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RUBB_BRANA
ID   RUBB_BRANA              Reviewed;         588 AA.
AC   P21241;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   03-AUG-2022, entry version 100.
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   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Westar;
RX   PubMed=1979547; DOI=10.1016/0378-1119(90)90385-5;
RA   Martel R., Cloney L.P., Pelcher L.E., Hemmingsen S.M.;
RT   "Unique composition of plastid chaperonin-60: alpha and beta polypeptide-
RT   encoding genes are highly divergent.";
RL   Gene 94:181-187(1990).
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; M35600; AAA32980.1; -; mRNA.
DR   PIR; PW0007; PW0007.
DR   AlphaFoldDB; P21241; -.
DR   SMR; P21241; -.
DR   PRIDE; P21241; -.
DR   EnsemblPlants; CDY02438; CDY02438; GSBRNA2T00114056001.
DR   Gramene; CDY02438; CDY02438; GSBRNA2T00114056001.
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   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Chloroplast; Nucleotide-binding; Phosphoprotein;
KW   Plastid; Transit peptide.
FT   TRANSIT         1..55
FT                   /note="Chloroplast"
FT   CHAIN           56..588
FT                   /note="RuBisCO large subunit-binding protein subunit beta,
FT                   chloroplastic"
FT                   /id="PRO_0000005023"
FT   MOD_RES         101
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P21238"
FT   MOD_RES         478
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P21240"
SQ   SEQUENCE   588 AA;  62473 MW;  EFE721105C436B3F CRC64;
     MASTFTATSS IGSMVAPNAH KTDKKLMNKL SSSSFGRRQN VFPKLRRSSP AVVCAAKELH
     FNKDGTTIRK LQAGVNKLAD LVGVTLGPKG RNVVLESKYG SPRIVNDGVT VAREVELEDP
     VENIGAKLVR QAAAKTNDLA GDGTTTSVVL AQGFIAEGVK VVAAGANPVL ITRGIEKTAK
     ALVAELKKMS KEVEDSELAD VAAVSAGNNA EIGSMIAEAM SRVGRKGVVT LEEGKSAENA
     LYVVEGMQFD RGYVSPYFVT DSEKMSVEFD NCKLLLVDKK ITNARDLVGV LEDAIRGGYP
     ILIIAEDIEQ EALATLVVNK LRGTLKIAAL KAPGFGERKS QYLDDIAILT GATVIREEVG
     LSLDKAGKEV LGHAAKVVLT KETSTIVGDG STQDAVQKRV TQIKNLIEQA EQDYEKEKLN
     ERIAKLSGGV AVIQVGAQTE TELKEKKLRV EDALNATKAA VEEGIVVGGG CTLLRLASKV
     DAIKAALDND EEKVGADIVK RALSYPLKLI AKNAGVNGSV VSEKVLSNDN VKFGYNAATG
     KYEDLMAAGI IDPTKVVRCC LEHAASVAKT FLMSDCVVVE IKEPEPVP
 
 
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