RUBB_POPEU
ID RUBB_POPEU Reviewed; 24 AA.
AC P84581;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 29.
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: Fragments;
OS Populus euphratica (Euphrates poplar).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=75702;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Leaf;
RX PubMed=16740589; DOI=10.1093/aob/mcl106;
RA Ferreira S., Hjernoe K., Larsen M., Wingsle G., Larsen P., Fey S.,
RA Roepstorff P., Pais M.S.;
RT "Proteome profiling of Populus euphratica Oliv. upon heat stress.";
RL Ann. Bot. 98:361-377(2006).
CC -!- FUNCTION: This protein binds RuBisCO small and large subunits and is
CC implicated in the assembly of the enzyme oligomer. {ECO:0000305}.
CC -!- SUBUNIT: Oligomer of probably six alpha and six beta subunits.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- MISCELLANEOUS: This protein shows ATPase activity. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000255}.
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DR AlphaFoldDB; P84581; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Chloroplast; Direct protein sequencing;
KW Nucleotide-binding; Plastid.
FT CHAIN <1..>24
FT /note="RuBisCO large subunit-binding protein subunit beta,
FT chloroplastic"
FT /id="PRO_0000063633"
FT NON_CONS 13..14
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 24
SQ SEQUENCE 24 AA; 2519 MW; 78D1DE1DAA695955 CRC64;
VVAAGANPVL ITRDLVNVLE DAIR