelPortal; Q8DLG8; -.
SMR; Q8DLG8; -.
STRING; 197221.tlr0525; -.
PRIDE; Q8DLG8; -.
EnsemblBacteria; BAC08077; BAC08077; BAC08077.
GeneID; 1012192; -.
KEGG; tel:tlr0525; -.
PATRIC; fig|197221.4.peg.553; -.
eggNOG; ENOG4105C4J; Bacteria.
eggNOG; COG0055; LUCA.
HOGENOM; HOG000009605; -.
KO; K02112; -.
OMA; FNMIMDG; -.
OrthoDB; POG091H014C; -.
BioCyc; TELO197221:G1G3I-539-MONOMER; -.
Proteomes; UP000000440; Chromosome.
GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
GO; GO:0042651; C:thylakoid membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
Gene3D; 1.10.1140.10; -; 1.
HAMAP; MF_01347; ATP_synth_beta_bact; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR005722; ATP_synth_F1_bsu.
InterPro; IPR020003; ATPase_a/bsu_AS.
InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
InterPro; IPR024034; ATPase_F1/V1_b/a_C.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00006; ATP-synt_ab; 1.
Pfam; PF02874; ATP-synt_ab_N; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF50615; SSF50615; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR01039; atpD; 1.
PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
1: Evidence at protein level;
ATP synthesis; ATP-binding; CF(1); Complete proteome;
Hydrogen ion transport; Hydrolase; Ion transport; Membrane;
Nucleotide-binding; Reference proteome; Thylakoid; Transport.
CHAIN 1 482 ATP synthase subunit beta.
/FTId=PRO_0000254404.
NP_BIND 162 169 ATP. {ECO:0000255|HAMAP-Rule:MF_01347}.
SEQUENCE 482 AA; 51756 MW; 3957723201BFA67F CRC64;
MVISAERTNV GFITQVIGPV VDIEFPSGKM PAIYNALRIQ GKNAAGLDVA VTCEVQQLLG
DNRVRAVAMS STDGLVRGME VVDTGAPISV PVGTATLGRI FNVLGEPVDE KGAVNATETL
PIHRPAPSFT QLETKPSVFE TGIKVIDLLT PYRRGGKIGL FGGAGVGKTV IMMELINNIA
TQHGGVSVFA GVGERTREGN DLYNEMIESG VIDKDDPSKS KIALVYGQMN EPPGARMRVG
LSGLTMAEYF RDVNKQDVLL FIDNIFRFVQ AGSEVSALLG RMPSAVGYQP TLGTDVGALQ
ERITSTTEGS ITSIQAVYVP ADDLTDPAPA TTFAHLDGTT VLSRSLAAKG IYPAVDPLGS
TSNMLQPDIV GEEHYQTARA VQATLQRYKE LQDIIAILGL DELSEEDRLT VARARKIERF
LSQPFFVAEV FTGAPGKYVT LEETIKGFQM ILSGELDDLP EQAFYMVGNI EEAKAKAEKL
KA


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