ID   CH60_LEITA              Reviewed;          47 AA.
AC   P56281;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Chaperonin HSP60, mitochondrial;
DE            Short=Protein Cpn60;
DE   AltName: Full=Heat shock protein 60;
DE   AltName: Full=groEL protein;
DE   Flags: Precursor; Fragment;
GN   Name=HSP60;
OS   Leishmania tarentolae (Sauroleishmania tarentolae).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania;
OC   lizard Leishmania.
OX   NCBI_TaxID=5689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE, AND PROTEIN SEQUENCE OF 9-18.
RX   PubMed=8719252; DOI=10.1016/0166-6851(95)02486-7;
RA   Bringaud F., Peyruchaud S., Baltz D., Giroud C., Simpson L., Baltz T.;
RT   "Molecular characterization of the mitochondrial heat shock protein 60 gene
RT   from Trypanosoma brucei.";
RL   Mol. Biochem. Parasitol. 74:119-123(1995).
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 matrix {ECO:0000250}.
CC   -!- INDUCTION: By heat shock. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR   AlphaFoldDB; P56281; -.
DR   SMR; P56281; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; Stress response; Transit peptide.
FT   TRANSIT         1..8
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:8719252"
FT   CHAIN           9..>47
FT                   /note="Chaperonin HSP60, mitochondrial"
FT                   /id="PRO_0000005036"
FT   NON_TER         47
SQ   SEQUENCE   47 AA;  5025 MW;  92589CD137336008 CRC64;
     MLRSAVRLAG KDVRFGEDAR RSMQKGVTRA VAAVATTLGP KGRNVII