ID   HSP78_SCHPO             Reviewed;         803 AA.
AC   O74402;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Heat shock protein 78, mitochondrial;
DE   Flags: Precursor;
GN   Name=hsp78; ORFNames=SPBC4F6.17c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: Required, in concert with mitochondrial Hsp70, for the
CC       dissociation, resolubilization and refolding of aggregates of damaged
CC       proteins in the mitochondrial matrix after heat stress. May extract
CC       proteins from aggregates by unfolding and threading them in an ATP-
CC       dependent process through the axial channel of the protein hexamer,
CC       after which they can be refolded by the Hsp70 chaperone system.
CC       Required for resumption of mitochondrial respiratory function, DNA
CC       synthesis and morphology after heat stress (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homohexamer, forming a ring with a central pore.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- DOMAIN: Has 2 AAA ATPase type nucleotide-binding domains (NBDs) per
CC       monomer. NBD1 is primarily responsible for ATP hydrolysis. NBD2 is
CC       crucial for oligomerization (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
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DR   EMBL; CU329671; CAA20737.1; -; Genomic_DNA.
DR   PIR; T40514; T40514.
DR   RefSeq; NP_596117.1; NM_001022034.2.
DR   AlphaFoldDB; O74402; -.
DR   SMR; O74402; -.
DR   BioGRID; 277414; 2.
DR   STRING; 4896.SPBC4F6.17c.1; -.
DR   MaxQB; O74402; -.
DR   PaxDb; O74402; -.
DR   PRIDE; O74402; -.
DR   EnsemblFungi; SPBC4F6.17c.1; SPBC4F6.17c.1:pep; SPBC4F6.17c.
DR   GeneID; 2540898; -.
DR   KEGG; spo:SPBC4F6.17c; -.
DR   PomBase; SPBC4F6.17c; hsp78.
DR   VEuPathDB; FungiDB:SPBC4F6.17c; -.
DR   eggNOG; KOG1051; Eukaryota.
DR   HOGENOM; CLU_005070_4_0_1; -.
DR   InParanoid; O74402; -.
DR   OMA; SKMMQGE; -.
DR   PhylomeDB; O74402; -.
DR   PRO; PR:O74402; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005759; C:mitochondrial matrix; ISO:PomBase.
DR   GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISO:PomBase.
DR   GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; ISS:PomBase.
DR   GO; GO:0070370; P:cellular heat acclimation; IBA:GO_Central.
DR   GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR   GO; GO:0042026; P:protein refolding; ISO:PomBase.
DR   GO; GO:0043335; P:protein unfolding; ISO:PomBase.
DR   Gene3D; 3.40.50.300; -; 3.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Coiled coil; Mitochondrion; Nucleotide-binding;
KW   Reference proteome; Repeat; Stress response; Transit peptide.
FT   TRANSIT         1..36
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           37..803
FT                   /note="Heat shock protein 78, mitochondrial"
FT                   /id="PRO_0000372309"
FT   REGION          94..342
FT                   /note="NBD1"
FT                   /evidence="ECO:0000250"
FT   REGION          465..656
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   COILED          343..431
FT                   /evidence="ECO:0000255"
FT   BINDING         139..146
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         539..546
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   803 AA;  90154 MW;  83C5C413DC2B1F12 CRC64;
     MNILPKSIPI RIQSLRRYQG SLKTSLRALS TRPIFEKRLL AETPFSIRPS NASVLIAKRS
     PKFGWKQVRF YAANPNGGNF RMDLGGGRKQ GAALEEYGTD LTALAKQGKL DPVIGREEEI
     QRTIQILSRR TKNNPALVGP AGVGKTAIME GLASRIIRGE VPESMKDKRV IVLDLGALIS
     GAKFRGDFEE RLKSVLSDLE GAEGKVILFV DEMHLLLGFG KAEGSIDASN LLKPALARGK
     LHCCGATTLE EYRKYIEKDA ALARRFQAVM VNEPSVADTI SILRGLKERY EVHHGVRITD
     DALVTAATYS ARYITDRFLP DKAIDLVDEA CSSLRLQQES KPDELRRLDR QIMTIQIELE
     SLRKETDTTS VERREKLESK LTDLKEEQDK LSAAWEEERK LLDSIKKAKT ELEQARIELE
     RTQREGNYAR ASELQYAIIP ELERSVPKEE KTLEEKKPSM VHDSVTSDDI AVVVSRATGI
     PTTNLMRGER DKLLNMEQTI GKKIIGQDEA LKAIADAVRL SRAGLQNTNR PLASFLFLGP
     TGVGKTALTK ALAEFLFDTD KAMIRFDMSE FQEKHTIARL IGSPPGYIGY EESGELTEAV
     RRKPYAVLLF DELEKAHHDI TNLLLQVLDE GFLTDSQGRK VDFRSTLIVM TSNLGSDILV
     ADPSTTVTPK SRDAVMDVVQ KYYPPEFLNR IDDQIVFNKL SEKNLEDIVN VRLDEVQQRL
     NDRRIILTVT EAARKWLAEK GYSPAYGARP LNRLIQKRIL NTMAMKIIQG EIKSDENVVI
     DVLDGELEFK ANKLEPQSTS HED