ID   HSP7M_DICDI             Reviewed;         658 AA.
AC   Q8I0H7; Q54BY7;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Heat shock 70 kDa protein, mitochondrial;
DE   AltName: Full=75 kDa glucose-regulated protein homolog;
DE            Short=GRP-75;
DE   Flags: Precursor;
GN   Name=mhsp70; Synonyms=hsp70; ORFNames=DDB_G0293298;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA   Maroun M., Barth C.;
RT   "Identification and cDNA cloning of the nuclear-encoded mitochondrial Hsp70
RT   in Dictyostelium discoideum.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [3]
RP   PROTEIN SEQUENCE OF 63-99; 124-134; 184-215; 272-284; 446-462; 480-490 AND
RP   524-550, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=AX2;
RA   Bienvenut W.V., Ura S., Insall R.H.;
RL   Submitted (JUL-2009) to UniProtKB.
CC   -!- FUNCTION: May function in protein folding and assembly, and disassembly
CC       of protein complexes. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; AF539617; AAN23118.1; -; mRNA.
DR   EMBL; AY170440; AAO12054.1; -; Genomic_DNA.
DR   EMBL; AAFI02000201; EAL60773.1; -; Genomic_DNA.
DR   RefSeq; XP_629204.1; XM_629202.1.
DR   AlphaFoldDB; Q8I0H7; -.
DR   SMR; Q8I0H7; -.
DR   STRING; 44689.DDB0215366; -.
DR   PaxDb; Q8I0H7; -.
DR   EnsemblProtists; EAL60773; EAL60773; DDB_G0293298.
DR   GeneID; 8629163; -.
DR   KEGG; ddi:DDB_G0293298; -.
DR   dictyBase; DDB_G0293298; mhsp70.
DR   eggNOG; KOG0102; Eukaryota.
DR   HOGENOM; CLU_005965_2_4_1; -.
DR   InParanoid; Q8I0H7; -.
DR   OMA; ISIKRHM; -.
DR   PhylomeDB; Q8I0H7; -.
DR   PRO; PR:Q8I0H7; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0031012; C:extracellular matrix; HDA:dictyBase.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR   GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR   GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 2.60.34.10; -; 1.
DR   HAMAP; MF_00332; DnaK; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR012725; Chaperone_DnaK.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR029048; HSP70_C_sf.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375; PTHR19375; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF100920; SSF100920; 1.
DR   SUPFAM; SSF100934; SSF100934; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   TIGRFAMs; TIGR02350; prok_dnaK; 1.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Direct protein sequencing; Mitochondrion;
KW   Nucleotide-binding; Reference proteome; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT   CHAIN           ?..658
FT                   /note="Heat shock 70 kDa protein, mitochondrial"
FT                   /id="PRO_0000327975"
FT   REGION          629..658
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        640..658
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   658 AA;  71362 MW;  6B4D385EA68A5B20 CRC64;
     MLRSLKALKL NSLNAQKGIR QFCSDSKISG QVIGIDLGTT NSCVAVMQGA EARVLENAEG
     GRTTPSVVAF TEDNQKIVGL PAKRQMVTNA ENTLFATKRL IGRRFDDPMT KKDMTMVPYK
     IVKGPNGDAW FEVKGKMISP SEAGAMVLQK MKETAETNLG GPVTDAVITV PAYFDDSQRQ
     ATRDAGTIAG LKVQRIINEP TAAALAYGFK KDEPKTVAVY DLGGGTFDIS ILEIVGGVFE
     VRATNGDTFL GGEDFDNALL EHFVAEFKKE KGIDLTKDTM ATQRLREAAE KAKCELSSTL
     TTEINLPYIS AGPSGPVHFN MKLTRSKFEQ LVADLIQRTI GPCNICLKDA GLSTSEINEV
     ILVGGMTRMP KVQELAKSTF NKEPFKGVNP DEAVAVGAAI QGGVLKGDTK GIVLVDVTPL
     SLGIETLGGV FTRLIKKNTN IPASKTDTFS TAADGQSEVE IKVFQGEREM AVDNKLLAKF
     TLFGLPPLPK GVPQIEVTFD IDVNGMLQVI AKDKATGKAQ QVRIQTSGGL SKDDIARILK
     ESEANAEVDR KRKELVEARN NGESVVYQVE KDLVEFKDYL SQPQTEEIKK AVQAVRDVLA
     KEDGSAIEAE IKKLHDLTRS SFETAYKAKL DSSASKSSST ENKENKDNTT EAEFTEKK