HSP77_YEASX
ID HSP77_YEASX Reviewed; 655 AA.
AC P0CS91; D6VWL6; P12398;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 53.
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=Heat shock protein SSC1, mitochondrial {ECO:0000305};
DE AltName: Full=mtHSP70 {ECO:0000305};
DE Flags: Precursor;
GN Name=SSC1 {ECO:0000305}; Synonyms=ENS1 {ECO:0000305};
OS Saccharomyces cerevisiae (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=4932;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 24-41.
RC STRAIN=ATCC 46276 / IAM 4274 / NCYC 1408 / OC-2;
RX PubMed=2203771; DOI=10.1016/s0021-9258(18)77240-2;
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 [2]
RP IDENTIFICATION IN ENDONUCLEASE SCEI, AND FUNCTION OF ENDONUCLEASE SCEI.
RC STRAIN=ATCC 46276 / IAM 4274 / NCYC 1408 / OC-2;
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, endo
RT SceI. A study using monoclonal antibodies.";
RL Eur. J. Biochem. 171:23-29(1988).
RN [3]
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 [4]
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 multisite
RT specificity of a unisite-specific endonuclease in yeast mitochondria.";
RL J. Biol. Chem. 274:25682-25690(1999).
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 (By similarity).
CC {ECO:0000250|UniProtKB:P0CS90}.
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 confers
CC broader sequence specificity, greater stability, and higher activity on
CC the catalytic subunit. {ECO:0000269|PubMed:10464305,
CC ECO:0000269|PubMed:2828049, 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 (By similarity). Component of endonuclease SceI (endo.SceI), which
CC is a heterodimer of ENS2 and SSC1. {ECO:0000250|UniProtKB:P0CS90,
CC ECO:0000269|PubMed:10464305, ECO:0000269|PubMed:2828049}.
CC -!- INTERACTION:
CC P0CS91; P42844: ZIM17; Xeno; NbExp=2; IntAct=EBI-7276682, EBI-28366;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P0CS90}.
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; M55275; AAA34590.1; -; Genomic_DNA.
DR AlphaFoldDB; P0CS91; -.
DR SMR; P0CS91; -.
DR IntAct; P0CS91; 1.
DR MINT; P0CS91; -.
DR VEuPathDB; FungiDB:YJR045C; -.
DR OMA; ISIKRHM; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
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; Stress response;
KW Transit peptide.
FT TRANSIT 1..23
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2203771"
FT CHAIN 24..655
FT /note="Import motor subunit, mitochondrial"
FT /id="PRO_0000417665"
FT REGION 629..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 330
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P0CS90"
FT VARIANT 644
FT /note="Missing (in strain: D273-10B)"
FT VARIANT 651
FT /note="D -> G (in strain: D273-10B)"
SQ SEQUENCE 655 AA; 70800 MW; 2B08AF9E3BC21082 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 NNNNGNNAES DETKQ
