ID   RCA1_TOBAC              Reviewed;         442 AA.
AC   Q40460; Q40564;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Ribulose bisphosphate carboxylase/oxygenase activase 1, chloroplastic;
DE            Short=RA 1;
DE            Short=RuBisCO activase 1;
DE   Flags: Precursor;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Petit Havana SR1; TISSUE=Leaf;
RA   Snyder G.W., Esau B.D., Portis A.R., Ogren W.L.;
RL   Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 237-442.
RC   STRAIN=cv. SR1; TISSUE=Leaf;
RX   PubMed=8108517; DOI=10.1104/pp.102.2.683;
RA   Qian J., Rodermel S.;
RT   "Ribulose-1,5-bisphosphate carboxylase/oxygenase activase cDNAs from
RT   Nicotiana tabacum.";
RL   Plant Physiol. 102:683-684(1993).
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   -!- INTERACTION:
CC       Q40460; Q40460: -; NbExp=2; IntAct=EBI-15950801, EBI-15950801;
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma.
CC   -!- SIMILARITY: Belongs to the RuBisCO activase family. {ECO:0000305}.
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DR   EMBL; U35111; AAA78277.1; -; mRNA.
DR   EMBL; Z14979; CAA78702.1; -; mRNA.
DR   PIR; S25482; S25482.
DR   RefSeq; NP_001312984.1; NM_001326055.1.
DR   PDB; 3T15; X-ray; 2.95 A; A=127-419.
DR   PDB; 3ZW6; EM; 20.00 A; A/B/C/D/E/F=127-419.
DR   PDBsum; 3T15; -.
DR   PDBsum; 3ZW6; -.
DR   AlphaFoldDB; Q40460; -.
DR   SMR; Q40460; -.
DR   DIP; DIP-59441N; -.
DR   STRING; 4097.Q40460; -.
DR   PRIDE; Q40460; -.
DR   ProMEX; Q40460; -.
DR   GeneID; 107819807; -.
DR   KEGG; nta:107819807; -.
DR   Proteomes; UP000084051; Unplaced.
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   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0046863; F:ribulose-1,5-bisphosphate carboxylase/oxygenase activator activity; IBA:GO_Central.
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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Chloroplast; Nucleotide-binding; Plastid;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..58
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           59..442
FT                   /note="Ribulose bisphosphate carboxylase/oxygenase activase
FT                   1, chloroplastic"
FT                   /id="PRO_0000030242"
FT   BINDING         169..176
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        237
FT                   /note="G -> E (in Ref. 2; CAA78702)"
FT                   /evidence="ECO:0000305"
FT   HELIX           139..151
FT                   /evidence="ECO:0007829|PDB:3T15"
FT   STRAND          163..169
FT                   /evidence="ECO:0007829|PDB:3T15"
FT   HELIX           175..185
FT                   /evidence="ECO:0007829|PDB:3T15"
FT   STRAND          191..194
FT                   /evidence="ECO:0007829|PDB:3T15"
FT   HELIX           195..199
FT                   /evidence="ECO:0007829|PDB:3T15"
FT   HELIX           205..221
FT                   /evidence="ECO:0007829|PDB:3T15"
FT   STRAND          229..232
FT                   /evidence="ECO:0007829|PDB:3T15"
FT   HELIX           251..263
FT                   /evidence="ECO:0007829|PDB:3T15"
FT   STRAND          284..287
FT                   /evidence="ECO:0007829|PDB:3T15"
FT   HELIX           297..303
FT                   /evidence="ECO:0007829|PDB:3T15"
FT   STRAND          304..309
FT                   /evidence="ECO:0007829|PDB:3T15"
FT   HELIX           313..324
FT                   /evidence="ECO:0007829|PDB:3T15"
FT   HELIX           325..327
FT                   /evidence="ECO:0007829|PDB:3T15"
FT   HELIX           331..340
FT                   /evidence="ECO:0007829|PDB:3T15"
FT   HELIX           346..367
FT                   /evidence="ECO:0007829|PDB:3T15"
FT   HELIX           374..377
FT                   /evidence="ECO:0007829|PDB:3T15"
FT   HELIX           394..418
FT                   /evidence="ECO:0007829|PDB:3T15"
SQ   SEQUENCE   442 AA;  48754 MW;  CC90BF8F3B5F2C40 CRC64;
     MATSVSTIGA VNKTPLSLNN SVAGTSVPST AFFGKTLKKV YGKGVSSPKV TNKSLRIVAE
     QIDVDPKKQT DSDRWKGLVQ DFSDDQQDIT RGKGMVDSLF QAPTGTGTHH AVLQSYEYVS
     QGLRQYNLDN KLDGFYIAPA FMDKLVVHIT KNFLKLPNIK VPLILGIWGG KGQGKSFQCE
     LVFRKMGINP IMMSAGELES GNAGEPAKLI RQRYREAAEI IRKGNMCCLF INDLDAGAGR
     MGGTTQYTVN NQMVNATLMN IADNPTNVQL PGMYNKQENA RVPIIVTGND FSTLYAPLIR
     DGRMEKFYWA PTREDRIGVC TGIFRTDNVP AEDVVKIVDN FPGQSIDFFG ALRARVYDDE
     VRKWVSGTGI EKIGDKLLNS FDGPPTFEQP KMTIEKLLEY GNMLVQEQEN VKRVQLADKY
     LKEAALGDAN ADAINNGSFF AS