ID   RUBC_CHLRE              Reviewed;         259 AA.
AC   Q42695;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=RuBisCO large subunit-binding protein subunit beta-2;
DE   AltName: Full=60 kDa chaperonin subunit beta-2;
DE   AltName: Full=CPN-60 beta-2;
DE   Flags: Fragment;
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7766872; DOI=10.1007/bf00037029;
RA   Thompson M.D., Paavola C.D., Lenvik T.R., Gantt J.S.;
RT   "Chlamydomonas transcripts encoding three divergent plastid chaperonins are
RT   heat-inducible.";
RL   Plant Mol. Biol. 27:1031-1035(1995).
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   -!- INDUCTION: By heat shock.
CC   -!- MISCELLANEOUS: This protein shows ATPase activity.
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L27473; AAA98643.1; -; mRNA.
DR   PIR; S56646; S56646.
DR   AlphaFoldDB; Q42695; -.
DR   SMR; Q42695; -.
DR   STRING; 3055.EDP03982; -.
DR   PRIDE; Q42695; -.
DR   ProMEX; Q42695; -.
DR   EnsemblPlants; PNW81012; PNW81012; CHLRE_07g339150v5.
DR   Gramene; PNW81012; PNW81012; CHLRE_07g339150v5.
DR   eggNOG; KOG0356; Eukaryota.
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   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 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   PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Chloroplast; Nucleotide-binding; Plastid;
KW   Stress response.
FT   CHAIN           <1..259
FT                   /note="RuBisCO large subunit-binding protein subunit beta-
FT                   2"
FT                   /id="PRO_0000063632"
FT   NON_TER         1
SQ   SEQUENCE   259 AA;  27800 MW;  E7B52E2676B87473 CRC64;
     SSYLEDIAIL TGGTVVKDEL GITLEKATEE VLGLAAKVSI SKEATTIVGD GRTQQQVEGR
     VKQIRNLAAE TEQEYEKEKL NERIARLSGG VAIIQVGAQT ETELKEKKLR VEDALNATKA
     AVEEGIVIGG GCTLLRLSQK VDSIKETLSN EEQKMGADII KRALSYPIKL IANNAGTNGS
     VVMQRVMDNI DQPYYGYNAA TDTFEDLMEA GIIDPTKVVR CSLENAVSVA KTFLLADVVV
     TEIPEKEKAP APAAGGGDY