ATPB1_BURTA
ID ATPB1_BURTA Reviewed; 464 AA.
AC Q2STE9;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=ATP synthase subunit beta 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01347};
DE AltName: Full=F-ATPase subunit beta 1 {ECO:0000255|HAMAP-Rule:MF_01347};
GN Name=atpD1 {ECO:0000255|HAMAP-Rule:MF_01347}; OrderedLocusNames=BTH_I3308;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
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}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01347}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC 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; CP000086; ABC36651.1; -; Genomic_DNA.
DR RefSeq; WP_004185243.1; NZ_CP008785.1.
DR PDB; 4Q4L; X-ray; 2.20 A; A=1-464.
DR PDBsum; 4Q4L; -.
DR AlphaFoldDB; Q2STE9; -.
DR SMR; Q2STE9; -.
DR PRIDE; Q2STE9; -.
DR EnsemblBacteria; ABC36651; ABC36651; BTH_I3308.
DR GeneID; 56593896; -.
DR GeneID; 66545412; -.
DR KEGG; bte:BTH_I3308; -.
DR HOGENOM; CLU_022398_0_2_4; -.
DR OMA; GFNMIMD; -.
DR OrthoDB; 430176at2; -.
DR Proteomes; UP000001930; Chromosome I.
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 inner membrane;
KW Cell membrane; CF(1); Hydrogen ion transport; Ion transport; Membrane;
KW Nucleotide-binding; Translocase; Transport.
FT CHAIN 1..464
FT /note="ATP synthase subunit beta 1"
FT /id="PRO_0000254235"
FT BINDING 153..160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
FT STRAND 8..22
FT /evidence="ECO:0007829|PDB:4Q4L"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:4Q4L"
FT STRAND 43..51
FT /evidence="ECO:0007829|PDB:4Q4L"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:4Q4L"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:4Q4L"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:4Q4L"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:4Q4L"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:4Q4L"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:4Q4L"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:4Q4L"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:4Q4L"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:4Q4L"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:4Q4L"
FT HELIX 159..174
FT /evidence="ECO:0007829|PDB:4Q4L"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:4Q4L"
FT HELIX 192..199
FT /evidence="ECO:0007829|PDB:4Q4L"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:4Q4L"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:4Q4L"
FT HELIX 217..236
FT /evidence="ECO:0007829|PDB:4Q4L"
FT STRAND 240..247
FT /evidence="ECO:0007829|PDB:4Q4L"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:4Q4L"
FT HELIX 258..262
FT /evidence="ECO:0007829|PDB:4Q4L"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:4Q4L"
FT HELIX 275..283
FT /evidence="ECO:0007829|PDB:4Q4L"
FT STRAND 286..291
FT /evidence="ECO:0007829|PDB:4Q4L"
FT STRAND 293..301
FT /evidence="ECO:0007829|PDB:4Q4L"
FT STRAND 320..325
FT /evidence="ECO:0007829|PDB:4Q4L"
FT HELIX 327..331
FT /evidence="ECO:0007829|PDB:4Q4L"
FT TURN 340..342
FT /evidence="ECO:0007829|PDB:4Q4L"
FT HELIX 350..353
FT /evidence="ECO:0007829|PDB:4Q4L"
FT HELIX 355..373
FT /evidence="ECO:0007829|PDB:4Q4L"
FT HELIX 375..381
FT /evidence="ECO:0007829|PDB:4Q4L"
FT HELIX 383..385
FT /evidence="ECO:0007829|PDB:4Q4L"
FT HELIX 388..403
FT /evidence="ECO:0007829|PDB:4Q4L"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:4Q4L"
FT HELIX 412..415
FT /evidence="ECO:0007829|PDB:4Q4L"
FT HELIX 424..436
FT /evidence="ECO:0007829|PDB:4Q4L"
FT TURN 437..441
FT /evidence="ECO:0007829|PDB:4Q4L"
FT HELIX 444..447
FT /evidence="ECO:0007829|PDB:4Q4L"
FT HELIX 453..460
FT /evidence="ECO:0007829|PDB:4Q4L"
SQ SEQUENCE 464 AA; 50623 MW; BCDC614B33CF456F CRC64;
MSTAALVEGK IVQCIGAVID VEFPRESMPK IYDALILEGS ELTLEVQQQL GDGVVRTICL
GASDGLRRGV VVKNTGNPIS VPVGKPTLGR IMDVLGRPID EAGPIESENK RSIHQKAPAF
DELSPSTELL ETGIKVIDLI CPFAKGGKVG LFGGAGVGKT VNMMELINNI AKEHGGYSVF
AGVGERTREG NDFYHEMKDS NVLDKVALVY GQMNEPPGNR LRVALTGLTM AEHFRDEGLD
VLFFVDNIYR FTLAGTEVSA LLGRMPSAVG YQPTLAEEMG KLQERITSTK KGSITSVQAV
YVPADDLTDP SPATTFGHLD ATVVLSRDIA SLGIYPAVDP LDSTSRQIDP NVIGEEHYSI
TRRVQQTLQR YKELRDIIAI LGMDELSPED KLSVARARKI QRFLSQPFHV AEVFTGSPGK
YVPLKETIRG FKMIVDGECD HLPEQAFYMV GTIDEAFEKA KKIQ
