ATPB_THEVB
ID ATPB_THEVB Reviewed; 482 AA.
AC Q8DLG8;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=ATP synthase subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
DE EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_01347};
DE AltName: Full=ATP synthase F1 sector subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
DE AltName: Full=F-ATPase subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
GN Name=atpD {ECO:0000255|HAMAP-Rule:MF_01347};
GN Synonyms=atpB {ECO:0000255|HAMAP-Rule:MF_01347}; OrderedLocusNames=tlr0525;
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).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. The catalytic sites are hosted primarily by the
CC beta subunits. {ECO:0000255|HAMAP-Rule:MF_01347}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01347};
CC -!- ACTIVITY REGULATION: Inhibited by dicyclohexylcarbodiimide.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius, activity was detected from
CC 4 to 95 degrees Celsius.;
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(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(9-12). {ECO:0000255|HAMAP-
CC Rule:MF_01347, ECO:0000269|PubMed:18206981}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_01347, ECO:0000269|PubMed:18206981}; Peripheral membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_01347}.
CC -!- MASS SPECTROMETRY: Mass=51795; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18206981};
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_01347}.
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DR EMBL; BA000039; BAC08077.1; -; Genomic_DNA.
DR RefSeq; NP_681315.1; NC_004113.1.
DR RefSeq; WP_011056375.1; NC_004113.1.
DR AlphaFoldDB; Q8DLG8; -.
DR SMR; Q8DLG8; -.
DR STRING; 197221.22294246; -.
DR EnsemblBacteria; BAC08077; BAC08077; BAC08077.
DR KEGG; tel:tlr0525; -.
DR PATRIC; fig|197221.4.peg.553; -.
DR eggNOG; COG0055; Bacteria.
DR OMA; GFNMIMD; -.
DR OrthoDB; 430176at2; -.
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:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR Gene3D; 1.10.1140.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01347; ATP_synth_beta_bact; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR005722; ATP_synth_F1_bsu.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR024034; ATPase_F1/V1_b/a_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01039; atpD; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW ATP synthesis; ATP-binding; CF(1); Hydrogen ion transport; Ion transport;
KW Membrane; Nucleotide-binding; Reference proteome; Thylakoid; Translocase;
KW Transport.
FT CHAIN 1..482
FT /note="ATP synthase subunit beta"
FT /id="PRO_0000254404"
FT BINDING 162..169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ 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
