ID   RCA_ANASC               Reviewed;         415 AA.
AC   Q06721;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Ribulose bisphosphate carboxylase/oxygenase activase;
DE            Short=RA;
DE            Short=RuBisCO activase;
GN   Name=rca;
OS   Anabaena sp. (strain CA / ATCC 33047).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena;
OC   unclassified Anabaena.
OX   NCBI_TaxID=52271;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CA / ATCC 33047;
RX   PubMed=8467074; DOI=10.1007/bf00027109;
RA   Li L.A., Gibson J.L., Tabita F.R.;
RT   "The Rubisco activase (rca) gene is located downstream from rbcS in
RT   Anabaena sp. strain CA and is detected in other Anabaena/Nostoc strains.";
RL   Plant Mol. Biol. 21:753-764(1993).
RN   [2]
RP   INDUCTION BY LIGHT, AND OPERON STRUCTURE.
RC   STRAIN=CA / ATCC 33047;
RX   PubMed=7961423; DOI=10.1128/jb.176.21.6697-6706.1994;
RA   Li L.A., Tabita F.R.;
RT   "Transcription control of ribulose bisphosphate carboxylase/oxygenase
RT   activase and adjacent genes in Anabaena species.";
RL   J. Bacteriol. 176:6697-6706(1994).
CC   -!- FUNCTION: Activation of RuBisCO (ribulose-1,5-bisohosphate
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   -!- INDUCTION: Transcribed in light but much less in the dark in both
CC       normal air and 1% CO(2); the nitrogen source has no effect on
CC       transcription. Constitutively expressed when grown on fructose.
CC       Transcribed separately from rbcL-rbcX-rbcS.
CC       {ECO:0000269|PubMed:7961423}.
CC   -!- SIMILARITY: Belongs to the RuBisCO activase family. {ECO:0000305}.
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DR   EMBL; X67942; CAA48129.1; -; Genomic_DNA.
DR   RefSeq; WP_066380864.1; NZ_LUHI01000044.1.
DR   AlphaFoldDB; Q06721; -.
DR   SMR; Q06721; -.
DR   PRIDE; Q06721; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   Gene3D; 3.30.190.10; -; 1.
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   InterPro; IPR000894; RuBisCO_ssu_dom.
DR   InterPro; IPR036385; RuBisCO_ssu_sf.
DR   PANTHER; PTHR32429; PTHR32429; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF00101; RuBisCO_small; 1.
DR   SMART; SM00961; RuBisCO_small; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF55239; SSF55239; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Nucleotide-binding.
FT   CHAIN           1..415
FT                   /note="Ribulose bisphosphate carboxylase/oxygenase
FT                   activase"
FT                   /id="PRO_0000216427"
FT   BINDING         37..44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   415 AA;  46595 MW;  1CF71296D94A892D CRC64;
     MSYYIAPRFL DKLAVHITKN FLNLPGVRVP LILGIHGRKG EGKTFQCELA FEKMGVEVTL
     ISGGELESPD AGDPARLIRL RYRETAELIK VRGKMCVLMI NDLDAGAGRF DEGTQYTVNT
     QLVNATLMNI ADNPTDVQLP GSYDSTPLRR VPIIVTGNDF STLYAPLIRD GRMEKFYWEP
     HRDEKVGIVG GIFAEDGLSQ RDVEKLVDSF PNQSIDFFSA LRSRIYDEQI RDFIHQVGYE
     NVSLRVVNSL EGPPAFKKPD FTLSHLIESA NFMVAEQKRI ETSQLVDEYN RLNRGRSYQP
     ASPVAEIATS QPSPNGVNQP QSASPHISLE TQEQIRQILA QGHKITFEHV DNRRFRTGSW
     QSCGTIHVDA ESDAISTLES CLAEYRGEYV RLVGIDPKAK RRVVETIIQR PNGTN