HSP7M_EMENI
ID HSP7M_EMENI Reviewed; 666 AA.
AC Q5B0C0; C8V337;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Iron-sulfur cluster biogenesis chaperone, mitochondrial {ECO:0000305};
DE EC=3.6.4.10 {ECO:0000250|UniProtKB:P22774};
DE AltName: Full=Heat shock 70 kDa protein;
DE Flags: Precursor;
GN ORFNames=AN6010;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17258477; DOI=10.1016/j.fgb.2006.12.001;
RA Kim Y., Nandakumar M.P., Marten M.R.;
RT "Proteome map of Aspergillus nidulans during osmoadaptation.";
RL Fungal Genet. Biol. 44:886-895(2007).
CC -!- FUNCTION: Required for the assembly of iron-sulfur (Fe/S) clusters in
CC mitochondria (By similarity). 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 (By
CC similarity). {ECO:0000250|UniProtKB:Q05931}.
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:0000250|UniProtKB:P22774};
CC -!- SUBUNIT: Interacts with the Fe/S cluster assembly and transfer
CC machinery (By similarity). Component of the PAM complex (By
CC similarity). {ECO:0000250|UniProtKB:P0CS90,
CC ECO:0000250|UniProtKB:Q05931}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P0CS90}.
CC -!- INDUCTION: Up-regulated when grown with elevated levels of potassium
CC chloride. {ECO:0000269|PubMed:17258477}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; AACD01000103; EAA57651.1; -; Genomic_DNA.
DR EMBL; BN001301; CBF70370.1; -; Genomic_DNA.
DR RefSeq; XP_663614.1; XM_658522.1.
DR AlphaFoldDB; Q5B0C0; -.
DR SMR; Q5B0C0; -.
DR STRING; 162425.CADANIAP00007009; -.
DR PRIDE; Q5B0C0; -.
DR EnsemblFungi; CBF70370; CBF70370; ANIA_06010.
DR EnsemblFungi; EAA57651; EAA57651; AN6010.2.
DR GeneID; 2871135; -.
DR KEGG; ani:AN6010.2; -.
DR VEuPathDB; FungiDB:AN6010; -.
DR eggNOG; KOG0102; Eukaryota.
DR HOGENOM; CLU_005965_2_1_1; -.
DR InParanoid; Q5B0C0; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 288077at2759; -.
DR Proteomes; UP000000560; Chromosome I.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
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:0071470; P:cellular response to osmotic stress; IEP:AspGD.
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:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0009847; P:spore germination; IMP:AspGD.
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; 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; Coiled coil; Hydrolase; Mitochondrion; Nucleotide-binding;
KW Reference proteome; Stress response; Transit peptide.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 34..666
FT /note="Iron-sulfur cluster biogenesis chaperone,
FT mitochondrial"
FT /id="PRO_0000348278"
FT REGION 635..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 566..637
FT /evidence="ECO:0000255"
SQ SEQUENCE 666 AA; 72372 MW; B0A5F96809B50E06 CRC64;
MLSSRLSRAL PRTAPFARAP AFRLPSTAAR RWNSTEEKVK GQVIGIDLGT TNSAVAVMEG
KTPKIIENAE GARTTPSVVA FAQDGERLVG IAAKRQAVVN PENTLFATKR LIGRKFTDAE
VQRDIKEVPY KIVQHTNGDA WVEARGEKYS PAQIGGFVLG KMKETAENYL SKPVKNAVVT
VPAYFNDSQR QATKDAGQIA GLNVLRVVNE PTAAALAYGL EKEADRVVAV YDLGGGTFDI
SVLEIQKGVF EVKSTNGDTH LGGEDFDISL VRHIVQQFKK ESGLDLSNDR MAIQRIREAA
EKAKIELSSS LQTEINLPFI TADASGAKHI NLKMTRAQLE SLVEPLISRT VDPVRKALKD
ANLQSSEVQD IILVGGMTRM PKVTESVKSL FGREPAKSVN PDEAVAIGAA IQGAVLAGEV
TDVLLLDVTP LSLGIETLGG VFTRLINRNT TIPTKKSQTF STAADFQTAV EIKVFQGERE
LVKDNKLLGN FQLVGIPPAH RGVPQIEVTF DIDADSIVHV HAKDKSTNKD QSITIASGSG
LSDAEIQSMV EDAEKYGAQD KERKAAIEAA NRADSVLNDT EKALKEFEDR LDKAEAEQIR
EKINTLREFV AKNQSGEVAA TAEELKQKTD ELQTASLTLF DKMHKAQSEQ QQQPNQGETG
QGENKP
