HSP7Q_YEAST
ID HSP7Q_YEAST Reviewed; 657 AA.
AC Q05931; D6VZ06;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Iron-sulfur cluster biogenesis chaperone, mitochondrial {ECO:0000305};
DE EC=3.6.4.10 {ECO:0000269|PubMed:16431909, ECO:0000269|PubMed:26545917};
DE AltName: Full=Heat shock protein SSQ1, mitochondrial {ECO:0000305};
DE AltName: Full=Stress-seventy subfamily Q protein 1 {ECO:0000305};
DE AltName: Full=mtHSP70 homolog {ECO:0000305};
DE Flags: Precursor;
GN Name=SSQ1 {ECO:0000303|PubMed:10779357, ECO:0000312|SGD:S000004361};
GN Synonyms=SSC2 {ECO:0000303|PubMed:9660806}; OrderedLocusNames=YLR369W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
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 [3]
RP FUNCTION.
RX PubMed=9660806; DOI=10.1074/jbc.273.29.18389;
RA Knight S.A.B., Sepuri N.B.V., Pain D., Dancis A.;
RT "Mt-Hsp70 homolog, Ssc2p, required for maturation of yeast frataxin and
RT mitochondrial iron homeostasis.";
RL J. Biol. Chem. 273:18389-18393(1998).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [5]
RP FUNCTION, INTERACTION WITH MGE1, AND SUBCELLULAR LOCATION.
RX PubMed=11273703; DOI=10.1006/jmbi.2001.4527;
RA Lutz T., Westermann B., Neupert W., Herrmann J.M.;
RT "The mitochondrial proteins Ssq1 and Jac1 are required for the assembly of
RT iron sulfur clusters in mitochondria.";
RL J. Mol. Biol. 307:815-825(2001).
RN [6]
RP FUNCTION, AND INTERACTION WITH ISU1.
RX PubMed=12756240; DOI=10.1074/jbc.m303527200;
RA Dutkiewicz R., Schilke B., Knieszner H., Walter W., Craig E.A.,
RA Marszalek J.;
RT "Ssq1, a mitochondrial Hsp70 involved in iron-sulfur (Fe/S) center
RT biogenesis. Similarities to and differences from its bacterial
RT counterpart.";
RL J. Biol. Chem. 278:29719-29727(2003).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
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).
RN [10]
RP FUNCTION, AND INTERACTION WITH ISU1.
RX PubMed=15123690; DOI=10.1074/jbc.m402947200;
RA Dutkiewicz R., Schilke B., Cheng S., Knieszner H., Craig E.A.,
RA Marszalek J.;
RT "Sequence-specific interaction between mitochondrial Fe-S scaffold protein
RT Isu and Hsp70 Ssq1 is essential for their in vivo function.";
RL J. Biol. Chem. 279:29167-29174(2004).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF PHE-462 AND VAL-472.
RX PubMed=15958384; DOI=10.1074/jbc.m503031200;
RA Knieszner H., Schilke B., Dutkiewicz R., D'Silva P., Cheng S., Ohlson M.,
RA Craig E.A., Marszalek J.;
RT "Compensation for a defective interaction of the hsp70 ssq1 with the
RT mitochondrial Fe-S cluster scaffold isu.";
RL J. Biol. Chem. 280:28966-28972(2005).
RN [12]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16431909; DOI=10.1074/jbc.m513301200;
RA Dutkiewicz R., Marszalek J., Schilke B., Craig E.A., Lill R.,
RA Muehlenhoff U.;
RT "The Hsp70 chaperone Ssq1p is dispensable for iron-sulfur cluster formation
RT on the scaffold protein Isu1p.";
RL J. Biol. Chem. 281:7801-7808(2006).
RN [13]
RP FUNCTION, AND INTERACTION WITH GRX5.
RX PubMed=23615440; DOI=10.1091/mbc.e12-09-0644;
RA Uzarska M.A., Dutkiewicz R., Freibert S.A., Lill R., Muehlenhoff U.;
RT "The mitochondrial Hsp70 chaperone Ssq1 facilitates Fe/S cluster transfer
RT from Isu1 to Grx5 by complex formation.";
RL Mol. Biol. Cell 24:1830-1841(2013).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH JAC1.
RX PubMed=26545917; DOI=10.1093/molbev/msv254;
RA Delewski W., Paterkiewicz B., Manicki M., Schilke B., Tomiczek B.,
RA Ciesielski S.J., Nierzwicki L., Czub J., Dutkiewicz R., Craig E.A.,
RA Marszalek J.;
RT "Iron-Sulfur Cluster Biogenesis Chaperones: Evidence for Emergence of
RT Mutational Robustness of a Highly Specific Protein-Protein Interaction.";
RL Mol. Biol. Evol. 33:643-656(2016).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=31040179; DOI=10.1074/jbc.ra119.008600;
RA Pandey A.K., Pain J., Dancis A., Pain D.;
RT "Mitochondria export iron-sulfur and sulfur intermediates to the cytoplasm
RT for iron-sulfur cluster assembly and tRNA thiolation in yeast.";
RL J. Biol. Chem. 294:9489-9502(2019).
CC -!- FUNCTION: Required for the assembly of iron-sulfur (Fe/S) clusters in
CC mitochondria (PubMed:10779357, PubMed:11273703, PubMed:12756240,
CC PubMed:15123690, PubMed:15958384, PubMed:16431909, PubMed:9660806,
CC PubMed:31040179). Assisted by the DnaJ-like co-chaperone JAC1 and the
CC nucleotide exchange factor MGE1, it mediates ATP-dependent Fe-S cluster
CC transfer from the scaffold proteins ISU1/ISU2 to GRX5 (PubMed:11273703,
CC PubMed:12756240, PubMed:15123690, PubMed:15958384, PubMed:16431909,
CC PubMed:31040179, PubMed:26545917, PubMed:23615440).
CC {ECO:0000269|PubMed:10779357, ECO:0000269|PubMed:11273703,
CC ECO:0000269|PubMed:12756240, ECO:0000269|PubMed:15123690,
CC ECO:0000269|PubMed:15958384, ECO:0000269|PubMed:16431909,
CC ECO:0000269|PubMed:23615440, ECO:0000269|PubMed:26545917,
CC ECO:0000269|PubMed:31040179, ECO:0000269|PubMed:9660806}.
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:0000269|PubMed:16431909, ECO:0000269|PubMed:26545917};
CC -!- SUBUNIT: Interacts with the Fe/S cluster assembly proteins ISU1, MGE1,
CC GRX5 and JAC1. {ECO:0000269|PubMed:11273703,
CC ECO:0000269|PubMed:12756240, ECO:0000269|PubMed:15123690,
CC ECO:0000269|PubMed:23615440, ECO:0000269|PubMed:26545917}.
CC -!- INTERACTION:
CC Q05931; Q03020: ISU1; NbExp=4; IntAct=EBI-35227, EBI-29901;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:10779357, ECO:0000269|PubMed:11273703,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}.
CC -!- DISRUPTION PHENOTYPE: Disrupts iron-sulfur (Fe-S) cluster assembly
CC (PubMed:31040179). Normal cytosolic tRNA thiolation (PubMed:31040179).
CC {ECO:0000269|PubMed:31040179}.
CC -!- MISCELLANEOUS: Present with 5550 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; U19103; AAB67565.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09672.1; -; Genomic_DNA.
DR PIR; S51387; S51387.
DR RefSeq; NP_013473.1; NM_001182258.1.
DR AlphaFoldDB; Q05931; -.
DR SMR; Q05931; -.
DR BioGRID; 31629; 31.
DR DIP; DIP-6407N; -.
DR IntAct; Q05931; 4.
DR MINT; Q05931; -.
DR STRING; 4932.YLR369W; -.
DR iPTMnet; Q05931; -.
DR MaxQB; Q05931; -.
DR PaxDb; Q05931; -.
DR PRIDE; Q05931; -.
DR EnsemblFungi; YLR369W_mRNA; YLR369W; YLR369W.
DR GeneID; 851084; -.
DR KEGG; sce:YLR369W; -.
DR SGD; S000004361; SSQ1.
DR VEuPathDB; FungiDB:YLR369W; -.
DR eggNOG; KOG0102; Eukaryota.
DR HOGENOM; CLU_005965_2_1_1; -.
DR InParanoid; Q05931; -.
DR OMA; RAEILCT; -.
DR BioCyc; MetaCyc:G3O-32438-MON; -.
DR BioCyc; YEAST:G3O-32438-MON; -.
DR PRO; PR:Q05931; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q05931; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
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: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; IDA:SGD.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:SGD.
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:0016226; P:iron-sulfur cluster assembly; IMP:SGD.
DR GO; GO:0106034; P:protein maturation by [2Fe-2S] cluster transfer; IMP:SGD.
DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IMP:SGD.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
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 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; Hydrolase; Mitochondrion; Nucleotide-binding;
KW Reference proteome; Stress response; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT CHAIN ?..657
FT /note="Iron-sulfur cluster biogenesis chaperone,
FT mitochondrial"
FT /id="PRO_0000270557"
FT MUTAGEN 462
FT /note="F->S: Decreases interaction with ISU1."
FT /evidence="ECO:0000269|PubMed:15958384"
FT MUTAGEN 472
FT /note="V->F: 10-fold decrease in interaction with ISU1."
FT /evidence="ECO:0000269|PubMed:15958384"
SQ SEQUENCE 657 AA; 72365 MW; AC2DF42F3D623892 CRC64;
MLKSGRLNFL KLNINSRLLY STNPQLTKKV IGIDLGTTNS AVAYIRDSND KKSATIIEND
EGQRTTPSIV AFDVKSSPQN KDQMKTLVGM AAKRQNAINS ENTFFATKRL IGRAFNDKEV
QRDMAVMPYK IVKCESNGQA YLSTSNGLIQ SPSQIASILL KYLKQTSEEY LGEKVNLAVI
TVPAYFNDSQ RQATKDAGKL AGLNVLRVIN EPTAAALSFG IDDKRNNGLI AVYDLGGGTF
DISILDIEDG VFEVRATNGD THLGGEDFDN VIVNYIIDTF IHENPEITRE EITKNRETMQ
RLKDVSERAK IDLSHVKKTF IELPFVYKSK HLRVPMTEEE LDNMTLSLIN RTIPPVKQAL
KDADIEPEDI DEVILVGGMT RMPKIRSVVK DLFGKSPNSS VNPDETVALG AAIQGGILSG
EIKNVLLLDV TPLTLGIETF GGAFSPLIPR NTTVPVKKTE IFSTGVDGQA GVDIKVFQGE
RGLVRNNKLI GDLKLTGITP LPKGIPQIYV TFDIDADGII NVSAAEKSSG KQQSITVIPN
SGLSEEEIAK LIEEANANRA QDNLIRQRLE LISKADIMIS DTENLFKRYE KLISSEKEYS
NIVEDIKALR QAIKNFKANE NDMSIDVNGI KKATDALQGR ALKLFQSATK NQQNQGK
