ID   RCA2_LARTR              Reviewed;         435 AA.
AC   Q7X999;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Ribulose bisphosphate carboxylase/oxygenase activase 2, chloroplastic;
DE            Short=RA 2;
DE            Short=RuBisCO activase 2;
DE   AltName: Full=RuBisCO activase beta form;
DE   Flags: Precursor;
GN   Name=RCA2;
OS   Larrea tridentata (Creosote bush) (Zygophyllum tridentatum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Zygophyllales; Zygophyllaceae; Larreoideae; Larrea.
OX   NCBI_TaxID=66636;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15084731; DOI=10.1104/pp.103.038323;
RA   Salvucci M.E., Crafts-Brandner S.J.;
RT   "Relationship between the heat tolerance of photosynthesis and the thermal
RT   stability of rubisco activase in plants from contrasting thermal
RT   environments.";
RL   Plant Physiol. 134:1460-1470(2004).
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RuBisCO activase family. {ECO:0000305}.
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DR   EMBL; AY312576; AAP83930.1; -; mRNA.
DR   AlphaFoldDB; Q7X999; -.
DR   SMR; Q7X999; -.
DR   PRIDE; Q7X999; -.
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..56
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           57..435
FT                   /note="Ribulose bisphosphate carboxylase/oxygenase activase
FT                   2, chloroplastic"
FT                   /id="PRO_0000030234"
FT   BINDING         165..172
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   435 AA;  48054 MW;  EBA17540A8E4E0C2 CRC64;
     MAAAYSTVGA VNRAPLSLNG SGARASLVPS TAFFGSSLKK SAAKFPKASS GNFKIVAQEI
     SEDQQTDKDK WKGLAYDISD DQQDITRGKG MVDTLFQAPM QSGTHYAVMS SYDYISQGLR
     QYNLDNNMDG FYIAPAFMDK LVVHITKNFL SLPNIKIPLI LGIWGGKGQG KSFQCELVFA
     KMGINPIMMS AGELESGNAG EPAKLIRQRY REAADIIKKG KMCCLFINDL DAGAGRMGGT
     TQYTVNNQMV NATLMNIADN PTNVQLPGMY NKEENPRVPI IVTGNDFSTL YAPLIRDGRM
     EKFYWAPTRE DRIGVCKGIF RTDNVPEEDI VKVVDQFPGQ SIDFFGALRA RVYDDEVRKW
     VSEVGVDTIG KKLVNSKEGP PTFEQPKMTI DKLLQYGNML VEEQENVKRV QLADKYMSEA
     ALGDANQDAI KRGTF