Heat shock protein SSQ1, mitochondrial precursor - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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Q05931 (HSP7Q_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 94. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Heat shock protein SSQ1, mitochondrial

Alternative name(s):
Stress-seventy subfamily Q protein 1
mtHSP70 homolog

Gene names

Name:	SSQ1
Synonyms:	SSC2
Ordered Locus Names:	YLR369W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	657 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Has a role in mitochondrial iron homeostasis. Appears to be involved in the processing of the intermediate form of the frataxin homolog YFH1. Required for the assembly of iron-sulfur (Fe/S) clusters in mitochondria. Ref.3 Ref.4 Ref.5 Ref.6 Ref.10 Ref.11 Ref.12
Subunit structure	Interacts with the Fe/S cluster assembly protein ISU1 and MGE1. Ref.5 Ref.6 Ref.10
Subcellular location	Mitochondrion matrix Ref.4 Ref.5 Ref.7 Ref.9.
Miscellaneous	Present with 5550 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the heat shock protein 70 family.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chaperone
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	intracellular sequestering of iron ion Inferred from mutant phenotype Ref.3. Source: SGD iron-sulfur cluster assembly Inferred from mutant phenotype PubMed 9813017. Source: SGD protein maturation Inferred from mutant phenotype Ref.4. Source: SGD response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mitochondrial matrix Inferred from direct assay PubMed 8707841. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW unfolded protein binding Inferred from sequence or structural similarity PubMed 8707841. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ISU1	Q03020	4	EBI-35227,EBI-29901

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – ?

Mitochondrion

Chain

? – 657

Heat shock protein SSQ1, mitochondrial

PRO_0000270557

Amino acid modifications

Modified residue

Phosphoserine Ref.13

Experimental info

Mutagenesis

462

F → S: Decreased interaction with ISU1. Ref.11

Mutagenesis

472

V → F: 10-fold decrease in interaction with ISU1. Ref.11

Sequences

Sequence

Length

Mass (Da)

Tools

Q05931 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: AC2DF42F3D623892
Show »

FASTA

657

72,365

        10         20         30         40         50         60 
MLKSGRLNFL KLNINSRLLY STNPQLTKKV IGIDLGTTNS AVAYIRDSND KKSATIIEND 

        70         80         90        100        110        120 
EGQRTTPSIV AFDVKSSPQN KDQMKTLVGM AAKRQNAINS ENTFFATKRL IGRAFNDKEV 

       130        140        150        160        170        180 
QRDMAVMPYK IVKCESNGQA YLSTSNGLIQ SPSQIASILL KYLKQTSEEY LGEKVNLAVI 

       190        200        210        220        230        240 
TVPAYFNDSQ RQATKDAGKL AGLNVLRVIN EPTAAALSFG IDDKRNNGLI AVYDLGGGTF 

       250        260        270        280        290        300 
DISILDIEDG VFEVRATNGD THLGGEDFDN VIVNYIIDTF IHENPEITRE EITKNRETMQ 

       310        320        330        340        350        360 
RLKDVSERAK IDLSHVKKTF IELPFVYKSK HLRVPMTEEE LDNMTLSLIN RTIPPVKQAL 

       370        380        390        400        410        420 
KDADIEPEDI DEVILVGGMT RMPKIRSVVK DLFGKSPNSS VNPDETVALG AAIQGGILSG 

       430        440        450        460        470        480 
EIKNVLLLDV TPLTLGIETF GGAFSPLIPR NTTVPVKKTE IFSTGVDGQA GVDIKVFQGE 

       490        500        510        520        530        540 
RGLVRNNKLI GDLKLTGITP LPKGIPQIYV TFDIDADGII NVSAAEKSSG KQQSITVIPN 

       550        560        570        580        590        600 
SGLSEEEIAK LIEEANANRA QDNLIRQRLE LISKADIMIS DTENLFKRYE KLISSEKEYS 

       610        620        630        640        650 
NIVEDIKALR QAIKNFKANE NDMSIDVNGI KKATDALQGR ALKLFQSATK NQQNQGK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. Hoheisel J.D. Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Mt-Hsp70 homolog, Ssc2p, required for maturation of yeast frataxin and mitochondrial iron homeostasis." Knight S.A.B., Sepuri N.B.V., Pain D., Dancis A. J. Biol. Chem. 273:18389-18393(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[4]	"Role of the mitochondrial Hsp70s, Ssc1 and Ssq1, in the maturation of Yfh1." Voisine C., Schilke B., Ohlson M., Beinert H., Marszalek J., Craig E.A. Mol. Cell. Biol. 20:3677-3684(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[5]	"The mitochondrial proteins Ssq1 and Jac1 are required for the assembly of iron sulfur clusters in mitochondria." Lutz T., Westermann B., Neupert W., Herrmann J.M. J. Mol. Biol. 307:815-825(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH MGE1, SUBCELLULAR LOCATION.
[6]	"Ssq1, a mitochondrial Hsp70 involved in iron-sulfur (Fe/S) center biogenesis. Similarities to and differences from its bacterial counterpart." Dutkiewicz R., Schilke B., Knieszner H., Walter W., Craig E.A., Marszalek J. J. Biol. Chem. 278:29719-29727(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ISU1.
[7]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"The proteome of Saccharomyces cerevisiae mitochondria." Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C. Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Strain: ATCC 76625 / YPH499.
[10]	"Sequence-specific interaction between mitochondrial Fe-S scaffold protein Isu and Hsp70 Ssq1 is essential for their in vivo function." Dutkiewicz R., Schilke B., Cheng S., Knieszner H., Craig E.A., Marszalek J. J. Biol. Chem. 279:29167-29174(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ISU1.
[11]	"Compensation for a defective interaction of the hsp70 ssq1 with the mitochondrial Fe-S cluster scaffold isu." Knieszner H., Schilke B., Dutkiewicz R., D'Silva P., Cheng S., Ohlson M., Craig E.A., Marszalek J. J. Biol. Chem. 280:28966-28972(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF PHE-462 AND VAL-472.
[12]	"The Hsp70 chaperone Ssq1p is dispensable for iron-sulfur cluster formation on the scaffold protein Isu1p." Dutkiewicz R., Marszalek J., Schilke B., Craig E.A., Lill R., Muehlenhoff U. J. Biol. Chem. 281:7801-7808(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U19103 Genomic DNA. Translation: AAB67565.1. BK006945 Genomic DNA. Translation: DAA09672.1.
PIR	S51387.
RefSeq	NP_013473.1. NM_001182258.1.
3D structure databases
ProteinModelPortal	Q05931.
SMR	Q05931. Positions 29-614.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6407N.
IntAct	Q05931. 4 interactions.
MINT	MINT-694730.
STRING	4932.YLR369W.
Proteomic databases
PaxDb	Q05931.
PeptideAtlas	Q05931.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YLR369W; YLR369W; YLR369W.
GeneID	851084.
KEGG	sce:YLR369W.
Organism-specific databases
CYGD	YLR369w.
SGD	S000004361. SSQ1.
Phylogenomic databases
eggNOG	COG0443.
GeneTree	ENSGT00700000104565.
HOGENOM	HOG000228135.
OMA	IENDEGQ.
OrthoDB	EOG40ZV5Z.
Enzyme and pathway databases
BioCyc	MetaCyc:G3O-32438-MONOMER. YEAST:G3O-32438-MONOMER.
Gene expression databases
Genevestigator	Q05931.
Family and domain databases
InterPro	IPR018181. Heat_shock_70_CS. IPR013126. Hsp_70_fam. [Graphical view]
Pfam	PF00012. HSP70. 1 hit. [Graphical view]
PRINTS	PR00301. HEATSHOCK70.
PROSITE	PS00297. HSP70_1. 1 hit. PS00329. HSP70_2. 1 hit. PS01036. HSP70_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	967747.

Entry information

Entry name

HSP7Q_YEAST

Accession

Primary (citable) accession number: Q05931
Secondary accession number(s): D6VZ06

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	November 1, 1996
Last modified:	May 29, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XII

Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents