CLPX_YEAST
ID CLPX_YEAST Reviewed; 520 AA.
AC P38323; D6VQM2;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=ATP-dependent clpX-like chaperone, mitochondrial {ECO:0000305|PubMed:9827555};
DE Short=mtClpX {ECO:0000303|PubMed:25957689};
DE AltName: Full=ATP-dependent unfoldase ClpX {ECO:0000303|PubMed:25957689};
DE Flags: Precursor;
GN Name=MCX1 {ECO:0000303|PubMed:9827555};
GN OrderedLocusNames=YBR227C {ECO:0000312|SGD:S000000431}; ORFNames=YBR1524;
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=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
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 SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=9827555; DOI=10.1016/s0014-5793(98)01310-6;
RA van Dyck L., Dembowski M., Neupert W., Langer T.;
RT "Mcx1p, a ClpX homologue in mitochondria of Saccharomyces cerevisiae.";
RL FEBS Lett. 438:250-254(1998).
RN [4]
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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF TYR-174 AND GLU-206, AND
RP INTERACTION WITH HEM1.
RX PubMed=25957689; DOI=10.1016/j.cell.2015.04.017;
RA Kardon J.R., Yien Y.Y., Huston N.C., Branco D.S., Hildick-Smith G.J.,
RA Rhee K.Y., Paw B.H., Baker T.A.;
RT "Mitochondrial ClpX activates a key enzyme for heme biosynthesis and
RT erythropoiesis.";
RL Cell 161:858-867(2015).
CC -!- FUNCTION: ATP-dependent unfoldase that stimulates the incorporation of
CC the pyridoxal phosphate cofactor into 5-aminolevulinate synthase
CC (HEM1), thereby activating 5-aminolevulinate (ALA) synthesis, the first
CC step in heme biosynthesis. Up-regulates heme biosynthesis.
CC {ECO:0000269|PubMed:25957689}.
CC -!- SUBUNIT: Homohexamer that forms a ring structure; this hexamerization
CC requires ATP binding (By similarity). Interacts with HEM1
CC (PubMed:25957689). {ECO:0000250|UniProtKB:O76031,
CC ECO:0000269|PubMed:25957689}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:9827555}; Peripheral membrane protein
CC {ECO:0000269|PubMed:9827555}; Matrix side {ECO:0000269|PubMed:9827555}.
CC -!- DISRUPTION PHENOTYPE: 5-fold reduced production of the first heme
CC precursor 5-aminolevulinic acid (ALA) and 2-fold reduction in total
CC heme. In combination with a disruption of HEM25 or an inactivated HEM1,
CC abrogates mitochondrial respiration. {ECO:0000269|PubMed:25957689}.
CC -!- MISCELLANEOUS: Present with 10900 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000305}.
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DR EMBL; Z36096; CAA85190.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07342.1; -; Genomic_DNA.
DR PIR; S46103; S46103.
DR RefSeq; NP_009786.1; NM_001178575.1.
DR AlphaFoldDB; P38323; -.
DR SMR; P38323; -.
DR BioGRID; 32922; 134.
DR DIP; DIP-6422N; -.
DR IntAct; P38323; 4.
DR MINT; P38323; -.
DR STRING; 4932.YBR227C; -.
DR iPTMnet; P38323; -.
DR MaxQB; P38323; -.
DR PaxDb; P38323; -.
DR PRIDE; P38323; -.
DR EnsemblFungi; YBR227C_mRNA; YBR227C; YBR227C.
DR GeneID; 852528; -.
DR KEGG; sce:YBR227C; -.
DR SGD; S000000431; MCX1.
DR VEuPathDB; FungiDB:YBR227C; -.
DR eggNOG; KOG0745; Eukaryota.
DR GeneTree; ENSGT00390000017625; -.
DR HOGENOM; CLU_014218_1_2_1; -.
DR InParanoid; P38323; -.
DR OMA; HYKRVQA; -.
DR BioCyc; YEAST:G3O-29160-MON; -.
DR PRO; PR:P38323; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38323; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IDA:SGD.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:SGD.
DR GO; GO:1904287; P:positive regulation of protein-pyridoxal-5-phosphate linkage; IDA:SGD.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IMP:SGD.
DR GO; GO:0042026; P:protein refolding; IMP:SGD.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..13
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 14..520
FT /note="ATP-dependent clpX-like chaperone, mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000160569"
FT BINDING 140..147
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00499"
FT MUTAGEN 174
FT /note="Y->A: Abrogates unfolding activity of unfoldase.
FT Mildly increased ATPase activity. Reduces ALA synthesis."
FT /evidence="ECO:0000269|PubMed:25957689"
FT MUTAGEN 206
FT /note="E->Q: Blocks ATP hydrolysis."
FT /evidence="ECO:0000305|PubMed:25957689"
SQ SEQUENCE 520 AA; 57946 MW; A054D1618CD50A26 CRC64;
MLKSASQNFF RAYSSRIGRY AATASGKLAQ SRLSNIPTPK ALKKFLDEYI VGQEIGKKVL
SVAVYNHYLR INDKQKKGEL QRQRELMERE KIADDRDEPI FSGNSESKAG WRNLQRQFNL
AGREVDEDLE LSKSNVLVVG PSGSGKTLLA TTLAKILNVP IAITDCTQLT QAGYIGEDVE
VCIERLLVNA EFDVARAEKG IIVLDEIDKL AKPAASIGTK DVSGEGVQQS LLKIIEGHKV
EITVKRPVKH DIDGQKNQTT TKKDEVFVVD TSNILFMIMG AFVGLDKHIV KRIEDMKKIQ
KAGESVESSN SKEVEKERAK KFRFSNTLEQ VELDNGKKVC ALDLTTPTDL VSFGLIPELI
GRVPIITALQ PLQRDDLFHI LKEPKNALLD QYEYIFKQFG VRLCVTQKAL KKVAQFALKE
GTGARGLRGI MERLLLNVNY DCPGSNIAYV LIDEATVDSL QETEHSLASQ VDVKYYSGDE
KDSLIRDVSE EDKKLGVMLE KELGHSANIH TPTIPKRSLT
