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ATP synthase subunit delta (ATP synthase F(1) sector subunit delta) (F-type ATPase subunit delta) (F-ATPase subunit delta)

 ATPD_THEEB              Reviewed;         185 AA.
Q8DLP4;
28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
28-FEB-2018, entry version 85.
RecName: Full=ATP synthase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
AltName: Full=ATP synthase F(1) sector subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
AltName: Full=F-type ATPase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
Short=F-ATPase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
Name=atpH {ECO:0000255|HAMAP-Rule:MF_01416};
Synonyms=atpD {ECO:0000255|HAMAP-Rule:MF_01416};
OrderedLocusNames=tlr0434;
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, 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_01416,
ECO:0000269|PubMed:18206981}.
-!- FUNCTION: This protein is part of the stalk that links CF(0) to
CF(1). It either transmits conformational changes from CF(0) to
CF(1) or is implicated in proton conduction. {ECO:0000255|HAMAP-
Rule:MF_01416}.
-!- 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). CF(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_01416, ECO:0000269|PubMed:18206981,
ECO:0000269|PubMed:20558739}.
-!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
{ECO:0000255|HAMAP-Rule:MF_01416, ECO:0000269|PubMed:18206981,
ECO:0000269|PubMed:20558739}; Peripheral membrane protein
{ECO:0000255|HAMAP-Rule:MF_01416}.
-!- MASS SPECTROMETRY: Mass=20621; Method=MALDI; Range=1-185;
Evidence={ECO:0000269|PubMed:18206981};
-!- MASS SPECTROMETRY: Mass=20507; Method=MALDI; Range=2-185; Note=May
be active form.; Evidence={ECO:0000269|PubMed:20558739};
-!- SIMILARITY: Belongs to the ATPase delta chain family.
{ECO:0000255|HAMAP-Rule:MF_01416}.
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EMBL; BA000039; BAC07986.1; -; Genomic_DNA.
RefSeq; NP_681224.1; NC_004113.1.
RefSeq; WP_011056289.1; NC_004113.1.
ProteinModelPortal; Q8DLP4; -.
SMR; Q8DLP4; -.
STRING; 197221.tlr0434; -.
EnsemblBacteria; BAC07986; BAC07986; BAC07986.
GeneID; 1012679; -.
KEGG; tel:tlr0434; -.
PATRIC; fig|197221.4.peg.458; -.
eggNOG; ENOG4105E3N; Bacteria.
eggNOG; COG0712; LUCA.
HOGENOM; HOG000075825; -.
KO; K02113; -.
OMA; MVDNIQD; -.
OrthoDB; POG091H00PI; -.
BioCyc; TELO197221:G1G3I-448-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:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
Gene3D; 1.10.520.20; -; 1.
HAMAP; MF_01416; ATP_synth_delta_bact; 1.
InterPro; IPR026015; ATP_synth_OSCP/delta_N_sf.
InterPro; IPR000711; ATPase_OSCP/dsu.
PANTHER; PTHR11910; PTHR11910; 1.
Pfam; PF00213; OSCP; 1.
PRINTS; PR00125; ATPASEDELTA.
SUPFAM; SSF47928; SSF47928; 1.
TIGRFAMs; TIGR01145; ATP_synt_delta; 1.
1: Evidence at protein level;
ATP synthesis; CF(1); Complete proteome; Hydrogen ion transport;
Ion transport; Membrane; Reference proteome; Thylakoid; Transport.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:20558739}.
CHAIN 2 185 ATP synthase subunit delta.
/FTId=PRO_1000184823.
SEQUENCE 185 AA; 20634 MW; BDF14D274514CCEA CRC64;
MMQTTVRGEV VEPYAEALLS LAQTHNLIDQ FQQDTQLMVE LVASSGELQQ FLANPLIKPE
AKKNVLRQLT VDKVHGYFLN FLMLLVDRRR INFLSSICEH YRALVRKLRN VALAEVTSAV
ELNDDQRRAV VEKVKTMTGA ADVELVTACD PELIGGVVIK VGSQIFDASL RGQLRRLSVT
LAQAT


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