ATPB_RHOCA
ID ATPB_RHOCA Reviewed; 472 AA.
AC P72247;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 121.
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 Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33303 / B10;
RX PubMed=9440534; DOI=10.1128/jb.180.2.416-421.1998;
RA Borghese R., Crimi M., Fava L., Melandri B.A.;
RT "The ATP synthase atpHAGDC (F1) operon from Rhodobacter capsulatus.";
RL J. Bacteriol. 180:416-421(1998).
RN [2]
RP PROTEIN SEQUENCE OF 2-19, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=GA;
RA Gabellini N., Gao Z., Eckerskorn C., Lottspeich F., Oesterhelt D.;
RT "Purification of the H+-ATPase from Rhodobacter capsulatus, identification
RT of the F1F0 components and reconstitution of the active enzyme.";
RL Biochim. Biophys. Acta 934:227-234(1988).
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, b, b' and c. {ECO:0000269|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Cellular chromatophore membrane
CC {ECO:0000269|Ref.2}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01347, ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_01347}.
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DR EMBL; X99599; CAA67910.1; -; Genomic_DNA.
DR RefSeq; WP_013068671.1; NZ_VIBE01000018.1.
DR AlphaFoldDB; P72247; -.
DR SMR; P72247; -.
DR GeneID; 31491766; -.
DR OMA; GFNMIMD; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0042717; C:plasma membrane-derived chromatophore 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; CF(1); Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Nucleotide-binding;
KW Translocase; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 2..472
FT /note="ATP synthase subunit beta"
FT /id="PRO_0000144464"
FT BINDING 150..157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
FT CONFLICT 2
FT /note="A -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 472 AA; 50126 MW; 3C1298981139309A CRC64;
MASKGKVTQV IGAVVDVQFE DGLPAILNAL ETTNNGKRLV LEVAQHLGEN TVRTIAMDAT
EGLVRGAAVS DTGGPITVPV GNATLGRILN VIGEPVDERG DVSKAEARAI HQPAPDFAAQ
STESQILVTG IKVIDLLAPY SKGGKIGLFG GAGVGKTVLI MELINNIAKV HSGFSVFAGV
GERTREGNDL YHEMIESGVI NLEKLEESKV ALVYGQMNEP PGARARVALT GLTLAEQFRD
QSGTDVLFFV DNIFRFTQAG SEVSALLGRI PSAVGYQPTL ATDMGALQER ITSTKAGSIT
SVQAIYVPAD DLTDPAPATS FAHLDATTVL SRAISELGIY PAVDPLDSTS RILDPQVVGE
EHYQVARDVQ GMLQRYKSLQ DIIAILGMDE LSEEDKLTVA RARKIQRFLS QPFDVAKVFT
GSDGVQVPLE DTIKSFKAVV AGEYDHLPEA AFYMVGGIDD VIAKAQRLAA AA
