ID   CH10C_POPEU             Reviewed;          53 AA.
AC   P84579;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=20 kDa chaperonin;
DE   AltName: Full=Chloroplast chaperonin 10;
DE            Short=Ch-Cpn10;
DE            Short=Chloroplast Cpn10;
DE   AltName: Full=Protein Cpn21;
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] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RC   TISSUE=Leaf {ECO:0000269|PubMed:16740589};
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).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 30-52.
RC   TISSUE=Leaf {ECO:0000269|Ref.2};
RA   Ferreira S.;
RT   "Molecular analysis of Populus euphratica Oliv. response to moderate heat
RT   stress.";
RL   Thesis (2006), ICAT-FCUL, Portugal.
CC   -!- FUNCTION: Seems to function only as a co-chaperone, along with cpn60,
CC       and in certain cases is essential for the discharge of biologically
CC       active proteins from cpn60. {ECO:0000250}.
CC   -!- SUBUNIT: Forms stable complexes with cpn60 in the presence of ATP.
CC       Homotetramer (By similarity). {ECO:0000250|UniProtKB:O65282}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GroES chaperonin family. {ECO:0000305}.
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DR   AlphaFoldDB; P84579; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   CDD; cd00320; cpn10; 1.
DR   Gene3D; 2.30.33.40; -; 1.
DR   InterPro; IPR020818; Chaperonin_GroES.
DR   InterPro; IPR037124; Chaperonin_GroES_sf.
DR   InterPro; IPR011032; GroES-like_sf.
DR   PANTHER; PTHR10772; PTHR10772; 1.
DR   Pfam; PF00166; Cpn10; 1.
DR   PRINTS; PR00297; CHAPERONIN10.
DR   SMART; SM00883; Cpn10; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
PE   1: Evidence at protein level;
KW   Chaperone; Chloroplast; Direct protein sequencing; Plastid; Repeat.
FT   CHAIN           <1..>53
FT                   /note="20 kDa chaperonin"
FT                   /id="PRO_0000174926"
FT   REGION          <1..>10
FT                   /note="Cpn-10 domain 1"
FT                   /evidence="ECO:0000250|UniProtKB:O65282"
FT   REGION          <11..>53
FT                   /note="Cpn-10 domain 2"
FT                   /evidence="ECO:0000250|UniProtKB:O65282"
FT   CONFLICT        44
FT                   /note="S -> P (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        50..52
FT                   /note="KIT -> NRK (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   NON_CONS        10..11
FT                   /evidence="ECO:0000303|PubMed:16740589"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:16740589"
FT   NON_TER         53
FT                   /evidence="ECO:0000303|PubMed:16740589"
SQ   SEQUENCE   53 AA;  5469 MW;  DF6A1F105BF6A638 CRC64;
     YTSIKPLGDR VAEAEEKTAG GLLLTETTKE KPSIGTVIAV GPGSLDEEGK ITP