ID   RUBB_CHLRE              Reviewed;         435 AA.
AC   Q42693;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=RuBisCO large subunit-binding protein subunit beta-1;
DE   AltName: Full=60 kDa chaperonin subunit beta-1;
DE   AltName: Full=CPN-60 beta-1;
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}.
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DR   EMBL; L27471; AAA98641.1; -; mRNA.
DR   PIR; S56644; S56644.
DR   AlphaFoldDB; Q42693; -.
DR   SMR; Q42693; -.
DR   STRING; 3055.EDO97815; -.
DR   ProMEX; Q42693; -.
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   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   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   SUPFAM; SSF48592; SSF48592; 1.
DR   SUPFAM; SSF52029; SSF52029; 1.
DR   SUPFAM; SSF54849; SSF54849; 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..435
FT                   /note="RuBisCO large subunit-binding protein subunit beta-
FT                   1"
FT                   /id="PRO_0000063631"
FT   NON_TER         1
SQ   SEQUENCE   435 AA;  46836 MW;  A9F3EFA1AC2F79D6 CRC64;
     KSGMEKTVQE LVKELRKMSS VVQTDKDLAN VACVSAGGNT DIGSLISDAM AKVGRTGVVT
     MEEGKTAEDQ LVFVEGMQFE RGYTSPYFVT DPERMICEYE NCKILLVDKK ISTARDIITI
     LESAIRGNYP LLIMAEEVEQ EALATLVVNK LRGTLKVVAI KAPGFGERRS SYLEDIAILT
     GGTVVGDEMG VSLEQATDAV LGTAAKITIT KERTTVVGDG STAADVAARV KQIRNLQMQT
     DQDYEREKLQ ERIARLSGGV AIIQVGAQTE TELKEKKLRV EDALNATRAA VEEGVVPGGG
     CTLLRLSEKV DVIKRRMTDP EQQMGADIIK RALCYPIKLI AQNAGVNGSV VMNEVMKNLD
     RPHYGYNAAT DSFENLMETG IIDPSKVVRC SMENAVSVAK TFLLADVVVT ELKEIEAGAK
     PNPVAPGAAG FGGGL