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GRPE_SCHPO
ID   GRPE_SCHPO              Reviewed;         223 AA.
AC   O43047;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=GrpE protein homolog, mitochondrial;
DE   Flags: Precursor;
GN   Name=mge1; ORFNames=SPBC3B9.19;
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 [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).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the PAM complex, at least composed of mtHsp70,
CC       mge1, tim44, pam16, pam17 and pam18. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000305}.
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DR   EMBL; CU329671; CAA17799.1; -; Genomic_DNA.
DR   PIR; T40358; T40358.
DR   RefSeq; NP_596677.1; NM_001022599.2.
DR   AlphaFoldDB; O43047; -.
DR   SMR; O43047; -.
DR   BioGRID; 277554; 5.
DR   STRING; 4896.SPBC3B9.19.1; -.
DR   MaxQB; O43047; -.
DR   PaxDb; O43047; -.
DR   PRIDE; O43047; -.
DR   EnsemblFungi; SPBC3B9.19.1; SPBC3B9.19.1:pep; SPBC3B9.19.
DR   GeneID; 2541039; -.
DR   KEGG; spo:SPBC3B9.19; -.
DR   PomBase; SPBC3B9.19; mge1.
DR   VEuPathDB; FungiDB:SPBC3B9.19; -.
DR   eggNOG; KOG3003; Eukaryota.
DR   HOGENOM; CLU_057217_0_0_1; -.
DR   InParanoid; O43047; -.
DR   OMA; YAYEKIA; -.
DR   PhylomeDB; O43047; -.
DR   PRO; PR:O43047; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0001405; C:PAM complex, Tim23 associated import motor; IBA:GO_Central.
DR   GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; ISO:PomBase.
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; ISS:PomBase.
DR   GO; GO:0044571; P:[2Fe-2S] cluster assembly; ISO:PomBase.
DR   GO; GO:0006457; P:protein folding; ISO:PomBase.
DR   GO; GO:0030150; P:protein import into mitochondrial matrix; ISO:PomBase.
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   3: Inferred from homology;
KW   Chaperone; Mitochondrion; Reference proteome; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..223
FT                   /note="GrpE protein homolog, mitochondrial"
FT                   /id="PRO_0000013045"
SQ   SEQUENCE   223 AA;  25334 MW;  FC4CFF3458EF523C CRC64;
     MLGLGRVFSS AVRPRTLIRA PINKRSFLWY STEAAKEEKP AEEKVAETEN VDVKELQSKL
     SELKSKYEAK DKEVAELKGS IRQSLADYRN LENRMKRDME QTRAFAVQKL TKDLLDSVDN
     LERALSIVPE EKRNNRESNK DLVDLYEGLA MTESNLMKTL GKYGLVRYDG IGEDFDPNIH
     EAVFQIPVEG KKPNTVFHCE SKGFQLNGRV IRPAKVGVVK GDD
 
 
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