ATPB_RHDSA
ID ATPB_RHDSA Reviewed; 471 AA.
AC A6MVY0;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=ATP synthase subunit beta, chloroplastic {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=atpB {ECO:0000255|HAMAP-Rule:MF_01347};
OS Rhodomonas salina (Cryptomonas salina).
OG Plastid; Chloroplast.
OC Eukaryota; Cryptophyceae; Pyrenomonadales; Pyrenomonadaceae; Rhodomonas.
OX NCBI_TaxID=52970;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1319 / NEPCC76 / CS-174;
RX PubMed=17522086; DOI=10.1093/molbev/msm101;
RA Khan H., Parks N., Kozera C., Curtis B.A., Parsons B.J., Bowman S.,
RA Archibald J.M.;
RT "Plastid genome sequence of the cryptophyte alga Rhodomonas salina
RT CCMP1319: lateral transfer of putative DNA replication machinery and a test
RT of chromist plastid phylogeny.";
RL Mol. Biol. Evol. 24:1832-1842(2007).
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: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01347}; Peripheral membrane protein
CC {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; EF508371; ABO70751.1; -; Genomic_DNA.
DR RefSeq; YP_001293559.1; NC_009573.1.
DR AlphaFoldDB; A6MVY0; -.
DR SMR; A6MVY0; -.
DR PRIDE; A6MVY0; -.
DR GeneID; 5228594; -.
DR GO; GO:0009535; C:chloroplast thylakoid 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 3: Inferred from homology;
KW ATP synthesis; ATP-binding; CF(1); Chloroplast; Hydrogen ion transport;
KW Ion transport; Membrane; Nucleotide-binding; Plastid; Thylakoid;
KW Translocase; Transport.
FT CHAIN 1..471
FT /note="ATP synthase subunit beta, chloroplastic"
FT /id="PRO_0000339639"
FT BINDING 151..158
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ SEQUENCE 471 AA; 51060 MW; C7D449234D535E18 CRC64;
MVNTATNTGF ITQIIGPVID IEFPNGKLPP IYNSVIVSDV TCEVQQLLGN NRVRAVSMTS
TDGLKRGMEV TDLNAPISVP VGKSTLGRIF NVLGVPVDEM GEVSMETTLP IHRLSPRFTE
LETKPSIFET GIKVVDLLAP YRRGGKIGLF GGAGVGKTVL IMELINNIAK AHGGVSVFGG
VGERTREGND LYMEMKESGV INASNLSESK VALVYGQMNE PPGARMRVGL TALTMAEYFR
DVNKQDVLLF IDNIFRFVQA GSEVSALLGR MPSAVGYQPT LATEMGTLQE RITSTREGSI
TSIQAVYVPA DDLTDPAPAT TFSHLDATTV LSRNLAAKGI YPAVDPLDST STMLQINIVG
SEHYDTAQDV KETLQRYKEL QDIIAILGLD ELSEEDRLTV ARARKVERFL SQPFFVAEVF
TGSPGKYVSL ADTIKGFNMI LNGELDELPE QAFYLVGNID EAIEKANSLK G