ID   CH60_SOLTU              Reviewed;          40 AA.
AC   P80502;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Chaperonin HSP60, mitochondrial;
DE   Flags: Fragment;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Tuber;
RX   PubMed=8919912; DOI=10.1046/j.1365-313x.1996.09030357.x;
RA   Jansch L., Kruft V., Schmitz U.K., Braun H.P.;
RT   "New insights into the composition, molecular mass and stoichiometry of the
RT   protein complexes of plant mitochondria.";
RL   Plant J. 9:357-368(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-15.
RC   STRAIN=cv. Romano; TISSUE=Tuber;
RX   PubMed=9729464; DOI=10.1042/bj3340571;
RA   Millar A.H., Knorpp C., Leaver C.J., Hill S.A.;
RT   "Plant mitochondrial pyruvate dehydrogenase complex: purification and
RT   identification of catalytic components in potato.";
RL   Biochem. J. 334:571-576(1998).
CC   -!- FUNCTION: Implicated in mitochondrial protein import and macromolecular
CC       assembly. May facilitate the correct folding of imported proteins. May
CC       also prevent misfolding and promote the refolding and proper assembly
CC       of unfolded polypeptides generated under stress conditions in the
CC       mitochondrial matrix.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- INDUCTION: By heat shock.
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR   AlphaFoldDB; P80502; -.
DR   SMR; P80502; -.
DR   STRING; 4113.PGSC0003DMT400069855; -.
DR   eggNOG; KOG0356; Eukaryota.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   Gene3D; 1.10.560.10; -; 1.
DR   InterPro; IPR027413; GROEL-like_equatorial_sf.
DR   SUPFAM; SSF48592; SSF48592; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Direct protein sequencing; Mitochondrion;
KW   Nucleotide-binding; Reference proteome; Stress response.
FT   CHAIN           1..>40
FT                   /note="Chaperonin HSP60, mitochondrial"
FT                   /id="PRO_0000063629"
FT   NON_TER         40
SQ   SEQUENCE   40 AA;  4240 MW;  1DA86B27029C47FD CRC64;
     AAKDIKFGVE ARGLMLQGVE QLADAVKVTM GPKGRNVVIE