ID   RUBA_PEA                Reviewed;         587 AA.
AC   P08926;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=RuBisCO large subunit-binding protein subunit alpha, chloroplastic;
DE   AltName: Full=60 kDa chaperonin subunit alpha;
DE   AltName: Full=CPN-60 alpha;
DE   Flags: Precursor;
OS   Pisum sativum (Garden pea).
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; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7629128; DOI=10.1074/jbc.270.30.18158;
RA   Viitanen P.V., Schmidt M., Buchner J., Suzuki T., Vierling E.,
RA   Dickson R.R., Lorimer G.H., Gatenby A., Soll J.;
RT   "Functional characterization of the higher plant chloroplast chaperonins.";
RL   J. Biol. Chem. 270:18158-18164(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 48-67.
RC   STRAIN=cv. Feltham First;
RX   PubMed=3549295; DOI=10.1111/j.1432-1033.1987.tb10900.x;
RA   Musgrove J.E., Johnson R.A., Ellis R.J.;
RT   "Dissociation of the ribulosebisphosphate-carboxylase large-subunit binding
RT   protein into dissimilar subunits.";
RL   Eur. J. Biochem. 163:529-534(1987).
CC   -!- FUNCTION: This protein binds RuBisCO small and large subunits and is
CC       implicated in the assembly of the enzyme oligomer.
CC   -!- SUBUNIT: Oligomer of probably six alpha and six beta subunits.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- MISCELLANEOUS: This protein shows ATPase activity.
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR   EMBL; U21105; AAA87731.1; -; mRNA.
DR   PIR; S07232; S07232.
DR   PIR; T06518; T06518.
DR   AlphaFoldDB; P08926; -.
DR   SMR; P08926; -.
DR   PRIDE; P08926; -.
DR   EnsemblPlants; Psat7g144320.1; Psat7g144320.1.cds; Psat7g144320.
DR   Gramene; Psat7g144320.1; Psat7g144320.1.cds; Psat7g144320.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR   CDD; cd03344; GroEL; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 1.
DR   HAMAP; MF_00600; CH60; 1.
DR   InterPro; IPR018370; Chaperonin_Cpn60_CS.
DR   InterPro; IPR001844; Cpn60/GroEL.
DR   InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR   InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR   InterPro; IPR027413; GROEL-like_equatorial_sf.
DR   InterPro; IPR027410; TCP-1-like_intermed_sf.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   PRINTS; PR00298; CHAPERONIN60.
DR   SUPFAM; SSF48592; SSF48592; 1.
DR   SUPFAM; SSF52029; SSF52029; 1.
DR   SUPFAM; SSF54849; SSF54849; 2.
DR   TIGRFAMs; TIGR02348; GroEL; 1.
DR   PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Chloroplast; Direct protein sequencing;
KW   Nucleotide-binding; Plastid; Transit peptide.
FT   TRANSIT         1..47
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:3549295"
FT   CHAIN           48..587
FT                   /note="RuBisCO large subunit-binding protein subunit alpha,
FT                   chloroplastic"
FT                   /id="PRO_0000005020"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   587 AA;  61979 MW;  94D16822846C8FAE CRC64;
     MASTNALSST SILRSPTNQA QTSLSKKVKQ HGRVNFRQKP NRFVVKAAAK DIAFDQHSRS
     AMQAGIDKLA DAVGLTLGPR GRNVVLDEFG SPKVVNDGVT IARAIELPDP MENAGAALIR
     EVASKTNDSA GDGTTTASIL AREIIKLGLL NVTSGANPVS IKKGIDKTVA ALVEELEKLA
     RPVKGGDDIK AVATISAGND ELIGKMIAEA IDKVGPDGVL SIESSNSFET TVEVEEGMEI
     DRGYISPQFV TNPEKSIVEF ENARVLITDQ KISAIKDIIP LLEKTTQLRA PLLIISEDIT
     GEALATLVVN KLRGILNVAA IKAPGFGERR KALLQDIAIL TGAEFQASDL GLLVENTTIE
     QLGLARKVTI SKDSTTIIAD AASKDELQSR VAQLKKELSE TDSIYDSEKL AERIAKLSGG
     VAVIKVGAAT ETELEDRKLR IEDAKNATFA AIEEGIVPGG GTALVHLSGY VPAIKEKLED
     ADERLGADIV QKALVAPAAL IAQNAGIEGE VVVEKIKNGE WEVGYNAMTD TYENLVESGV
     IDPAKVTRCA LQNAASVAGM VLTTQAIVVE KPKPKAAVAA APQGLTI