ID   TCM62_YEAST             Reviewed;         572 AA.
AC   P38228; D6VQ44; Q9Y793;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 2.
DT   04-NOV-2026, entry version 180.
DE   RecName: Full=Mitochondrial chaperone TCM62;
DE   Flags: Precursor;
GN   Name=TCM62; OrderedLocusNames=YBR044C; ORFNames=YBR0414;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, SUBCELLULAR LOCATION,
RP   AND TOPOLOGY.
RC   STRAIN=S288c / GRF88;
RX   PubMed=9822678; DOI=10.1074/jbc.273.48.32042;
RA   Dibrov E., Fu S., Lemire B.D.;
RT   "The Saccharomyces cerevisiae TCM62 gene encodes a chaperone necessary for
RT   the assembly of the mitochondrial succinate dehydrogenase (complex II).";
RL   J. Biol. Chem. 273:32042-32048(1998).
RN   [2]
RP   SEQUENCE REVISION TO 566.
RA   Lemire B.D.;
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [4]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 566.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   CHARACTERIZATION.
RX   PubMed=10745098; DOI=10.1016/s0014-5793(00)01322-3;
RA   Klanner C., Neupert W., Langer T.;
RT   "The chaperonin-related protein Tcm62p ensures mitochondrial gene
RT   expression under heat stress.";
RL   FEBS Lett. 470:365-369(2000).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 76625 / YPH499;
RX   PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA   Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA   Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA   Pfanner N., Meisinger C.;
RT   "The proteome of Saccharomyces cerevisiae mitochondria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
CC   -!- FUNCTION: Chaperone. Required for the assembly of succinate
CC       dehydrogenase subunits. Ensures mitochondrial gene expression at
CC       elevated temperatures and prevents heat-aggregation of the ribosomal
CC       subunit VAR1.
CC   -!- SUBUNIT: Forms a high molecular mass protein complex of approximately
CC       850 kDa.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:9822678}; Single-pass
CC       membrane protein {ECO:0000269|PubMed:14576278,
CC       ECO:0000269|PubMed:9822678}; Matrix side {ECO:0000269|PubMed:14576278,
CC       ECO:0000269|PubMed:9822678}.
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA84986.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF125155; AAD24466.1; -; Genomic_DNA.
DR   EMBL; Z35913; CAA84986.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; BK006936; DAA07164.2; -; Genomic_DNA.
DR   PIR; S45902; S45902.
DR   RefSeq; NP_009600.2; NM_001178392.2.
DR   AlphaFoldDB; P38228; -.
DR   SMR; P38228; -.
DR   BioGRID; 32745; 111.
DR   DIP; DIP-2609N; -.
DR   FunCoup; P38228; 154.
DR   IntAct; P38228; 4.
DR   MINT; P38228; -.
DR   STRING; 4932.YBR044C; -.
DR   PaxDb; 4932-YBR044C; -.
DR   PeptideAtlas; P38228; -.
DR   EnsemblFungi; YBR044C_mRNA; YBR044C; YBR044C.
DR   GeneID; 852332; -.
DR   KEGG; sce:YBR044C; -.
DR   AGR; SGD:S000000248; -.
DR   SGD; S000000248; TCM62.
DR   VEuPathDB; FungiDB:YBR044C; -.
DR   eggNOG; KOG0356; Eukaryota.
DR   HOGENOM; CLU_485763_0_0_1; -.
DR   InParanoid; P38228; -.
DR   OMA; ACQQDNI; -.
DR   OrthoDB; 4056908at2759; -.
DR   BioCyc; YEAST:G3O-29017-MONOMER; -.
DR   BioGRID-ORCS; 852332; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P38228; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P38228; protein.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IBA:GO_Central.
DR   GO; GO:0051131; P:chaperone-mediated protein complex assembly; ISS:SGD.
DR   GO; GO:0034553; P:mitochondrial respiratory chain complex II assembly; IMP:SGD.
DR   GO; GO:0034514; P:mitochondrial unfolded protein response; IBA:GO_Central.
DR   GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0045041; P:protein import into mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR   Gene3D; 3.50.7.10; GroEL; 1.
DR   Gene3D; 1.10.560.10; GroEL-like equatorial domain; 1.
DR   InterPro; IPR001844; Cpn60/GroEL.
DR   InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR   InterPro; IPR027413; GROEL-like_equatorial_sf.
DR   PANTHER; PTHR45633; 60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL; 1.
DR   SUPFAM; SSF52029; GroEL apical domain-like; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Nucleotide-binding; Reference proteome;
KW   Stress response; Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..16
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..572
FT                   /note="Mitochondrial chaperone TCM62"
FT                   /id="PRO_0000063639"
FT   TOPO_DOM        17..471
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        472..488
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        489..572
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   572 AA;  64252 MW;  1AAE3CD22AD8D5BD CRC64;
     MLRNCLRKLG NHQTKCSVKT LHTPIYRTKN LQVLRDTLSG IKLLEKIITS SSYNKTLIYE
     PKYKSKPQVV SSHDTMRLHN VMRELLDSLQ VDEATNTRLQ SNRPRKLGRV GLQLFMDCIQ
     DNLTATSTSL TCSLLEHYFK YPEKEVTNGI KAGLRYIRDF LAKNKIIVKS QNDVDALVEQ
     LTMSSSDSQS IKRVLKAINY ELFSDDIVRV INGNKTYDEV DVSKGWKYPA GILDSNEAYL
     RSLELPTKKL VSIDKDMLVL MYDGTLRDAN KILPTITYAR KLRKSVLLIV NGDCTGDALT
     SVTINNNRNK RENNESRIVV LKYSKKANND LAPQENLDFI KFLRLPCGYD SIYSPEYSPL
     VPSKMCADKY YGSIESIKAT TGEAFLYNSI DAEAIPNKVP KSFLQNTVTL SIGGHNEIEI
     DRRRNAIDNC LNNVLCHGLA KGFIPGYGIS LLKAIPGLNE LKANEPNFMT KVGINAVLSA
     VILPSEVAFK NAYGYNYYEI NSLIAGAINE KSFPMAKFSP NSEPVNTVKD GNLEPWSKMD
     SCLAGVETFI ELLTSCNTII TCVYKKPERH KA
//