ID   CH60_TRYBB              Reviewed;         562 AA.
AC   Q37683;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   14-AUG-2001, sequence version 2.
DT   03-AUG-2022, entry version 99.
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;
GN   Name=HSP60;
OS   Trypanosoma brucei brucei.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=5702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=EATRO 164;
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).
RN   [2]
RP   SEQUENCE REVISION TO C-TERMINUS.
RA   Bringaud F., Peyruchaud S., Baltz D., Giroud C., Simpson L., Baltz T.;
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
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   -!- DEVELOPMENTAL STAGE: More abundant in the procyclic forms than in the
CC       bloodstream forms.
CC   -!- INDUCTION: By heat shock. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR   EMBL; L43797; AAC37260.3; -; mRNA.
DR   AlphaFoldDB; Q37683; -.
DR   SMR; Q37683; -.
DR   PRIDE; Q37683; -.
DR   GO; GO:0005929; C:cilium; IDA:GeneDB.
DR   GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:GeneDB.
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:0051082; F:unfolded protein binding; ISA:GeneDB.
DR   GO; GO:0006457; P:protein folding; ISA:GeneDB.
DR   GO; GO:0030150; P:protein import into mitochondrial matrix; ISA:GeneDB.
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   HAMAP; MF_00600; CH60; 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   PRINTS; PR00298; CHAPERONIN60.
DR   SUPFAM; SSF48592; SSF48592; 1.
DR   SUPFAM; SSF52029; SSF52029; 1.
DR   SUPFAM; SSF54849; SSF54849; 1.
DR   TIGRFAMs; TIGR02348; GroEL; 1.
DR   PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Mitochondrion; Nucleotide-binding; Stress response;
KW   Transit peptide.
FT   TRANSIT         1..8
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           9..562
FT                   /note="Chaperonin HSP60, mitochondrial"
FT                   /id="PRO_0000005038"
SQ   SEQUENCE   562 AA;  59529 MW;  575B55F2B2C1E8EF CRC64;
     MFRCVVRFGA KDIRFGTEAR QSMLKGVQRA VEAVATTLGP KGRNVIIEQS YGAPKITKDG
     VTVAKSIEFK DPFENMGAQL VRQVCNKTND LAGDGTTTSA VLVASIFSEG IKSIATGTNP
     IDMKRGMDRA VEVILKNIES QSRTVTNTEN VVQVATISAN GDVELGKLIG EAMEKVGKDG
     VITTQDGKTL TTELEVVEGM SVDRGYISPY FVTDAKTQKA ELEDAFVLVS AKKLNNIHTI
     LPVLNHVVRS GRPLLIIADD VESEALTTMI FNKLQGKLKI ACVKAPGFGD NKAAMLQDIA
     IFSGACVVGE EGSGVELDAE KFEASILGSV KKATITKDDT VLLNGGGDVA MMKERVDLVR
     GLIERETSDY NREKLQERLA KLSGGVAVIR VGGASEVEVN EKKDRITDAL CSTRAAVQEG
     IVPGGGPALL RASKALDGLL QDQSLTADQR TGVQIIRNAV RLPAHRIVAN AGREGAVVVE
     KVLENTDAAV GYDAQLDRYV NMFEAGIIDP ARVVRVALTD AASVASLMMT AEAAVVDLPK
     DDAPAAGGMG GMGGMGGMDG MY