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ATP synthase subunit b' (ATP synthase F(0) sector subunit b') (ATPase subunit II) (F-type ATPase subunit b') (F-ATPase subunit b')

 ATPX_THEEB              Reviewed;         138 AA.
Q8DLP6;
14-APR-2009, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
10-OCT-2018, entry version 82.
RecName: Full=ATP synthase subunit b' {ECO:0000255|HAMAP-Rule:MF_01399};
AltName: Full=ATP synthase F(0) sector subunit b' {ECO:0000255|HAMAP-Rule:MF_01399};
AltName: Full=ATPase subunit II {ECO:0000255|HAMAP-Rule:MF_01399};
AltName: Full=F-type ATPase subunit b' {ECO:0000255|HAMAP-Rule:MF_01399};
Short=F-ATPase subunit b' {ECO:0000255|HAMAP-Rule:MF_01399};
Name=atpG {ECO:0000255|HAMAP-Rule:MF_01399};
OrderedLocusNames=tlr0432;
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).
[3]
SUBUNIT, SUBCELLULAR LOCATION, FORMYLATION AT MET-1, AND MASS
SPECTROMETRY.
STRAIN=BP-1;
PubMed=20558739; DOI=10.1074/jbc.M110.127589;
Broser M., Gabdulkhakov A., Kern J., Guskov A., Muh F., Saenger W.,
Zouni A.;
"Crystal structure of monomeric photosystem II from
Thermosynechococcus elongatus at 3.6 A resolution.";
J. Biol. Chem. 285:26255-26262(2010).
-!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the
presence of a proton or sodium gradient. F-type ATPases consist of
two structural domains, F(1) containing the extramembraneous
catalytic core and F(0) containing the membrane proton channel,
linked together by a central stalk and a peripheral stalk. During
catalysis, ATP synthesis in the catalytic domain of F(1) is
coupled via a rotary mechanism of the central stalk subunits to
proton translocation. {ECO:0000255|HAMAP-Rule:MF_01399,
ECO:0000269|PubMed:18206981}.
-!- FUNCTION: Component of the F(0) channel, it forms part of the
peripheral stalk, linking F(1) to F(0). The b'-subunit is a
diverged and duplicated form of b found in plants and
photosynthetic bacteria. {ECO:0000255|HAMAP-Rule:MF_01399}.
-!- 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}.
-!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic
core - and F(0) - the membrane proton channel. F(1) has five
subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0)
has four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha
and beta chains form an alternating ring which encloses part of
the gamma chain. F(1) is attached to F(0) by a central stalk
formed by the gamma and epsilon chains, while a peripheral stalk
is formed by the delta, b and b' chains. {ECO:0000255|HAMAP-
Rule:MF_01399, ECO:0000269|PubMed:18206981,
ECO:0000269|PubMed:20558739}.
-!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
{ECO:0000255|HAMAP-Rule:MF_01399, ECO:0000269|PubMed:18206981,
ECO:0000269|PubMed:20558739}; Single-pass membrane protein
{ECO:0000255|HAMAP-Rule:MF_01399}.
-!- MASS SPECTROMETRY: Mass=15457; Method=MALDI; Range=1-138;
Evidence={ECO:0000269|PubMed:18206981};
-!- MASS SPECTROMETRY: Mass=15497; Method=MALDI; Range=1-138;
Evidence={ECO:0000269|PubMed:20558739};
-!- SIMILARITY: Belongs to the ATPase B chain family.
{ECO:0000255|HAMAP-Rule:MF_01399}.
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EMBL; BA000039; BAC07984.1; -; Genomic_DNA.
RefSeq; NP_681222.1; NC_004113.1.
RefSeq; WP_011056287.1; NC_004113.1.
SMR; Q8DLP6; -.
STRING; 197221.tlr0432; -.
PRIDE; Q8DLP6; -.
EnsemblBacteria; BAC07984; BAC07984; BAC07984.
GeneID; 1012674; -.
KEGG; tel:tlr0432; -.
PATRIC; fig|197221.4.peg.456; -.
eggNOG; ENOG4105S30; Bacteria.
eggNOG; COG0711; LUCA.
HOGENOM; HOG000015377; -.
KO; K02109; -.
OMA; PLMAIQF; -.
OrthoDB; POG091H029A; -.
BioCyc; TELO197221:G1G3I-446-MONOMER; -.
Proteomes; UP000000440; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
GO; GO:0042651; C:thylakoid membrane; IEA:UniProtKB-SubCell.
GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
HAMAP; MF_01398; ATP_synth_b_bprime; 1.
HAMAP; MF_01399; ATP_synth_bprime; 1.
InterPro; IPR034679; ATP_synth_b'.
InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt.
Pfam; PF00430; ATP-synt_B; 1.
1: Evidence at protein level;
ATP synthesis; CF(0); Complete proteome; Formylation;
Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
Thylakoid; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 138 ATP synthase subunit b'.
/FTId=PRO_0000369056.
TRANSMEM 6 26 Helical. {ECO:0000255|HAMAP-
Rule:MF_01399}.
MOD_RES 1 1 N-formylmethionine.
{ECO:0000269|PubMed:20558739}.
SEQUENCE 138 AA; 15467 MW; D1EEB8F8E8AAC110 CRC64;
MFDFDATLPL MAVQFLILTV ILNALLYKPL GQALDNRDEY IRTNLQQAKE RLQQATELAQ
QYEQELASTR RQAQALIEEA RVEAQKIATA EIAEAQQAVQ AELLKIQAEI DQQKQATLQA
LEGQVASLSE QLLAKLMA


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