ID ATPB_IPOSE Reviewed; 490 AA. AC Q7H8M1; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 09-FEB-2010, entry version 43. DE RecName: Full=ATP synthase subunit beta, chloroplastic; DE EC=3.6.3.14; DE AltName: Full=F-ATPase subunit beta; DE AltName: Full=ATP synthase F1 sector subunit beta; GN Name=atpB; OS Ipomoea setosa (Brazilian morning glory). OG Plastid; Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea. OX NCBI_TaxID=89662; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX AGRICOLA=IND23320510; RA Stefanovic S., Krueger L., Olmstead R.G.; RT "Monophyly of the Convolvulaceae and circumscription of their major RT lineages based on DNA sequences of multiple chloroplast loci."; RL Am. J. Bot. 89:1510-1522(2002). CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton CC gradient across the membrane. The catalytic sites are hosted CC primarily by the beta subunits (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate + CC H(+)(Out). CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic CC core - and CF(0) - the membrane proton channel. CF(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) CC has four main subunits: a(1), b(1), b'(1) and c(9-12) (By CC similarity). CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; CC Peripheral membrane protein (By similarity). CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY100750; AAM52104.1; -; Genomic_DNA. DR HSSP; P00825; 1KMH. DR SMR; Q7H8M1; 19-483. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW. DR GO; GO:0019898; C:extrinsic to membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045261; C:proton-transporting ATP synthase complex, c...; IEA:UniProtKB-KW. DR GO; GO:0009579; C:thylakoid; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0046933; F:hydrogen ion transporting ATP synthase acti...; IEA:HAMAP. DR GO; GO:0008553; F:hydrogen-exporting ATPase activity, phospho...; IEA:InterPro. DR GO; GO:0046961; F:proton-transporting ATPase activity, rotati...; IEA:InterPro. DR GO; GO:0042777; P:plasma membrane ATP synthesis coupled proto...; IEA:HAMAP. DR HAMAP; MF_01347; ATP_synth_beta_bact; 1; -. DR InterPro; IPR003593; ATPase_AAA+_core. DR InterPro; IPR005722; ATPase_F1-cplx_bsu. DR InterPro; IPR018118; ATPase_F1/A1-cplx_a/bsu_N. DR InterPro; IPR000793; ATPase_F1/V1/A1-cplx_a/bsu_C. DR InterPro; IPR004100; ATPase_F1/V1/A1-cplx_a/bsu_N. DR InterPro; IPR020003; ATPase_F1/V1/A1_a/bsu_AS. DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd. DR PANTHER; PTHR15184:SF8; ATPase_F1_b; 1. DR Pfam; PF00006; ATP-synt_ab; 1. DR Pfam; PF00306; ATP-synt_ab_C; 1. DR Pfam; PF02874; ATP-synt_ab_N; 1. DR SMART; SM00382; AAA; 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; KW Hydrogen ion transport; Hydrolase; Ion transport; Membrane; KW Nucleotide-binding; Plastid; Thylakoid; Transport. FT CHAIN 1 490 ATP synthase subunit beta, chloroplastic. FT /FTId=PRO_0000254490. FT NP_BIND 170 177 ATP (By similarity). SQ SEQUENCE 490 AA; 52827 MW; 5ED186DAD8B0FD94 CRC64; MRINPTTSGS EVSAVEKKNL GRIVKIIGPV LDVAFPPGKM PNIYNALVVQ GRGNEQTNVT CEVQQLLGNN RVRAVAMSDT DGLMRGMEVI DTGAPISVPV GGSTLGRIFN VLGQPVDNLG PVDTNTTSPI HRSAPAFIQL DTKLSIFETG IKVVDLLAPY RRGGKIGLFG GAGVGKTVLI MELINNIAKA HGGVSVFGGV GERTREGNDL YLEMKESGVI NEENIPESKV ALVYGQMNEP PGARMRVGLT ALTMAEYFRD VNEQDVLLFI DNIFRFVQAG SEVSALLGRM PSAVGYQPTL STEMGSLQER ITSTKEGSIT SIQAVYVPAD DLTDPAPATT FAHLDATTVL SRGLAAKGIY PAVDPLDSTS TMLQPRIVGE EHYETAQRVK QTLQRYKELQ DIIAILGLDE LSEEDRLTVA RARKIERFLS QPFFVAEVFT GSPGKYVGLA ETIRGFQLIL SGELDGLPEQ AFYLVGNIDE ATAKAMNLKT //