ID   RCA_PHAVU               Reviewed;         441 AA.
AC   O64981;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Ribulose bisphosphate carboxylase/oxygenase activase, chloroplastic;
DE            Short=RA;
DE            Short=RuBisCO activase;
DE   Flags: Precursor;
GN   Name=RCA1;
OS   Phaseolus vulgaris (Kidney bean) (French bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX   NCBI_TaxID=3885;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Tendergreen; TISSUE=Leaf;
RA   Ryan J.E., Andralojc P.J., Willis A.C., Gutteridge S., Parry M.A.J.;
RT   "Cloning and sequencing of a Phaseolus vulgaris cDNA encoding Rubisco
RT   activase.";
RL   (er) Plant Gene Register PGR98-044(1998).
CC   -!- FUNCTION: Activation of RuBisCO (ribulose-1,5-bisphosphate
CC       carboxylase/oxygenase; EC 4.1.1.39) involves the ATP-dependent
CC       carboxylation of the epsilon-amino group of lysine leading to a
CC       carbamate structure.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma.
CC   -!- SIMILARITY: Belongs to the RuBisCO activase family. {ECO:0000305}.
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DR   EMBL; AF041068; AAC12868.1; -; mRNA.
DR   PIR; T10815; T10815.
DR   AlphaFoldDB; O64981; -.
DR   SMR; O64981; -.
DR   STRING; 3885.XP_007163435.1; -.
DR   PRIDE; O64981; -.
DR   eggNOG; KOG0651; Eukaryota.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR044960; RCA-like.
DR   PANTHER; PTHR32429; PTHR32429; 1.
DR   Pfam; PF00004; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chloroplast; Nucleotide-binding; Plastid; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..441
FT                   /note="Ribulose bisphosphate carboxylase/oxygenase
FT                   activase, chloroplastic"
FT                   /id="PRO_0000030240"
FT   BINDING         167..174
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   441 AA;  48201 MW;  07C9D8F2CB828BD7 CRC64;
     MAASLSTVGA VNRTLLNLNG SGGGASGPSS AFFGTSLKKV ISSRVPNSKL TSGSFKIVAA
     DKEIEETQQT EGDRWRGLAY DVSDDQQDIT RGKGLVDSLF QAPMDAGTHY AVISSHKYLS
     AGLRQYNFDN IKDGFYIAPA FLDKLVVHIA KNFMTLPNIK VPLILGVWGG KGQGKSFQCE
     LVFAKMGINP IMMSAGELES GNAGEPAKLI RQRYREASDL IKKGKMCVLF INDLDAGAGR
     LGGTTQYTVN NQMVNATLMN IADNPTNVQL PGMYNKEDNA RVPIIVTGND FSTLYAPLIR
     DGRMEKFYWA PTREDRIGVC KGIFRTDGVP EKDIVELVDK HPGQSIDFFG ALRARVYDDE
     VRKWISGVGV DSVGKKLVNS KEGPPTFDQP KMTLDKLLLY ASMLVQEQEN VKRVQLADQY
     LNEAALGNAN EDAIKSGSFF K