ATPA_THEVB
ID ATPA_THEVB Reviewed; 503 AA.
AC Q8DLP3;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=ATP synthase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
DE EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_01346};
DE AltName: Full=ATP synthase F1 sector subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
DE AltName: Full=F-ATPase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
GN Name=atpA {ECO:0000255|HAMAP-Rule:MF_01346}; OrderedLocusNames=tlr0435;
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 alpha chain is a regulatory subunit.
CC {ECO:0000255|HAMAP-Rule:MF_01346}.
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_01346};
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:0000269|PubMed:18206981}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_01346, ECO:0000269|PubMed:18206981}; Peripheral membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_01346}.
CC -!- MASS SPECTROMETRY: Mass=54271; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18206981};
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_01346}.
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DR EMBL; BA000039; BAC07987.1; -; Genomic_DNA.
DR RefSeq; NP_681225.1; NC_004113.1.
DR RefSeq; WP_011056290.1; NC_004113.1.
DR AlphaFoldDB; Q8DLP3; -.
DR SMR; Q8DLP3; -.
DR STRING; 197221.22294156; -.
DR EnsemblBacteria; BAC07987; BAC07987; BAC07987.
DR KEGG; tel:tlr0435; -.
DR PATRIC; fig|197221.4.peg.459; -.
DR eggNOG; COG0056; Bacteria.
DR OMA; LQAPGVM; -.
DR OrthoDB; 837522at2; -.
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 CDD; cd18113; ATP-synt_F1_alpha_C; 1.
DR CDD; cd01132; F1_ATPase_alpha; 1.
DR Gene3D; 1.20.150.20; -; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01346; ATP_synth_alpha_bact; 1.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
DR InterPro; IPR000793; ATP_synth_asu_C.
DR InterPro; IPR038376; ATP_synth_asu_C_sf.
DR InterPro; IPR033732; ATP_synth_F1_a.
DR InterPro; IPR005294; ATP_synth_F1_asu.
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; IPR027417; P-loop_NTPase.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF00306; ATP-synt_ab_C; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR PIRSF; PIRSF039088; F_ATPase_subunit_alpha; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00962; atpA; 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..503
FT /note="ATP synthase subunit alpha"
FT /id="PRO_0000238376"
FT BINDING 170..177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT SITE 363
FT /note="Required for activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
SQ SEQUENCE 503 AA; 54305 MW; 927167949C4601F0 CRC64;
MVSIRPDEIS SIIRQQIEQY EQSIKVDNVG TVLQVGDGIA RVYGLDKVMA SELVEFEDGT
VGIALNLEED NVGVVLMGDG LSIEEGSTVR ATGKIASIPV GEAAIGRVVD ALMRPIDGKG
EIHTTQSRLI ESPAPGIVQR KSVCEPLQTG ITAIDAMIPI GRGQRELIIG DRQTGKTAVA
IDTILNQKGQ DVICVYVAIG QKASSVAQVV NVLRERGALD YTIVIAANAS DPAALQYLAP
YTGATVAEYF MYQGKHTLVV YDDLSKQAQA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE
RAAKLNDALG GGSMTALPVV ETQAGDVSAY IPTNVISITD GQIFLSSDLF NAGLRPAINA
GISVSRVGSA AQIKAMKQVA GKLKLELAQF DELQAFAQFA SDLDKATQNQ LARGQRLREI
LKQPQYSPIP VEYQVATIYA GTNGYLDDIP VEAVAKFVAG LRDYLRTNKP EYGEIIRTTQ
KLDEKAEALL KEAIAEYKAT FTA
