GRPE_YEAST
ID GRPE_YEAST Reviewed; 228 AA.
AC P38523; D6W2T6;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=GrpE protein homolog, mitochondrial;
DE Flags: Precursor;
GN Name=MGE1; Synonyms=GRPE, GRPE1, YGE1; OrderedLocusNames=YOR232W;
GN ORFNames=O5099;
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 [GENOMIC DNA], AND PROTEIN SEQUENCE OF 50-66; 91-96 AND
RP 109-116.
RX PubMed=8168496; DOI=10.1002/j.1460-2075.1994.tb06469.x;
RA Bolliger L., Deloche O., Glick B.S., Georgopoulos C., Jenoe P.,
RA Kronidou N., Horst M., Morishima N., Schatz G.;
RT "A mitochondrial homolog of bacterial GrpE interacts with mitochondrial
RT hsp70 and is essential for viability.";
RL EMBO J. 13:1998-2006(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 26786 / X2180-1A;
RX PubMed=8112465; DOI=10.1016/0014-5793(94)80428-1;
RA Ikeda E., Yoshida S., Mitsuzawa H., Uno I., Toh-e A.;
RT "YGE1 is a yeast homologue of Escherichia coli grpE and is required for
RT maintenance of mitochondrial functions.";
RL FEBS Lett. 339:265-268(1994).
RN [3]
RP ERRATUM OF PUBMED:8112465.
RA Ikeda E., Yoshida S., Mitsuzawa H., Uno I., Toh-e A.;
RL FEBS Lett. 343:181-181(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8022808; DOI=10.1073/pnas.91.14.6481;
RA Laloraya S., Gambill D.B., Craig E.A.;
RT "A role for a eukaryotic GrpE-related protein, Mge1p, in protein
RT translocation.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:6481-6485(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8972580;
RX DOI=10.1002/(sici)1097-0061(199612)12:15<1575::aid-yea45>3.0.co;2-e;
RA Boyer J., Michaux G., Fairhead C., Gaillon L., Dujon B.;
RT "Sequence and analysis of a 26.9 kb fragment from chromosome XV of the
RT yeast Saccharomyces cerevisiae.";
RL Yeast 12:1575-1586(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [7]
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 [8]
RP FUNCTION.
RX PubMed=7628446; DOI=10.1002/j.1460-2075.1995.tb07351.x;
RA Westermann B., Prip-Buus C., Neupert W., Schwarz E.;
RT "The role of the GrpE homologue, Mge1p, in mediating protein import and
RT protein folding in mitochondria.";
RL EMBO J. 14:3452-3460(1995).
RN [9]
RP INTERACTION WITH SSQ1.
RX PubMed=11273703; DOI=10.1006/jmbi.2001.4527;
RA Lutz T., Westermann B., Neupert W., Herrmann J.M.;
RT "The mitochondrial proteins Ssq1 and Jac1 are required for the assembly of
RT iron sulfur clusters in mitochondria.";
RL J. Mol. Biol. 307:815-825(2001).
RN [10]
RP IDENTIFICATION IN THE PAM COMPLEX WITH PAM16; PAM17; PAM18; TIM44 AND SSC1.
RX PubMed=16107694; DOI=10.1128/mcb.25.17.7449-7458.2005;
RA van der Laan M., Chacinska A., Lind M., Perschil I., Sickmann A.,
RA Meyer H.E., Guiard B., Meisinger C., Pfanner N., Rehling P.;
RT "Pam17 is required for architecture and translocation activity of the
RT mitochondrial protein import motor.";
RL Mol. Cell. Biol. 25:7449-7458(2005).
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. Seems to control the nucleotide-dependent binding of SSC1 to
CC substrate proteins and the association of SSC1 with TIM44.
CC {ECO:0000269|PubMed:7628446}.
CC -!- SUBUNIT: Component of the PAM complex, at least composed of SSC1
CC (mtHsp70), MGE1, TIM44, PAM16/TIM16, PAM17 and PAM18/TIM14. Interacts
CC with SSQ1. {ECO:0000269|PubMed:11273703, ECO:0000269|PubMed:16107694}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000305|PubMed:16107694}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000305}.
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DR EMBL; X78350; CAA55145.1; -; Genomic_DNA.
DR EMBL; D26059; BAA05058.1; -; Genomic_DNA.
DR EMBL; U09565; AAA19253.1; -; Unassigned_RNA.
DR EMBL; Z75140; CAA99452.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11002.1; -; Genomic_DNA.
DR PIR; S41760; S41760.
DR RefSeq; NP_014875.3; NM_001183651.3.
DR AlphaFoldDB; P38523; -.
DR SMR; P38523; -.
DR BioGRID; 34625; 351.
DR ComplexPortal; CPX-539; TIM23 mitochondrial inner membrane pre-sequence translocase complex, motor variant.
DR DIP; DIP-775N; -.
DR IntAct; P38523; 22.
DR MINT; P38523; -.
DR STRING; 4932.YOR232W; -.
DR TCDB; 3.A.8.1.1; the mitochondrial protein translocase (mpt) family.
DR iPTMnet; P38523; -.
DR MetOSite; P38523; -.
DR MaxQB; P38523; -.
DR PaxDb; P38523; -.
DR PRIDE; P38523; -.
DR EnsemblFungi; YOR232W_mRNA; YOR232W; YOR232W.
DR GeneID; 854407; -.
DR KEGG; sce:YOR232W; -.
DR SGD; S000005758; MGE1.
DR VEuPathDB; FungiDB:YOR232W; -.
DR eggNOG; KOG3003; Eukaryota.
DR GeneTree; ENSGT00390000005589; -.
DR HOGENOM; CLU_057217_0_0_1; -.
DR InParanoid; P38523; -.
DR OMA; YAYEKIA; -.
DR BioCyc; YEAST:G3O-33730-MON; -.
DR PRO; PR:P38523; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P38523; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0001405; C:PAM complex, Tim23 associated import motor; IDA:SGD.
DR GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; IC:ComplexPortal.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IDA:SGD.
DR GO; GO:0051087; F:chaperone binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IC:ComplexPortal.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IMP:SGD.
DR GO; GO:0042026; P:protein refolding; IDA:SGD.
DR CDD; cd00446; GrpE; 1.
DR Gene3D; 2.30.22.10; -; 1.
DR Gene3D; 3.90.20.20; -; 1.
DR HAMAP; MF_01151; GrpE; 1.
DR InterPro; IPR000740; GrpE.
DR InterPro; IPR013805; GrpE_coiled_coil.
DR InterPro; IPR009012; GrpE_head.
DR PANTHER; PTHR21237; PTHR21237; 1.
DR Pfam; PF01025; GrpE; 1.
DR PRINTS; PR00773; GRPEPROTEIN.
DR SUPFAM; SSF51064; SSF51064; 1.
DR SUPFAM; SSF58014; SSF58014; 1.
DR PROSITE; PS01071; GRPE; 1.
PE 1: Evidence at protein level;
KW Chaperone; Direct protein sequencing; Mitochondrion; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..228
FT /note="GrpE protein homolog, mitochondrial"
FT /id="PRO_0000013046"
FT REGION 46..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 228 AA; 26066 MW; 816A5E26C648E613 CRC64;
MRAFSAATVR ATTRKSFIPM APRTPFVTPS FTKNVGSMRR MRFYSDEAKS EESKENNEDL
TEEQSEIKKL ESQLSAKTKE ASELKDRLLR SVADFRNLQQ VTKKDIQKAK DFALQKFAKD
LLESVDNFGH ALNAFKEEDL QKSKEISDLY TGVRMTRDVF ENTLRKHGIE KLDPLGEPFD
PNKHEATFEL PQPDKEPGTV FHVQQLGFTL NDRVIRPAKV GIVKGEEN
