ID   HSP77_YEAST             Reviewed;         654 AA.
AC   P12398;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   01-SEP-2009, entry version 103.
DE   RecName: Full=Heat shock protein SSC1, mitochondrial;
DE   AltName: Full=mtHSP70;
DE   AltName: Full=Endonuclease SceI 75 kDa subunit;
DE            Short=Endo.SceI 75 kDa subunit;
DE   Flags: Precursor;
GN   Name=SSC1; Synonyms=ENS1; OrderedLocusNames=YJR045C; ORFNames=J1639;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 24657 / D273-10B;
RX   MEDLINE=89384560; PubMed=2674677;
RA   Craig E.A., Kramer J., Shilling J., Werner-Washburne M., Holmes S.,
RA   Kosic-Smithers J., Nicolet C.M.;
RT   "SSC1, an essential member of the yeast HSP70 multigene family,
RT   encodes a mitochondrial protein.";
RL   Mol. Cell. Biol. 9:3000-3008(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 24-41.
RC   STRAIN=IAM 4274;
RX   MEDLINE=90368701; PubMed=2203771;
RA   Morishima N., Nakagawa K., Yamamoto E., Shibata T.;
RT   "A subunit of yeast site-specific endonuclease SceI is a mitochondrial
RT   version of the 70-kDa heat shock protein.";
RL   J. Biol. Chem. 265:15189-15197(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   MEDLINE=95397595; PubMed=7668047; DOI=10.1002/yea.320110809;
RA   Huang M.-E., Chuat J.-C., Galibert F.;
RT   "Analysis of a 42.5 kb DNA sequence of chromosome X reveals three tRNA
RT   genes and 14 new open reading frames including a gene most probably
RT   belonging to the family of ubiquitin-protein ligases.";
RL   Yeast 11:775-781(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   MEDLINE=96208490; PubMed=8641269;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N.,
RA   Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H.,
RA   Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A.,
RA   Hennemann A., Herbert C.J., Heumann K., Hilger F., Hollenberg C.P.,
RA   Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L.,
RA   Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V.,
RA   Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M.,
RA   Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W.,
RA   Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M.,
RA   Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A.,
RA   Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M.,
RA   Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [5]
RP   PROTEIN SEQUENCE OF 24-38.
RX   MEDLINE=91092254; PubMed=2265609;
RA   Scherer P.E., Krieg U.C., Hwang S.T., Vestweber D., Schatz G.;
RT   "A precursor protein partly translocated into yeast mitochondria is
RT   bound to a 70 kd mitochondrial stress protein.";
RL   EMBO J. 9:4315-4322(1990).
RN   [6]
RP   IDENTIFICATION IN ENDONUCLEASE SCEI, AND FUNCTION OF ENDONUCLEASE
RP   SCEI.
RX   PubMed=2828049; DOI=10.1111/j.1432-1033.1988.tb13753.x;
RA   Nakagawa K., Hashikawa J., Makino O., Ando T., Shibata T.;
RT   "Subunit structure of a yeast site-specific endodeoxyribonuclease,
RT   endo SceI. A study using monoclonal antibodies.";
RL   Eur. J. Biochem. 171:23-29(1988).
RN   [7]
RP   FUNCTION OF ENDONUCLEASE SCEI.
RX   PubMed=7625280; DOI=10.1016/0065-227X(95)99384-2;
RA   Shibata T., Nakagawa K., Morishima N.;
RT   "Multi-site-specific endonucleases and the initiation of homologous
RT   genetic recombination in yeast.";
RL   Adv. Biophys. 31:77-91(1995).
RN   [8]
RP   INTERACTION WITH ENS2, AND FUNCTION IN ENDONUCLEASE SCEI.
RX   PubMed=10464305; DOI=10.1074/jbc.274.36.25682;
RA   Mizumura H., Shibata T., Morishima N.;
RT   "Stable association of 70-kDa heat shock protein induces latent
RT   multisite specificity of a unisite-specific endonuclease in yeast
RT   mitochondria.";
RL   J. Biol. Chem. 274:25682-25690(1999).
RN   [9]
RP   FUNCTION.
RX   PubMed=10779357; DOI=10.1128/MCB.20.10.3677-3684.2000;
RA   Voisine C., Schilke B., Ohlson M., Beinert H., Marszalek J.,
RA   Craig E.A.;
RT   "Role of the mitochondrial Hsp70s, Ssc1 and Ssq1, in the maturation of
RT   Yfh1.";
RL   Mol. Cell. Biol. 20:3677-3684(2000).
RN   [10]
RP   FUNCTION, INTERACTION WITH TIM44, AND MUTAGENESIS OF PRO-442.
RX   PubMed=12032075; DOI=10.1093/emboj/21.11.2626;
RA   Strub A., Roettgers K., Voos W.;
RT   "The Hsp70 peptide-binding domain determines the interaction of the
RT   ATPase domain with Tim44 in mitochondria.";
RL   EMBO J. 21:2626-2635(2002).
RN   [11]
RP   INTERACTION WITH PAM18.
RX   PubMed=14517234; DOI=10.1093/emboj/cdg485;
RA   Mokranjac D., Sichting M., Neupert W., Hell K.;
RT   "Tim14, a novel key component of the import motor of the TIM23 protein
RT   translocase of mitochondria.";
RL   EMBO J. 22:4945-4956(2003).
RN   [12]
RP   IDENTIFICATION IN THE PAM COMPLEX WITH PAM16; PAM17; PAM18; TIM44 AND
RP   MGE1.
RX   PubMed=16107694; DOI=10.1128/MCB.25.17.7449-7458.2005;
RA   van der Laan M., Chacinska A., Lind M., Perschil I., Sickmann A.,
RA   Meyer H.E., Guiard B., Meisinger C., Pfanner N., Rehling P.;
RT   "Pam17 is required for architecture and translocation activity of the
RT   mitochondrial protein import motor.";
RL   Mol. Cell. Biol. 25:7449-7458(2005).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-330, AND MASS
RP   SPECTROMETRY.
RX   PubMed=17761666; DOI=10.1074/mcp.M700098-MCP200;
RA   Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,
RA   van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
RT   "Profiling phosphoproteins of yeast mitochondria reveals a role of
RT   phosphorylation in assembly of the ATP synthase.";
RL   Mol. Cell. Proteomics 6:1896-1906(2007).
RN   [14]
RP   INTERACTION WITH NAP1, AND MASS SPECTROMETRY.
RX   PubMed=18086883; DOI=10.1128/MCB.01035-07;
RA   Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F.,
RA   Pemberton L.F.;
RT   "Phosphorylation by casein kinase 2 regulates Nap1 localization and
RT   function.";
RL   Mol. Cell. Biol. 28:1313-1325(2008).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-14; SER-16 AND
RP   THR-137, AND MASS SPECTROMETRY.
RX   PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- FUNCTION: Essential component of the PAM complex, a complex
CC       required for the translocation of transit peptide-containing
CC       proteins from the inner membrane into the mitochondrial matrix in
CC       an ATP-dependent manner. Constitutes the ATP-driven core of the
CC       motor and binds the precursor preprotein. Required for the import
CC       of the processed fratxin homolog YFH1 into the mitochondrion.
CC   -!- FUNCTION: Acts as a non-catalytic component of endonuclease SceI
CC       (endo.SceI), which cleaves specifically at multiple sites on
CC       mitochondrial DNA and produces double-stranded breaks. SSC1
CC       confers broader sequence specificity, greater stability, and
CC       higher activity on the catalytic subunit.
CC   -!- SUBUNIT: Component of the PAM complex, at least composed of SSC1
CC       (mtHsp70), MGE1, TIM44, PAM16/TIM16, PAM17 and PAM18/TIM14. In the
CC       complex, SSC1 interacts directly with PAM18 and TIM44. Component
CC       of endonuclease SceI (endo.SceI), which is a heterodimer of ENS2
CC       and SSC1. Interacts with NAP1.
CC   -!- INTERACTION:
CC       P12294:ENS2; NbExp=1; IntAct=EBI-8637, EBI-6490;
CC       P32335:MSS51; NbExp=1; IntAct=EBI-8637, EBI-11318;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix. Nucleus. Note=Detected
CC       also in the nucleus after heat shock.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
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DR   EMBL; M27229; AAA63792.1; -; Genomic_DNA.
DR   EMBL; M55275; AAA34590.1; -; Genomic_DNA.
DR   EMBL; L36344; AAA88747.1; -; Genomic_DNA.
DR   EMBL; Z49545; CAA89573.1; -; Genomic_DNA.
DR   PIR; A32493; HHBYS1.
DR   RefSeq; NP_012579.1; -.
DR   HSSP; P04475; 1DKG.
DR   DIP; DIP:411N; -.
DR   IntAct; P12398; 37.
DR   STRING; P12398; -.
DR   SWISS-2DPAGE; P12398; -.
DR   PeptideAtlas; P12398; -.
DR   PRIDE; P12398; -.
DR   Ensembl; YJR045C; YJR045C; YJR045C; Saccharomyces cerevisiae.
DR   GeneID; 853503; -.
DR   GenomeReviews; Y13136_GR; YJR045C.
DR   KEGG; sce:YJR045C; -.
DR   NMPDR; fig|4932.3.peg.3553; -.
DR   CYGD; YJR045c; -.
DR   SGD; S000003806; SSC1.
DR   HOGENOM; P12398; -.
DR   OMA; P12398; ANNGDAW.
DR   NextBio; 974151; -.
DR   ArrayExpress; P12398; -.
DR   GermOnline; YJR045C; Saccharomyces cerevisiae.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0001405; C:presequence translocase-associated import m...; IPI:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IDA:SGD.
DR   GO; GO:0030234; F:enzyme regulator activity; IDA:SGD.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0032079; P:positive regulation of endodeoxyribonucleas...; IDA:SGD.
DR   GO; GO:0030150; P:protein import into mitochondrial matrix; IDA:SGD.
DR   GO; GO:0042026; P:protein refolding; IDA:SGD.
DR   GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR   InterPro; IPR012725; DnaK_prok.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR001023; Hsp70.
DR   InterPro; IPR013126; Hsp_70.
DR   PANTHER; PTHR19375; Hsp70; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   ProDom; PD000089; Hsp70; 1.
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; Complete proteome; Direct protein sequencing;
KW   Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Stress response; Transit peptide.
FT   TRANSIT       1     23       Mitochondrion.
FT   CHAIN        24    654       Heat shock protein SSC1, mitochondrial.
FT                                /FTId=PRO_0000013553.
FT   COMPBIAS    634    646       Asn-rich.
FT   MOD_RES      12     12       Phosphoserine.
FT   MOD_RES      14     14       Phosphoserine.
FT   MOD_RES      16     16       Phosphoserine.
FT   MOD_RES     137    137       Phosphothreonine.
FT   MOD_RES     330    330       Phosphothreonine.
FT   MUTAGEN     442    442       P->S: No interaction with TIM44.
FT   CONFLICT    643    643       N -> NN (in Ref. 2; AA sequence).
FT   CONFLICT    650    650       G -> D (in Ref. 2; AAA34590).
SQ   SEQUENCE   654 AA;  70628 MW;  1E5672E76FCE24AC CRC64;
     MLAAKNILNR SSLSSSFRIA TRLQSTKVQG SVIGIDLGTT NSAVAIMEGK VPKIIENAEG
     SRTTPSVVAF TKEGERLVGI PAKRQAVVNP ENTLFATKRL IGRRFEDAEV QRDIKQVPYK
     IVKHSNGDAW VEARGQTYSP AQIGGFVLNK MKETAEAYLG KPVKNAVVTV PAYFNDSQRQ
     ATKDAGQIVG LNVLRVVNEP TAAALAYGLE KSDSKVVAVF DLGGGTFDIS ILDIDNGVFE
     VKSTNGDTHL GGEDFDIYLL REIVSRFKTE TGIDLENDRM AIQRIREAAE KAKIELSSTV
     STEINLPFIT ADASGPKHIN MKFSRAQFET LTAPLVKRTV DPVKKALKDA GLSTSDISEV
     LLVGGMSRMP KVVETVKSLF GKDPSKAVNP DEAVAIGAAV QGAVLSGEVT DVLLLDVTPL
     SLGIETLGGV FTRLIPRNTT IPTKKSQIFS TAAAGQTSVE IRVFQGEREL VRDNKLIGNF
     TLAGIPPAPK GVPQIEVTFD IDADGIINVS ARDKATNKDS SITVAGSSGL SENEIEQMVN
     DAEKFKSQDE ARKQAIETAN KADQLANDTE NSLKEFEGKV DKAEAQKVRD QITSLKELVA
     RVQGGEEVNA EELKTKTEEL QTSSMKLFEQ LYKNDSNNNN NNNGNNAESG ETKQ
//