JAC1_YEAST
ID JAC1_YEAST Reviewed; 184 AA.
AC P53193; D6VUB9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=J-type co-chaperone JAC1, mitochondrial {ECO:0000305};
DE AltName: Full=J-type accessory chaperone 1 {ECO:0000305};
DE Flags: Precursor;
GN Name=JAC1 {ECO:0000303|PubMed:11171977, ECO:0000312|SGD:S000002986};
GN Synonyms=SEO2; OrderedLocusNames=YGL018C;
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=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP PROTEIN SEQUENCE OF 11-17, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF 48-HIS--ASP-50.
RX PubMed=11171977; DOI=10.1073/pnas.98.4.1483;
RA Voisine C., Cheng Y.C., Ohlson M., Schilke B., Hoff K., Beinert H.,
RA Marszalek J., Craig E.A.;
RT "Jac1, a mitochondrial J-type chaperone, is involved in the biogenesis of
RT Fe/S clusters in Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:1483-1488(2001).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF ASP-32.
RX PubMed=9813017; DOI=10.1074/jbc.273.47.31138;
RA Strain J., Lorenz C.R., Bode J., Garland S., Smolen G.A., Ta D.T.,
RA Vickery L.E., Culotta V.C.;
RT "Suppressors of superoxide dismutase (SOD1) deficiency in Saccharomyces
RT cerevisiae. Identification of proteins predicted to mediate iron-sulfur
RT cluster assembly.";
RL J. Biol. Chem. 273:31138-31144(1998).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11278728; DOI=10.1074/jbc.m010695200;
RA Kim R., Saxena S., Gordon D.M., Pain D., Dancis A.;
RT "J-domain protein, Jac1p, of yeast mitochondria required for iron
RT homeostasis and activity of Fe-S cluster proteins.";
RL J. Biol. Chem. 276:17524-17532(2001).
RN [7]
RP FUNCTION, 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 [8]
RP FUNCTION.
RX PubMed=12970193; DOI=10.1093/emboj/cdg446;
RA Muehlenhoff U., Gerber J., Richhardt N., Lill R.;
RT "Components involved in assembly and dislocation of iron-sulfur clusters on
RT the scaffold protein Isu1p.";
RL EMBO J. 22:4815-4825(2003).
RN [9]
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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
RP FUNCTION.
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 [15]
RP FUNCTION, INTERACTION WITH ISU1, AND MUTAGENESIS OF 104-LEU--GLN-117.
RX PubMed=16551614; DOI=10.1074/jbc.m600842200;
RA Andrew A.J., Dutkiewicz R., Knieszner H., Craig E.A., Marszalek J.;
RT "Characterization of the interaction between the J-protein Jac1p and the
RT scaffold for Fe-S cluster biogenesis, Isu1p.";
RL J. Biol. Chem. 281:14580-14587(2006).
RN [16]
RP FUNCTION, INTERACTION WITH SSQ1, AND DISRUPTION PHENOTYPE.
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 [17]
RP FUNCTION, INTERACTION WITH SSQ1, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP LYS-20; ARG-35; LYS-38; ARG-41; HIS-48; PRO-49 AND ASP-50.
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).
CC -!- FUNCTION: Co-chaperone required for the assembly of iron-sulfur (Fe/S)
CC clusters in mitochondria. Stimulates the ATPase activity of its
CC specialized Hsp70 chaperone partner SSQ1, to mediate the transfer of
CC iron-sulfur clusters from ISU1 to GRX5. Binds to the substrate protein
CC ISU1 and targets it to SSQ1. {ECO:0000269|PubMed:11171977,
CC ECO:0000269|PubMed:11273703, ECO:0000269|PubMed:11278728,
CC ECO:0000269|PubMed:12756240, ECO:0000269|PubMed:12970193,
CC ECO:0000269|PubMed:15123690, ECO:0000269|PubMed:16431909,
CC ECO:0000269|PubMed:16551614, ECO:0000269|PubMed:23615440,
CC ECO:0000269|PubMed:26545917, ECO:0000269|PubMed:9813017}.
CC -!- SUBUNIT: Interacts with ISU1 and SSQ1. {ECO:0000269|PubMed:12756240,
CC ECO:0000269|PubMed:15123690, ECO:0000269|PubMed:16551614,
CC ECO:0000269|PubMed:23615440, ECO:0000269|PubMed:26545917}.
CC -!- INTERACTION:
CC P53193; Q03020: ISU1; NbExp=3; IntAct=EBI-23714, EBI-29901;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:11171977, ECO:0000269|PubMed:11273703,
CC ECO:0000269|PubMed:11278728, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278}.
CC -!- DISRUPTION PHENOTYPE: Increases association between GRX5 and SSQ1
CC (PubMed:23615440). Inviable vegetative cell population growth
CC (PubMed:26545917). {ECO:0000269|PubMed:23615440,
CC ECO:0000269|PubMed:26545917}.
CC -!- MISCELLANEOUS: Present with 2010 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the HscB family. {ECO:0000305}.
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DR EMBL; Z72540; CAA96718.1; -; Genomic_DNA.
DR EMBL; AY558479; AAS56805.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08080.1; -; Genomic_DNA.
DR PIR; S64020; S64020.
DR RefSeq; NP_011497.1; NM_001180883.1.
DR PDB; 3UO2; X-ray; 2.13 A; A/B=10-184.
DR PDB; 3UO3; X-ray; 1.85 A; A/B=5-182.
DR PDBsum; 3UO2; -.
DR PDBsum; 3UO3; -.
DR AlphaFoldDB; P53193; -.
DR SMR; P53193; -.
DR BioGRID; 33228; 34.
DR DIP; DIP-5603N; -.
DR IntAct; P53193; 1.
DR STRING; 4932.YGL018C; -.
DR MaxQB; P53193; -.
DR PaxDb; P53193; -.
DR PRIDE; P53193; -.
DR EnsemblFungi; YGL018C_mRNA; YGL018C; YGL018C.
DR GeneID; 852866; -.
DR KEGG; sce:YGL018C; -.
DR SGD; S000002986; JAC1.
DR VEuPathDB; FungiDB:YGL018C; -.
DR eggNOG; KOG3192; Eukaryota.
DR GeneTree; ENSGT00390000008206; -.
DR HOGENOM; CLU_068529_1_1_1; -.
DR InParanoid; P53193; -.
DR OMA; ECVRLRF; -.
DR BioCyc; MetaCyc:G3O-30538-MON; -.
DR BioCyc; YEAST:G3O-30538-MON; -.
DR Reactome; R-SCE-1268020; Mitochondrial protein import.
DR Reactome; R-SCE-1362409; Mitochondrial iron-sulfur cluster biogenesis.
DR PRO; PR:P53193; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53193; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005758; C:mitochondrial intermembrane space; TAS:Reactome.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0001671; F:ATPase activator activity; IDA:SGD.
DR GO; GO:0051087; F:chaperone binding; IMP:SGD.
DR GO; GO:0044571; P:[2Fe-2S] cluster assembly; IBA:GO_Central.
DR GO; GO:0009060; P:aerobic respiration; IMP:SGD.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:SGD.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:InterPro.
DR GO; GO:0106034; P:protein maturation by [2Fe-2S] cluster transfer; IMP:SGD.
DR GO; GO:0106035; P:protein maturation by [4Fe-4S] cluster transfer; IMP:SGD.
DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IMP:SGD.
DR CDD; cd06257; DnaJ; 1.
DR DisProt; DP02809; -.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 1.20.1280.20; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR004640; HscB.
DR InterPro; IPR036386; HscB_C_sf.
DR InterPro; IPR009073; HscB_oligo_C.
DR InterPro; IPR036869; J_dom_sf.
DR PANTHER; PTHR14021; PTHR14021; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF07743; HSCB_C; 1.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF47144; SSF47144; 1.
DR TIGRFAMs; TIGR00714; hscB; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Direct protein sequencing; Mitochondrion;
KW Reference proteome; Stress response; Transit peptide.
FT TRANSIT 1..10
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:11171977"
FT CHAIN 11..184
FT /note="J-type co-chaperone JAC1, mitochondrial"
FT /id="PRO_0000071163"
FT DOMAIN 13..82
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 71..184
FT /note="Interaction with ISU1"
FT MOTIF 48..50
FT /note="HSP70 binding"
FT /evidence="ECO:0000269|PubMed:26545917"
FT MUTAGEN 20
FT /note="K->A: Decreases JAC1 ATPase activator activity; when
FT associated with A-35; S-38 and L-41. Abolishes JAC1 ATPase
FT activator activity; when associated with A-35; S-38; L-41
FT and A-48."
FT /evidence="ECO:0000269|PubMed:26545917"
FT MUTAGEN 32
FT /note="Missing: In JAC1-1; temperature sensitive; causes
FT growth defect at high temperatures."
FT /evidence="ECO:0000269|PubMed:9813017"
FT MUTAGEN 35
FT /note="R->A: Decreases JAC1 ATPase activator activity; when
FT associated with A-20; S-38 and L-41. Abolishes JAC1 ATPase
FT activator activity; when associated with A-20; S-38; L-41
FT and A-48."
FT /evidence="ECO:0000269|PubMed:26545917"
FT MUTAGEN 38
FT /note="K->S: Decreases JAC1 ATPase activator activity; when
FT associated with A-20; A-35 and L-41. Abolishes JAC1 ATPase
FT activator activity; when associated with A-20; A-35; L-41
FT and A-48."
FT /evidence="ECO:0000269|PubMed:26545917"
FT MUTAGEN 41
FT /note="R->L: Decreases JAC1 ATPase activator activity; when
FT associated with A-20; A-35 and S-38. Abolishes JAC1 ATPase
FT activator activity; when associated with A-20; A-35; S-38
FT and A-48."
FT /evidence="ECO:0000269|PubMed:26545917"
FT MUTAGEN 48..50
FT /note="HPD->AAA: In JAC1-A3; temperature sensitive; causes
FT growth defect at high temperatures."
FT /evidence="ECO:0000269|PubMed:11171977"
FT MUTAGEN 48
FT /note="H->A: Decreases JAC1 ATPase activator activity.
FT Decreases vegetative cell population growth. Sensitive to
FT high temperature. Abolishes JAC1 ATPase activator activity;
FT when associated with A-20; A-35; S-38 and L-41."
FT /evidence="ECO:0000269|PubMed:26545917"
FT MUTAGEN 49
FT /note="P->A: Decreases JAC1 ATPase activator activity.
FT Decreases vegetative cell population growth. Sensitive to
FT high temperature."
FT /evidence="ECO:0000269|PubMed:26545917"
FT MUTAGEN 50
FT /note="D->A: Decreases JAC1 ATPase activator activity.
FT Decreases vegetative cell population growth. Sensitive to
FT high temperature."
FT /evidence="ECO:0000269|PubMed:26545917"
FT MUTAGEN 104..117
FT /note="LLLKVLDIHDELSQ->ALLAVLAIHAALSA: In JAC1(LKDDEQ);
FT impairs interaction with ISU1, but does not affect
FT stimulation of SSQ1 ATPase activity."
FT /evidence="ECO:0000269|PubMed:16551614"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:3UO3"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:3UO3"
FT HELIX 33..45
FT /evidence="ECO:0007829|PDB:3UO3"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:3UO3"
FT HELIX 62..70
FT /evidence="ECO:0007829|PDB:3UO3"
FT HELIX 72..84
FT /evidence="ECO:0007829|PDB:3UO3"
FT HELIX 91..99
FT /evidence="ECO:0007829|PDB:3UO3"
FT HELIX 102..117
FT /evidence="ECO:0007829|PDB:3UO3"
FT HELIX 121..147
FT /evidence="ECO:0007829|PDB:3UO3"
FT HELIX 151..172
FT /evidence="ECO:0007829|PDB:3UO3"
SQ SEQUENCE 184 AA; 21778 MW; 92B600F279866DF9 CRC64;
MLKYLVQRRF TSTFYELFPK TFPKKLPIWT IDQSRLRKEY RQLQAQHHPD MAQQGSEQSS
TLNQAYHTLK DPLRRSQYML KLLRNIDLTQ EQTSNEVTTS DPQLLLKVLD IHDELSQMDD
EAGVKLLEKQ NKERIQDIEA QLGQCYNDKD YAAAVKLTVE LKYWYNLAKA FKDWAPGKQL
EMNH
