CPNB2_ARATH
ID CPNB2_ARATH Reviewed; 596 AA.
AC Q9LJE4;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Chaperonin 60 subunit beta 2, chloroplastic;
DE Short=CPN-60 beta 2;
DE Flags: Precursor;
GN Name=CPN60B2; Synonyms=Cpn60-B(2); OrderedLocusNames=At3g13470;
GN ORFNames=MRP15.11;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP FUNCTION, PROTEIN SEQUENCE OF 51-64, AND INTERACTION WITH RAB.
RX PubMed=18353762; DOI=10.1093/jxb/erm343;
RA Salvucci M.E.;
RT "Association of Rubisco activase with chaperonin-60beta: a possible
RT mechanism for protecting photosynthesis during heat stress.";
RL J. Exp. Bot. 59:1923-1933(2008).
RN [4]
RP INDUCTION BY LIGHT.
RX PubMed=12231961; DOI=10.1104/pp.103.2.553;
RA Pilgrim M.L., McClung C.R.;
RT "Differential involvement of the circadian clock in the expression of genes
RT required for ribulose-1,5-bisphosphate carboxylase/oxygenase synthesis,
RT assembly, and activation in Arabidopsis thaliana.";
RL Plant Physiol. 103:553-564(1993).
RN [5]
RP FUNCTION, AND INTERACTION.
RX DOI=10.1074/jbc.270.30.18158;
RA Viitanen P.V., Schmidt M., Buchner J., Suzuki T., Vierling E., Dickson R.,
RA 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 [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11599560; DOI=10.1379/1466-1268(2001)006<0190:attiai>2.0.co;2;
RA Hill J.E., Hemmingsen S.M.;
RT "Arabidopsis thaliana type I and II chaperonins.";
RL Cell Stress Chaperones 6:190-200(2001).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=19344532; DOI=10.1186/1471-2229-9-38;
RA Suzuki K., Nakanishi H., Bower J., Yoder D.W., Osteryoung K.W.,
RA Miyagishima S.Y.;
RT "Plastid chaperonin proteins Cpn60 alpha and Cpn60 beta are required for
RT plastid division in Arabidopsis thaliana.";
RL BMC Plant Biol. 9:38-38(2009).
RN [8]
RP FUNCTION, AND IDENTIFICATION IN CPN60 COMPLEX.
RX PubMed=19224397; DOI=10.1007/s12192-009-0104-2;
RA Bonshtien A.L., Parnas A., Sharkia R., Niv A., Mizrahi I., Azem A.,
RA Weiss C.;
RT "Differential effects of co-chaperonin homologs on cpn60 oligomers.";
RL Cell Stress Chaperones 14:509-519(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [10]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=21483722; DOI=10.1371/journal.pbio.1001040;
RA Peng L., Fukao Y., Myouga F., Motohashi R., Shinozaki K., Shikanai T.;
RT "A chaperonin subunit with unique structures is essential for folding of a
RT specific substrate.";
RL PLoS Biol. 9:E1001040-E1001040(2011).
CC -!- FUNCTION: Involved in protein assisted folding.
CC {ECO:0000269|PubMed:18353762, ECO:0000269|PubMed:19224397,
CC ECO:0000269|PubMed:19344532, ECO:0000269|Ref.5}.
CC -!- SUBUNIT: Part of the Cpn60 complex composed of 7 alpha and 7 beta
CC subunits. Can also form a complex composed of 14 beta subunits only.
CC Both complexes show ATPase activity. The Cpn60 complex interacts with
CC the Cpn10 complex. Interacts with RAB during heat stress.
CC {ECO:0000269|PubMed:18353762, ECO:0000269|PubMed:19224397,
CC ECO:0000269|Ref.5}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:19344532}.
CC -!- INDUCTION: Up-regulated by light. {ECO:0000269|PubMed:12231961}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype; due to redundancy with
CC CPN60B1. Cpn60B1 and cpn60B2 double mutant produces small albino
CC seedlings. {ECO:0000269|PubMed:19344532}.
CC -!- MISCELLANEOUS: Assisted protein folding requires ATP hydrolysis, but
CC not K(+) ions.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR EMBL; AP000603; BAB01754.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75362.1; -; Genomic_DNA.
DR PIR; PS0374; PS0374.
DR RefSeq; NP_187956.1; NM_112193.4.
DR AlphaFoldDB; Q9LJE4; -.
DR SMR; Q9LJE4; -.
DR BioGRID; 5883; 27.
DR IntAct; Q9LJE4; 2.
DR MINT; Q9LJE4; -.
DR STRING; 3702.AT3G13470.1; -.
DR iPTMnet; Q9LJE4; -.
DR MetOSite; Q9LJE4; -.
DR PaxDb; Q9LJE4; -.
DR PRIDE; Q9LJE4; -.
DR ProteomicsDB; 224488; -.
DR EnsemblPlants; AT3G13470.1; AT3G13470.1; AT3G13470.
DR GeneID; 820549; -.
DR Gramene; AT3G13470.1; AT3G13470.1; AT3G13470.
DR KEGG; ath:AT3G13470; -.
DR Araport; AT3G13470; -.
DR TAIR; locus:2092825; AT3G13470.
DR eggNOG; KOG0356; Eukaryota.
DR HOGENOM; CLU_016503_4_1_1; -.
DR InParanoid; Q9LJE4; -.
DR OMA; NPEVGNM; -.
DR OrthoDB; 415781at2759; -.
DR PhylomeDB; Q9LJE4; -.
DR PRO; PR:Q9LJE4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LJE4; baseline and differential.
DR Genevisible; Q9LJE4; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
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:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
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; Coiled coil;
KW Direct protein sequencing; Nucleotide-binding; Phosphoprotein; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..50
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:18353762"
FT CHAIN 51..596
FT /note="Chaperonin 60 subunit beta 2, chloroplastic"
FT /id="PRO_0000413684"
FT COILED 388..489
FT /evidence="ECO:0000255"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21238"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 596 AA; 63342 MW; B99C3825AB0BC15F CRC64;
MASTFTATSS LGSLLAPNAI KLSSATSISS SSFGRRHNVC VRRSRPAIVC AAKELHFNKD
GTTIRKLQTG VNKLADLVGV TLGPKGRNVV LESKYGSPRI VNDGVTVARE VELEDPVENI
GAKLVRQAAA KTNDLAGDGT TTSVVLAQGF IAEGVKVVAA GANPVLITRG IEKTAKALVN
ELKLMSKEVE DSELADVAAV SAGNNHEVGS MIAEAMSKVG RKGVVTLEEG KSAENNLYVV
EGMQFDRGYI SPYFVTDSEK MSVEYDNCKL LLVDKKVTNA RDLVGVLEDA IRGGYPILII
AEDIEQEALA TLVVNKLRGT LKIAALKAPG FGERKSQYLD DIAILTGATV IREEVGLSLD
KAGKEVLGNA SKVVLTKEMT TIVGDGTTQE AVNKRVVQIR NLIEQAEQDY EKEKLNERIA
KLSGGVAVIQ VGAQTETELK EKKLRVEDAL NATKAAVEEG IVVGGGCTLL RLASKVDAIK
DTLENDEEKV GAEIVKRALS YPLKLIAKNA GVNGSVVSEK VLANDNVKFG YNAATGKYED
LMAAGIIDPT KVVRCCLEHA ASVAKTFLMS DCVVVEIPEP EPVPAGNPMD NSGYGY
