ATPA_BACP3
ID ATPA_BACP3 Reviewed; 502 AA.
AC P09219;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 157.
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};
OS Bacillus sp. (strain PS3).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2334;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-42; 106-121 AND
RP 164-174, AND SUBUNIT.
RX PubMed=2894854; DOI=10.1016/0005-2728(88)90064-3;
RA Ohta S., Yohda M., Ishizuka M., Hirata H., Hamamoto T.,
RA Otawara-Hamamoto Y., Matsuda K., Kagawa Y.;
RT "Sequence and over-expression of subunits of adenosine triphosphate
RT synthase in thermophilic bacterium PS3.";
RL Biochim. Biophys. Acta 933:141-155(1988).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
RX PubMed=9261073; DOI=10.1016/s0969-2126(97)00236-0;
RA Shirakihara Y., Leslie A.G.W., Abrahams J.P., Walker J.E., Ueda T.,
RA Seikimoto Y., Kambara M., Saika K., Kagawa Y., Yoshida M.;
RT "The crystal structure of the nucleotide-free alpha 3 beta 3 subcomplex of
RT F1-ATPase from the thermophilic Bacillus PS3 is a symmetric trimer.";
RL Structure 5:825-836(1997).
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 -!- 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 -!- 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 three main
CC subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an
CC alternating ring which encloses part of the gamma chain. CF(1) is
CC attached to CF(0) by a central stalk formed by the gamma and epsilon
CC chains, while a peripheral stalk is formed by the delta and b chains.
CC {ECO:0000255|HAMAP-Rule:MF_01346, ECO:0000269|PubMed:2894854}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01346};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01346}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_01346}.
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DR EMBL; X07804; CAA30652.1; -; Genomic_DNA.
DR PDB; 1SKY; X-ray; 3.20 A; B=1-502.
DR PDBsum; 1SKY; -.
DR AlphaFoldDB; P09219; -.
DR BMRB; P09219; -.
DR SMR; P09219; -.
DR DIP; DIP-6214N; -.
DR IntAct; P09219; 1.
DR MINT; P09219; -.
DR ChEMBL; CHEMBL3308987; -.
DR TCDB; 3.A.2.1.14; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR PRIDE; P09219; -.
DR SABIO-RK; P09219; -.
DR EvolutionaryTrace; P09219; -.
DR GO; GO:0005886; C:plasma 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 3D-structure; ATP synthesis; ATP-binding; Cell membrane; CF(1);
KW Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane;
KW Nucleotide-binding; Translocase; Transport.
FT CHAIN 1..502
FT /note="ATP synthase subunit alpha"
FT /id="PRO_0000144316"
FT BINDING 169..176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT SITE 362
FT /note="Required for activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 87..98
FT /evidence="ECO:0007829|PDB:1SKY"
FT TURN 102..105
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 151..156
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 175..184
FT /evidence="ECO:0007829|PDB:1SKY"
FT TURN 185..190
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 192..199
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 202..214
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 220..226
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 232..250
FT /evidence="ECO:0007829|PDB:1SKY"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 255..261
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 263..276
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 290..298
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 312..320
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 329..335
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 338..344
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 346..352
FT /evidence="ECO:0007829|PDB:1SKY"
FT TURN 359..361
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 373..392
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 404..420
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 430..439
FT /evidence="ECO:0007829|PDB:1SKY"
FT TURN 440..447
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 450..452
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 453..466
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 467..470
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 472..478
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 483..497
FT /evidence="ECO:0007829|PDB:1SKY"
SQ SEQUENCE 502 AA; 54591 MW; 19B2721AD8CF8661 CRC64;
MSIRAEEISA LIKQQIENYE SQIQVSDVGT VIQVGDGIAR AHGLDNVMSG EAVEFANAVM
GMALNLEENN VGIVILGPYT GIKEGDEVRR TGRIMEVPVG ETLIGRVVNP LGQPVDGLGP
VETTETRPIE SRAPGVMDRR SVHEPLQTGI KAIDALVPIG RGQRELIIGD RQTGKTSVAI
DTIINQKDQN MICIYVAIGQ KESTVATVVE TLAKHGAPDY TIVVTASASQ PAPLLFLAPY
AGVAMGEYFM IMGKHVLVVI DDLSKQAAAY RQLSLLLRRP PGREAYPGDI FYLHSRLLER
AAKLSDAKGG GSLTALPFVE TQAGDISAYI PTNVISITDG QIFLQSDLFF SGVRPAINAG
LSVSRVGGAA QIKAMKKVAG TLRLDLAAYR ELEAFAQFGS DLDKATQANV ARGARTVEVL
KQDLHQPIPV EKQVLIIYAL TRGFLDDIPV EDVRRFEKEF YLWLDQNGQH LLEHIRTTKD
LPNEDDLNQA IEAFKKTFVV SQ
