ATPB_BACP3
ID ATPB_BACP3 Reviewed; 473 AA.
AC P07677;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 147.
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};
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 1-19, AND SUBUNIT.
RX PubMed=2880841; DOI=10.1093/oxfordjournals.jbchem.a121805;
RA Kagawa Y., Ishizuka M., Saishu T., Nakao S.;
RT "Stable structure of thermophilic proton ATPase beta subunit.";
RL J. Biochem. 100:923-934(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [3]
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 catalytic sites are hosted primarily by the
CC beta subunits. {ECO:0000255|HAMAP-Rule:MF_01347}.
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 -!- 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_01347, ECO:0000269|PubMed:2880841}.
CC -!- INTERACTION:
CC P07677; P09222: atpG; NbExp=2; IntAct=EBI-8612954, EBI-15654225;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01347};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01347}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_01347}.
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DR EMBL; D00113; BAA00066.1; -; Genomic_DNA.
DR EMBL; X04609; CAA28277.1; -; Genomic_DNA.
DR EMBL; X07804; CAA30655.1; -; Genomic_DNA.
DR PDB; 1SKY; X-ray; 3.20 A; E=1-473.
DR PDB; 7L1Q; EM; 3.40 A; D/E/F=1-473.
DR PDB; 7L1R; EM; 3.10 A; D/E/F=1-473.
DR PDB; 7L1S; EM; 3.60 A; D/E/F=1-473.
DR PDBsum; 1SKY; -.
DR PDBsum; 7L1Q; -.
DR PDBsum; 7L1R; -.
DR PDBsum; 7L1S; -.
DR AlphaFoldDB; P07677; -.
DR BMRB; P07677; -.
DR SMR; P07677; -.
DR DIP; DIP-6215N; -.
DR IntAct; P07677; 2.
DR MINT; P07677; -.
DR ChEMBL; CHEMBL3308988; -.
DR TCDB; 3.A.2.1.14; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR SABIO-RK; P07677; -.
DR EvolutionaryTrace; P07677; -.
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 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 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..473
FT /note="ATP synthase subunit beta"
FT /id="PRO_0000144422"
FT BINDING 158..165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 44..55
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 140..145
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 164..178
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 183..190
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 192..204
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 222..242
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 246..252
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 255..268
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 281..289
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 299..305
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 316..322
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 326..331
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 335..338
FT /evidence="ECO:0007829|PDB:1SKY"
FT TURN 346..348
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 356..387
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 395..409
FT /evidence="ECO:0007829|PDB:1SKY"
FT TURN 415..417
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 418..421
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 430..441
FT /evidence="ECO:0007829|PDB:1SKY"
FT TURN 442..447
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 450..452
FT /evidence="ECO:0007829|PDB:1SKY"
FT STRAND 456..459
FT /evidence="ECO:0007829|PDB:1SKY"
FT HELIX 460..466
FT /evidence="ECO:0007829|PDB:1SKY"
FT TURN 467..469
FT /evidence="ECO:0007829|PDB:1SKY"
SQ SEQUENCE 473 AA; 51938 MW; 3CFDE82E98D58DEB CRC64;
MTRGRVIQVM GPVVDVKFEN GHLPAIYNAL KIQHKARNEN EVDIDLTLEV ALHLGDDTVR
TIAMASTDGL IRGMEVIDTG APISVPVGQV TLGRVFNVLG EPIDLEGDIP ADARRDPIHR
PAPKFEELAT EVEILETGIK VVDLLAPYIK GGKIGLFGGA GVGKTVLIQE LIHNIAQEHG
GISVFAGVGE RTREGNDLYH EMKDSGVISK TAMVFGQMNE PPGARMRVAL TGLTMAEYFR
DEQGQDGLLF IDNIFRFTQA GSEVSALLGR MPSAIGYQPT LATEMGQLQE RITSTAKGSI
TSIQAIYVPA DDYTDPAPAT TFSHLDATTN LERKLAEMGI YPAVDPLVST SRALAPEIVG
EEHYQVARKV QQTLERYKEL QDIIAILGMD ELSDEDKLVV HRARRIQFFL SQNFHVAEQF
TGQPGSYVPV KETVRGFKEI LEGKYDHLPE DRFRLVGRIE EVVEKAKAMG VEV
