ATPD_THEVB
ID ATPD_THEVB Reviewed; 185 AA.
AC Q8DLP4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=ATP synthase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
DE AltName: Full=ATP synthase F(1) sector subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
DE AltName: Full=F-type ATPase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
DE Short=F-ATPase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
GN Name=atpH {ECO:0000255|HAMAP-Rule:MF_01416};
GN Synonyms=atpD {ECO:0000255|HAMAP-Rule:MF_01416}; OrderedLocusNames=tlr0434;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
RN [2]
RP FUNCTION, MASS SPECTROMETRY, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=18206981; DOI=10.1016/j.bbamem.2007.12.017;
RA Suhai T., Dencher N.A., Poetsch A., Seelert H.;
RT "Remarkable stability of the proton translocating F1FO-ATP synthase from
RT the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1.";
RL Biochim. Biophys. Acta 1778:1131-1140(2008).
RN [3]
RP SUBUNIT, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=20558739; DOI=10.1074/jbc.m110.127589;
RA Broser M., Gabdulkhakov A., Kern J., Guskov A., Muh F., Saenger W.,
RA Zouni A.;
RT "Crystal structure of monomeric photosystem II from Thermosynechococcus
RT elongatus at 3.6 A resolution.";
RL J. Biol. Chem. 285:26255-26262(2010).
CC -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence
CC of a proton or sodium gradient. F-type ATPases consist of two
CC structural domains, F(1) containing the extramembraneous catalytic core
CC and F(0) containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation. {ECO:0000255|HAMAP-
CC Rule:MF_01416, ECO:0000269|PubMed:18206981}.
CC -!- FUNCTION: This protein is part of the stalk that links CF(0) to CF(1).
CC It either transmits conformational changes from CF(0) to CF(1) or is
CC implicated in proton conduction. {ECO:0000255|HAMAP-Rule:MF_01416}.
CC -!- FUNCTION: The complex from the organism is particularly stable to
CC disruption and remains functional after 6 hrs at 55 degrees Celsius.
CC {ECO:0000269|PubMed:18206981}.
CC -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core
CC - and F(0) - the membrane proton channel. F(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main
CC subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains
CC form an alternating ring which encloses part of the gamma chain. F(1)
CC is attached to F(0) by a central stalk formed by the gamma and epsilon
CC chains, while a peripheral stalk is formed by the delta, b and b'
CC chains. {ECO:0000255|HAMAP-Rule:MF_01416, ECO:0000269|PubMed:18206981,
CC ECO:0000269|PubMed:20558739}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_01416, ECO:0000269|PubMed:18206981,
CC ECO:0000269|PubMed:20558739}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01416}.
CC -!- MASS SPECTROMETRY: Mass=20621; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18206981};
CC -!- MASS SPECTROMETRY: Mass=20507; Method=MALDI; Note=May be active form.;
CC Evidence={ECO:0000269|PubMed:20558739};
CC -!- SIMILARITY: Belongs to the ATPase delta chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01416}.
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DR EMBL; BA000039; BAC07986.1; -; Genomic_DNA.
DR RefSeq; NP_681224.1; NC_004113.1.
DR RefSeq; WP_011056289.1; NC_004113.1.
DR AlphaFoldDB; Q8DLP4; -.
DR SMR; Q8DLP4; -.
DR STRING; 197221.22294155; -.
DR EnsemblBacteria; BAC07986; BAC07986; BAC07986.
DR KEGG; tel:tlr0434; -.
DR PATRIC; fig|197221.4.peg.458; -.
DR eggNOG; COG0712; Bacteria.
DR OMA; MVDNIQD; -.
DR OrthoDB; 1937493at2; -.
DR Proteomes; UP000000440; Chromosome.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.520.20; -; 1.
DR HAMAP; MF_01416; ATP_synth_delta_bact; 1.
DR InterPro; IPR026015; ATP_synth_OSCP/delta_N_sf.
DR InterPro; IPR000711; ATPase_OSCP/dsu.
DR PANTHER; PTHR11910; PTHR11910; 1.
DR Pfam; PF00213; OSCP; 1.
DR PRINTS; PR00125; ATPASEDELTA.
DR SUPFAM; SSF47928; SSF47928; 1.
DR TIGRFAMs; TIGR01145; ATP_synt_delta; 1.
PE 1: Evidence at protein level;
KW ATP synthesis; CF(1); Hydrogen ion transport; Ion transport; Membrane;
KW Reference proteome; Thylakoid; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:20558739"
FT CHAIN 2..185
FT /note="ATP synthase subunit delta"
FT /id="PRO_1000184823"
SQ 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
