ATPB_RHORU
ID ATPB_RHORU Reviewed; 474 AA.
AC P05038;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 129.
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 Rhodospirillum rubrum.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=1085;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2861810; DOI=10.1042/bj2280391;
RA Falk G., Hampe A., Walker J.E.;
RT "Nucleotide sequence of the Rhodospirillum rubrum atp operon.";
RL Biochem. J. 228:391-407(1985).
RN [2]
RP PROTEIN SEQUENCE OF 2-20.
RX PubMed=1327870; DOI=10.1016/0014-5793(92)81326-h;
RA Andralojc P.J., Harris D.A.;
RT "Isolation and characterisation of a functional alpha beta heterodimer from
RT the ATP synthase of Rhodospirillum rubrum.";
RL FEBS Lett. 310:187-192(1992).
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 four main
CC subunits: a(1), b(1), b'(1) and c(9-12). {ECO:0000255|HAMAP-
CC 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; X02499; CAA26340.1; -; Genomic_DNA.
DR PIR; S08583; PWQFB.
DR RefSeq; WP_011388981.1; NZ_NHSM01000086.1.
DR AlphaFoldDB; P05038; -.
DR SMR; P05038; -.
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 ATP synthesis; ATP-binding; Cell inner membrane; Cell membrane; CF(1);
KW Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane;
KW Nucleotide-binding; Translocase; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1327870"
FT CHAIN 2..474
FT /note="ATP synthase subunit beta"
FT /id="PRO_0000144463"
FT BINDING 152..159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ SEQUENCE 474 AA; 50853 MW; CC4AEE0D1DD66ED7 CRC64;
MAKNNLGTIT QVTGAVVDVK FEGELPSILS ALETDNHGNR LVLEVAQHLG ESVVRTIAMD
STEGLVRGQQ VTSTGGPITV PVGPQVLGRI MNVIGEPVDE RGPVVTAQRY PIHRQAPTFA
EQATETEILV TGIKVIDLIA PYTKGGKVGL FGGAGVGKTV LIQELINNVA KGHGGYSVFA
GVGERTREGN DLYHEMIDAG IIDLEGDKSK VALVYGQMNE PPGARARVAL AGLTQAEYFR
DEEGQDVLFF VDNIFRFTQA GSEVSALLGR IPSAVGYQPT LATDMGALQE RITSTKKGSI
TSVQAIYVPA DDLTDPAPAA SFAHLDATTT LNRSIAELGI YPAVDPLDST SRALDPLVVG
EEHYKVAREV QRVLQTYKSL QDIIAILGMD ELSEEDRLVV ARARKIQRFL SQPFHVAEVF
TGSPGKLVSL EDTIKGFKGL VEGEYDHLPE QAFYMVGNMA EAIEKAKKMA AEAA
