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RuBisCO large subunit-binding protein subunit beta, chloroplastic (60 kDa chaperonin subunit beta) (CPN-60 beta)

 RUBB_PEA                Reviewed;         595 AA.
P08927; Q37267;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
07-NOV-2018, entry version 95.
RecName: Full=RuBisCO large subunit-binding protein subunit beta, chloroplastic;
AltName: Full=60 kDa chaperonin subunit beta;
AltName: Full=CPN-60 beta;
Flags: Precursor;
Pisum sativum (Garden pea).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
50 kb inversion clade; NPAAA clade; Hologalegina; IRL clade; Fabeae;
Pisum.
NCBI_TaxID=3888;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7629128; DOI=10.1074/jbc.270.30.18158;
Viitanen P.V., Schmidt M., Buchner J., Suzuki T., Vierling E.,
Dickson R.R., Lorimer G.H., Gatenby A., Soll J.;
"Functional characterization of the higher plant chloroplast
chaperonins.";
J. Biol. Chem. 270:18158-18164(1995).
[2]
PROTEIN SEQUENCE OF 50-79.
STRAIN=cv. Feltham First;
PubMed=3549295; DOI=10.1111/j.1432-1033.1987.tb10900.x;
Musgrove J.E., Johnson R.A., Ellis R.J.;
"Dissociation of the ribulosebisphosphate-carboxylase large-subunit
binding protein into dissimilar subunits.";
Eur. J. Biochem. 163:529-534(1987).
-!- FUNCTION: This protein binds RuBisCO small and large subunits and
is implicated in the assembly of the enzyme oligomer.
-!- SUBUNIT: Oligomer of probably six alpha and six beta subunits.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast.
-!- MISCELLANEOUS: This protein shows ATPase activity.
-!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
{ECO:0000305}.
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EMBL; U21139; AAA66365.1; -; mRNA.
PIR; T06412; T06412.
ProteinModelPortal; P08927; -.
SMR; P08927; -.
PRIDE; P08927; -.
GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042026; P:protein refolding; IEA:InterPro.
CDD; cd03344; GroEL; 1.
Gene3D; 1.10.560.10; -; 1.
Gene3D; 3.30.260.10; -; 1.
Gene3D; 3.50.7.10; -; 1.
HAMAP; MF_00600; CH60; 1.
InterPro; IPR018370; Chaperonin_Cpn60_CS.
InterPro; IPR001844; Chaprnin_Cpn60.
InterPro; IPR002423; Cpn60/TCP-1.
InterPro; IPR027409; GroEL-like_apical_dom_sf.
InterPro; IPR027413; GROEL-like_equatorial_sf.
InterPro; IPR027410; TCP-1-like_intermed_sf.
Pfam; PF00118; Cpn60_TCP1; 1.
PRINTS; PR00298; CHAPERONIN60.
SUPFAM; SSF48592; SSF48592; 1.
SUPFAM; SSF52029; SSF52029; 1.
SUPFAM; SSF54849; SSF54849; 1.
TIGRFAMs; TIGR02348; GroEL; 1.
PROSITE; PS00296; CHAPERONINS_CPN60; 1.
1: Evidence at protein level;
ATP-binding; Chaperone; Chloroplast; Direct protein sequencing;
Nucleotide-binding; Plastid; Transit peptide.
TRANSIT 1 49 Chloroplast.
{ECO:0000269|PubMed:3549295}.
CHAIN 50 595 RuBisCO large subunit-binding protein
subunit beta, chloroplastic.
/FTId=PRO_0000005024.
CONFLICT 63 63 K -> R (in Ref. 2; AA sequence).
{ECO:0000305}.
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


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