HSP7M_SCHPO
ID HSP7M_SCHPO Reviewed; 674 AA.
AC P22774;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Iron-sulfur cluster biogenesis chaperone, mitochondrial {ECO:0000303|PubMed:26545917};
DE EC=3.6.4.10 {ECO:0000269|PubMed:26545917};
DE Flags: Precursor;
GN Name=ssc1 {ECO:0000303|PubMed:26545917}; Synonyms=ssp1 {ECO:0000305};
GN ORFNames=SPAC664.11 {ECO:0000312|PomBase:SPAC664.11};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=2123810; DOI=10.1016/0378-1119(90)90420-v;
RA Powell M.J., Watts F.Z.;
RT "Isolation of a gene encoding a mitochondrial HSP70 protein from
RT Schizosaccharomyces pombe.";
RL Gene 95:105-110(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40, AND ALTERNATIVE INITIATION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=1923816; DOI=10.1093/nar/19.19.5331;
RA Kasai H., Isono K.;
RT "Dual modes of transcriptional and translational initiation of SSP1, the
RT gene for a mitochondrial HSP70, responding to heat-shock in
RT Schizosaccharomyces pombe.";
RL Nucleic Acids Res. 19:5331-5337(1991).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH ISU1 AND 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).
CC -!- FUNCTION: Required for the assembly of iron-sulfur (Fe/S) clusters in
CC mitochondria (PubMed:26545917). Assisted by the DnaJ-like co-chaperone
CC jac1 and the nucleotide exchange factor mge1, it mediates ATP-dependent
CC Fe-S cluster transfer from the scaffold proteins isu1/isu2 to grx5
CC (PubMed:26545917). {ECO:0000269|PubMed:26545917}.
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 manner
CC (By similarity). Constitutes the ATP-driven core of the motor and binds
CC the precursor preprotein (By similarity).
CC {ECO:0000250|UniProtKB:P0CS90}.
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:26545917};
CC -!- SUBUNIT: Interacts with the Fe/S cluster transfer protein GRX5 (By
CC similarity). Interacts with the Fe/S cluster assembly proteins ISU1 and
CC JAC1 (PubMed:26545917). Component of the PAM complex (By similarity).
CC {ECO:0000250|UniProtKB:P0CS90, ECO:0000250|UniProtKB:Q05931,
CC ECO:0000269|PubMed:26545917}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000305|PubMed:26545917}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Long; Synonyms=Mitochondrial;
CC IsoId=P22774-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P22774-2; Sequence=VSP_018751;
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; M60208; AAA35314.1; -; mRNA.
DR EMBL; CU329670; CAB65812.1; -; Genomic_DNA.
DR EMBL; X59987; CAA42603.1; -; Genomic_DNA.
DR PIR; S18670; S18670.
DR RefSeq; NP_593459.1; NM_001018892.2.
DR AlphaFoldDB; P22774; -.
DR SMR; P22774; -.
DR BioGRID; 279462; 7.
DR DIP; DIP-54555N; -.
DR IntAct; P22774; 3.
DR STRING; 4896.SPAC664.11.1; -.
DR iPTMnet; P22774; -.
DR MaxQB; P22774; -.
DR PaxDb; P22774; -.
DR PRIDE; P22774; -.
DR EnsemblFungi; SPAC664.11.1; SPAC664.11.1:pep; SPAC664.11. [P22774-1]
DR GeneID; 2543026; -.
DR KEGG; spo:SPAC664.11; -.
DR PomBase; SPAC664.11; -.
DR VEuPathDB; FungiDB:SPAC664.11; -.
DR eggNOG; KOG0102; Eukaryota.
DR HOGENOM; CLU_005965_2_1_1; -.
DR InParanoid; P22774; -.
DR OMA; DKMVLQR; -.
DR PhylomeDB; P22774; -.
DR PRO; PR:P22774; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:PomBase.
DR GO; GO:0001405; C:PAM complex, Tim23 associated import motor; ISO:PomBase.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:PomBase.
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; IBA:GO_Central.
DR GO; GO:0044571; P:[2Fe-2S] cluster assembly; EXP:PomBase.
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:0006457; P:protein folding; ISO:PomBase.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; ISO:PomBase.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
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 Alternative initiation; ATP-binding; Hydrolase; Mitochondrion;
KW Nucleotide-binding; Reference proteome; Stress response; Transit peptide.
FT TRANSIT 1..43
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 44..674
FT /note="Iron-sulfur cluster biogenesis chaperone,
FT mitochondrial"
FT /id="PRO_0000013551"
FT REGION 655..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..33
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_018751"
SQ SEQUENCE 674 AA; 72977 MW; AF4A12D4D1ECBE3B CRC64;
MISSRFTNVV RSGLRFQSKG ASFKIGASLH GSRMTARWNS NASGNEKVKG PVIGIDLGTT
TSCLAIMEGQ TPKVIANAEG TRTTPSVVAF TKDGERLVGV SAKRQAVINP ENTFFATKRL
IGRRFKEPEV QRDIKEVPYK IVEHSNGDAW LEARGKTYSP SQIGGFILSK MRETASTYLG
KDVKNAVVTV PAYFNDSQRQ ATKAAGAIAG LNVLRVVNEP TAAALAYGLD KKNDAIVAVF
DLGGGTFDIS ILELNNGVFE VRSTNGDTHL GGEDFDVALV RHIVETFKKN EGLDLSKDRL
AVQRIREAAE KAKCELSSLS KTDISLPFIT ADATGPKHIN MEISRAQFEK LVDPLVRRTI
DPCKRALKDA NLQTSEINEV ILVGGMTRMP RVVETVKSIF KREPAKSVNP DEAVAIGAAI
QGGVLSGHVK DLVLLDVTPL SLGIETLGGV FTRLINRNTT IPTRKSQVFS TAADGQTAVE
IRVFQGEREL VRDNKLIGNF QLTGIAPAPK GQPQIEVSFD VDADGIINVS ARDKATNKDS
SITVAGSSGL TDSEIEAMVA DAEKYRASDM ARKEAIENGN RAESVCTDIE SNLDIHKDKL
DQQAVEDLRS KITDLRETVA KVNAGDEGIT SEDMKKKIDE IQQLSLKVFE SVYKNQNQGN
ESSGDNSAPE GDKK
