HSP77_YEAST
ID HSP77_YEAST Reviewed; 654 AA.
AC P0CS90; D6VWL6; P12398;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Import motor subunit, mitochondrial {ECO:0000305};
DE EC=3.6.4.10 {ECO:0000250|UniProtKB:Q05931};
DE AltName: Full=Endonuclease SceI 75 kDa subunit {ECO:0000305};
DE Short=Endo.SceI 75 kDa subunit {ECO:0000305};
DE AltName: Full=mtHSP70 {ECO:0000305};
DE Flags: Precursor;
GN Name=SSC1 {ECO:0000303|PubMed:2674677, ECO:0000312|SGD:S000003806};
GN Synonyms=ENS1 {ECO:0000312|SGD:S000003806}; OrderedLocusNames=YJR045C;
GN ORFNames=J1639;
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].
RC STRAIN=ATCC 24657 / D273-10B;
RX PubMed=2674677; DOI=10.1128/mcb.9.7.3000-3008.1989;
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, encodes a
RT mitochondrial protein.";
RL Mol. Cell. Biol. 9:3000-3008(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [4]
RP GENOME REANNOTATION.
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 PROTEIN SEQUENCE OF 24-38, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 24657 / D273-10B;
RX PubMed=2265609; DOI=10.1002/j.1460-2075.1990.tb07880.x;
RA Scherer P.E., Krieg U.C., Hwang S.T., Vestweber D., Schatz G.;
RT "A precursor protein partly translocated into yeast mitochondria is bound
RT to a 70 kd mitochondrial stress protein.";
RL EMBO J. 9:4315-4322(1990).
RN [6]
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 genetic
RT recombination in yeast.";
RL Adv. Biophys. 31:77-91(1995).
RN [7]
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., 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 [8]
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 ATPase
RT domain with Tim44 in mitochondria.";
RL EMBO J. 21:2626-2635(2002).
RN [9]
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 [10]
RP IDENTIFICATION IN THE PAM COMPLEX WITH PAM16; PAM17; PAM18; TIM44 AND 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-330, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
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 [12]
RP INTERACTION WITH NAP1, AND IDENTIFICATION BY 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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Essential component of the PAM complex, a complex required
CC for the translocation of transit peptide-containing proteins from the
CC inner membrane into the mitochondrial matrix in an ATP-dependent
CC manner. Constitutes the ATP-driven core of the motor and binds the
CC precursor preprotein. Required for the import of the processed frataxin
CC homolog YFH1 into the mitochondrion. {ECO:0000269|PubMed:10779357,
CC ECO:0000269|PubMed:12032075, ECO:0000269|PubMed:7625280}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10;
CC Evidence={ECO:0000250|UniProtKB:Q05931};
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. Interacts with
CC NAP1. {ECO:0000269|PubMed:12032075, ECO:0000269|PubMed:14517234,
CC ECO:0000269|PubMed:16107694, ECO:0000269|PubMed:18086883}.
CC -!- INTERACTION:
CC P0CS90; P38257: MMS4; NbExp=2; IntAct=EBI-8637, EBI-21547;
CC P0CS90; P53632: PAP2; NbExp=2; IntAct=EBI-8637, EBI-19517;
CC P0CS90; P06779: RAD7; NbExp=2; IntAct=EBI-8637, EBI-14780;
CC P0CS90; P38827: SET1; NbExp=2; IntAct=EBI-8637, EBI-16977;
CC P0CS90; Q01852: TIM44; NbExp=3; IntAct=EBI-8637, EBI-9141;
CC P0CS90; P12294: ENS2; Xeno; NbExp=2; IntAct=EBI-8637, EBI-6490;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:2265609}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
CC -!- CAUTION: S.cerevisiae displays strain polymorphism with regard to
CC Endo.SceI endouclease activity. This is due to the mitochondrion-
CC encoded, catalytic subunit ENS2, which exhibits strain polymorphism. It
CC can be either present as continuous ORF in the mitochondrial genome
CC (e.g. strain IAM 4274), present but disrupted by the insertion of GC
CC clusters (e.g. strain D273-10B/A), or completely absent in the
CC mitochondrial genome (e.g. strain S288c). Sequences for the 2 subunits
CC ENS2 (AC P12294) and SSC1 (AC P0CS91) for an active Endo.SceI
CC endonuclease can be found in strain IAM 4274. {ECO:0000305}.
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DR EMBL; M27229; AAA63792.1; -; Genomic_DNA.
DR EMBL; L36344; AAA88747.1; -; Genomic_DNA.
DR EMBL; Z49545; CAA89573.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08832.1; -; Genomic_DNA.
DR PIR; A32493; HHBYS1.
DR RefSeq; NP_012579.1; NM_001181703.1.
DR AlphaFoldDB; P0CS90; -.
DR SMR; P0CS90; -.
DR BioGRID; 33797; 981.
DR ComplexPortal; CPX-1423; COX1 pre-assembly complex.
DR ComplexPortal; CPX-1741; Endonuclease SceI.
DR ComplexPortal; CPX-539; TIM23 mitochondrial inner membrane pre-sequence translocase complex, motor variant.
DR IntAct; P0CS90; 216.
DR MINT; P0CS90; -.
DR STRING; 4932.YJR045C; -.
DR iPTMnet; P0CS90; -.
DR MaxQB; P0CS90; -.
DR PaxDb; P0CS90; -.
DR PRIDE; P0CS90; -.
DR EnsemblFungi; YJR045C_mRNA; YJR045C; YJR045C.
DR GeneID; 853503; -.
DR KEGG; sce:YJR045C; -.
DR SGD; S000003806; SSC1.
DR VEuPathDB; FungiDB:YJR045C; -.
DR eggNOG; KOG0102; Eukaryota.
DR GeneTree; ENSGT00920000149123; -.
DR HOGENOM; CLU_005965_2_1_1; -.
DR InParanoid; P0CS90; -.
DR OMA; ISIKRHM; -.
DR BioCyc; YEAST:G3O-31680-MON; -.
DR BRENDA; 7.4.2.3; 984.
DR PRO; PR:P0CS90; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P0CS90; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:1905347; C:endodeoxyribonuclease complex; IDA:ComplexPortal.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:ComplexPortal.
DR GO; GO:0001405; C:PAM complex, Tim23 associated import motor; IDA:SGD.
DR GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; IC:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:SGD.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0030234; F:enzyme regulator activity; IDA:SGD.
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:0008566; F:mitochondrial protein-transporting ATPase activity; IMP:FlyBase.
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:0006886; P:intracellular protein transport; IC:ComplexPortal.
DR GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; IC:ComplexPortal.
DR GO; GO:0032042; P:mitochondrial DNA metabolic process; IDA:ComplexPortal.
DR GO; GO:0070130; P:negative regulation of mitochondrial translation; IC:ComplexPortal.
DR GO; GO:0032079; P:positive regulation of endodeoxyribonuclease activity; 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:0050821; P:protein stabilization; IC:ComplexPortal.
DR GO; GO:0043335; P:protein unfolding; IMP:SGD.
DR GO; GO:0000018; P:regulation of DNA recombination; IDA:ComplexPortal.
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; Hydrolase;
KW Mitochondrion; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Stress response; Transit peptide.
FT TRANSIT 1..23
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2265609"
FT CHAIN 24..654
FT /note="Import motor subunit, mitochondrial"
FT /id="PRO_0000013553"
FT REGION 629..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 330
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17761666"
FT MUTAGEN 442
FT /note="P->S: No interaction with TIM44."
FT /evidence="ECO:0000269|PubMed:12032075"
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
