ID A0A7M3URW0_CROPI Unreviewed; 495 AA. AC A0A7M3URW0; DT 07-APR-2021, integrated into UniProtKB/TrEMBL. DT 07-APR-2021, sequence version 1. DT 24-JAN-2024, entry version 12. DE RecName: Full=ATP synthase subunit beta, chloroplastic {ECO:0000256|HAMAP-Rule:MF_01347}; DE EC=7.1.2.2 {ECO:0000256|HAMAP-Rule:MF_01347}; DE AltName: Full=ATP synthase F1 sector subunit beta {ECO:0000256|HAMAP-Rule:MF_01347}; DE AltName: Full=F-ATPase subunit beta {ECO:0000256|HAMAP-Rule:MF_01347}; GN Name=atpB {ECO:0000256|HAMAP-Rule:MF_01347, GN ECO:0000313|EMBL:QOJ44424.1}; OS Crotalaria pallida (Smooth rattlebox) (Crotalaria striata). OG Plastid; Chloroplast {ECO:0000313|EMBL:QOJ44424.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC genistoids sensu lato; core genistoids; Crotalarieae; Crotalaria. OX NCBI_TaxID=3830 {ECO:0000313|EMBL:QOJ44424.1}; RN [1] {ECO:0000313|EMBL:QOJ44424.1} RP NUCLEOTIDE SEQUENCE. RA Li H., Zhou N.; RT "The complete chloroplast genome sequences of Crotalaria pallida RT (Leguminosae)."; RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases. 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:0000256|ARBA:ARBA00037290, ECO:0000256|HAMAP- CC 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:0000256|ARBA:ARBA00001741, ECO:0000256|HAMAP- CC Rule:MF_01347, ECO:0000256|RuleBase:RU003553}; 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:0000256|HAMAP- CC Rule:MF_01347, ECO:0000256|RuleBase:RU003553}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170}; CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}. Plastid, CC chloroplast thylakoid membrane {ECO:0000256|HAMAP-Rule:MF_01347}; CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01347}. CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. CC {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|HAMAP-Rule:MF_01347}. 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; MT920364; QOJ44424.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7M3URW0; -. 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:0016887; F:ATP hydrolysis activity; IEA:InterPro. 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 CDD; cd18110; ATP-synt_F1_beta_C; 1. DR CDD; cd18115; ATP-synt_F1_beta_N; 1. DR CDD; cd01133; F1-ATPase_beta_CD; 1. DR Gene3D; 2.40.10.170; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR01039; atpD; 1. DR PANTHER; PTHR15184; ATP SYNTHASE; 1. DR PANTHER; PTHR15184:SF71; ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL; 1. DR Pfam; PF00006; ATP-synt_ab; 1. DR Pfam; PF02874; ATP-synt_ab_N; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1. DR SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1. PE 3: Inferred from homology; KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310, ECO:0000256|HAMAP- KW Rule:MF_01347}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01347}; KW CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|HAMAP-Rule:MF_01347}; KW Chloroplast {ECO:0000313|EMBL:QOJ44424.1}; KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781, ECO:0000256|HAMAP- KW Rule:MF_01347}; KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP- KW Rule:MF_01347}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01347}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01347}; KW Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000313|EMBL:QOJ44424.1}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01347}; KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP- KW Rule:MF_01347}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01347}. FT DOMAIN 161..353 FT /note="AAA+ ATPase" FT /evidence="ECO:0000259|SMART:SM00382" FT BINDING 169..176 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01347" SQ SEQUENCE 495 AA; 53248 MW; 6D9C051810F60583 CRC64; MKLNPTTSGP TISAKTPGRI AQIIGPVLDV AFPPGKMPNI YNALVVKGQD TVGQQINVTC EVQQLLGNNR VRAVAMSATD GLKRGMEVID TGAPLSVPVG GATLGRIFNV LGEPIDNLGP VDIRTTSPIH RSAPAFIQLD TKLSIFETGI KVVDLLAPYR RGGKIGLFGG AGVGKTVLIM ELINNIAKAH GGVSVFGGVG ERTREGNDLY MEMKESGVIN EQNIAESKVA LVYGQMNEPP GARMRVGLTA LTMAEYFRDV NEQDVLLFID NIFRFVQAGS EVSALLGRMP SAVGYQPTLS TEMGSLQERI TSTKEGSITS IQAVYVPADD LTDPAPATTF AHLDATTVLS RGLAAKGIYP AVDPLDSTST MLQPRIVGEE HYETAQRVKQ TLQRYKELQD IIAILGLDEL SEEDRLTVAR ARKIERFLSQ PFFVAEVFTG SPGKYVGLAE TIRGFKLILS GELDGLPEQA FYLVGNIDEA TAKATNLETE SKLKK //