ID   RUBB_PEA                Reviewed;         595 AA.
AC   P08927; Q37267;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=RuBisCO large subunit-binding protein subunit beta, chloroplastic;
DE   AltName: Full=60 kDa chaperonin subunit beta;
DE   AltName: Full=CPN-60 beta;
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 50-79.
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; U21139; AAA66365.1; -; mRNA.
DR   PIR; T06412; T06412.
DR   AlphaFoldDB; P08927; -.
DR   SMR; P08927; -.
DR   PRIDE; P08927; -.
DR   EnsemblPlants; Psat1g001680.1; Psat1g001680.1.cds; Psat1g001680.
DR   Gramene; Psat1g001680.1; Psat1g001680.1.cds; Psat1g001680.
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; 1.
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..49
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:3549295"
FT   CHAIN           50..595
FT                   /note="RuBisCO large subunit-binding protein subunit beta,
FT                   chloroplastic"
FT                   /id="PRO_0000005024"
FT   CONFLICT        63
FT                   /note="K -> R (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   595 AA;  62984 MW;  E5153B532A0D89E7 CRC64;
     MASTFSATTS SCNLSSSAAI SSFPLAAGKR NANKVVLPRK NRNVKVSAMA KELHFNKDGS
     AIKKLQNGVN KLADLVGVTL GPKGRNVVLE SKYGSPKIVN DGVTVAKEVE LEDPVENIGA
     KLVRQAAAKT NDLAGDGTTT SVVLAQGLIA EGVKVVAAGA NPVLITRGIE KTSKALVAEL
     KKMSKEVEDS ELADVAAVSA GNNHEVGNMI AEALSKVGRK GVVTLEEGKS AENSLYVVEG
     MQFDRGYISP YFVTDSEKMT VEFENCKLLL VDKKITNARD LINILEDAIR SGFPIVIIAE
     DIEQEALATL VVNKLRGSLK IAALKAPGFG ERKSQYLDDI AILTGGTVIR EEVGLTLDKA
     DKEVLGNAAK VVLTKDTTTI VGDGSTQEAV NKRVSQIKNQ IEAAEQEYEK EKLSERIAKL
     SGGVAVIQVG AQTETELKEK KLRVEDALNA TKAAVEEGIV VGGGCTLLRL ASKVDAIKDT
     LANDEEKVGA DIVKRALSYP LKLIAKNAGV NGSVVSEKVL SSDNPKYGYN AATGKYEDLM
     AAGIIDPTKV VRCCLEHASS VAKTFLMSDC VVVEIKEPES APVGNPMDNS GYGNI