ID   GRPE_ECOLI              Reviewed;         197 AA.
AC   P09372;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   24-JAN-2024, entry version 187.
DE   RecName: Full=Protein GrpE;
DE   AltName: Full=HSP-70 cofactor;
DE   AltName: Full=HSP24;
DE   AltName: Full=Heat shock protein B25.3;
GN   Name=grpE; OrderedLocusNames=b2614, JW2594;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B178;
RX   PubMed=3045760; DOI=10.1093/nar/16.15.7545;
RA   Lipinska B., King J., Ang D., Georgopoulos C.;
RT   "Sequence analysis and transcriptional regulation of the Escherichia coli
RT   grpE gene, encoding a heat shock protein.";
RL   Nucleic Acids Res. 16:7545-7562(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA   Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA   Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA   Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA   Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT   "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT   genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT   its sequence features.";
RL   DNA Res. 4:91-113(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   POSSIBLE FUNCTION.
RX   PubMed=1826368; DOI=10.1073/pnas.88.7.2874;
RA   Liberek K., Marszalek J., Ang D., Georgopoulos C., Zylicz M.;
RT   "Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate
RT   ATPase activity of DnaK.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:2874-2878(1991).
RN   [6]
RP   FUNCTION, AND MUTAGENESIS.
RX   PubMed=8890154; DOI=10.1002/j.1460-2075.1996.tb00861.x;
RA   Wu B., Wawrzynow A., Zylicz M., Georgopoulos C.;
RT   "Structure-function analysis of the Escherichia coli GrpE heat shock
RT   protein.";
RL   EMBO J. 15:4806-4816(1996).
RN   [7]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
RN   [8]
RP   POSSIBLE ROLE IN PEPTIDE RELEASE FROM DNAK.
RX   PubMed=11401497; DOI=10.1006/bbrc.2001.4567;
RA   Mehl A.F., Heskett L.D., Neal K.M.;
RT   "A GrpE mutant containing the NH(2)-terminal 'tail' region is able to
RT   displace bound polypeptide substrate from DnaK.";
RL   Biochem. Biophys. Res. Commun. 282:562-569(2001).
RN   [9]
RP   POSSIBLE ROLE AS A THERMOSENSOR.
RX   PubMed=12639955; DOI=10.1074/jbc.m300924200;
RA   Grimshaw J.P., Jelesarov I., Siegenthaler R.K., Christen P.;
RT   "Thermosensor action of GrpE. The DnaK chaperone system at heat shock
RT   temperatures.";
RL   J. Biol. Chem. 278:19048-19053(2003).
RN   [10]
RP   ROLE IN DNAK INTERACTION WITH SUBSTRATE.
RX   PubMed=15102842; DOI=10.1074/jbc.m403558200;
RA   Brehmer D., Gaessler C., Rist W., Mayer M.P., Bukau B.;
RT   "Influence of GrpE on DnaK-substrate interactions.";
RL   J. Biol. Chem. 279:27957-27964(2004).
RN   [11]
RP   MUTAGENESIS OF PHE-86; ARG-183 AND VAL-192.
RX   PubMed=12885238; DOI=10.1021/bi034416b;
RA   Gelinas A.D., Toth J., Bethoney K.A., Langsetmo K., Stafford W.F.,
RA   Harrison C.J.;
RT   "Thermodynamic linkage in the GrpE nucleotide exchange factor, a molecular
RT   thermosensor.";
RL   Biochemistry 42:9050-9059(2003).
RN   [12]
RP   MUTAGENESIS OF ARG-73; ARG-74; LYS-82; ARG-104; GLU-107; VAL-108; LEU-149;
RP   PRO-151; GLN-155; ILE-157; MET-159; MET-174; ARG-183 AND VAL-192.
RX   PubMed=15136046; DOI=10.1016/j.jmb.2004.03.074;
RA   Gelinas A.D., Toth J., Bethoney K.A., Stafford W.F., Harrison C.J.;
RT   "Mutational analysis of the energetics of the GrpE.DnaK binding interface:
RT   equilibrium association constants by sedimentation velocity analytical
RT   ultracentrifugation.";
RL   J. Mol. Biol. 339:447-458(2004).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH ATPASE DOMAIN OF
RP   DNAK, AND MUTAGENESIS OF GLY-122.
RX   PubMed=9103205; DOI=10.1126/science.276.5311.431;
RA   Harrison C.J., Hayer-Hartl M., di Liberto M., Hartl F.-U., Kuriyan J.;
RT   "Crystal structure of the nucleotide exchange factor GrpE bound to the
RT   ATPase domain of the molecular chaperone DnaK.";
RL   Science 276:431-435(1997).
CC   -!- FUNCTION: Participates actively in the response to hyperosmotic and
CC       heat shock by preventing the aggregation of stress-denatured proteins,
CC       in association with DnaK and GrpE. It is the nucleotide exchange factor
CC       for DnaK and may function as a thermosensor. Unfolded proteins bind
CC       initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK
CC       hydrolyzes its bound ATP, resulting in the formation of a stable
CC       complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the
CC       release of the substrate protein, thus completing the reaction cycle.
CC       Several rounds of ATP-dependent interactions between DnaJ, DnaK and
CC       GrpE are required for fully efficient folding.
CC       {ECO:0000269|PubMed:15102842, ECO:0000269|PubMed:8890154}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9103205}.
CC   -!- INTERACTION:
CC       P09372; P0A6Y8: dnaK; NbExp=10; IntAct=EBI-547441, EBI-542092;
CC       P09372; P0A6F5: groEL; NbExp=3; IntAct=EBI-547441, EBI-543750;
CC       P09372; P0A769: mntH; NbExp=3; IntAct=EBI-547441, EBI-551337;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: By the sigma(32) subunit of RNA polymerase.
CC   -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000305}.
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DR   EMBL; X07863; CAA30711.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75663.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16498.1; -; Genomic_DNA.
DR   PIR; S01240; S01240.
DR   RefSeq; NP_417104.1; NC_000913.3.
DR   RefSeq; WP_001393454.1; NZ_LN832404.1.
DR   PDB; 1DKG; X-ray; 2.80 A; A/B=1-197.
DR   PDBsum; 1DKG; -.
DR   AlphaFoldDB; P09372; -.
DR   SMR; P09372; -.
DR   BioGRID; 4260616; 160.
DR   BioGRID; 851433; 2.
DR   DIP; DIP-6141N; -.
DR   IntAct; P09372; 50.
DR   STRING; 511145.b2614; -.
DR   ChEMBL; CHEMBL1293284; -.
DR   jPOST; P09372; -.
DR   PaxDb; 511145-b2614; -.
DR   EnsemblBacteria; AAC75663; AAC75663; b2614.
DR   GeneID; 947097; -.
DR   KEGG; ecj:JW2594; -.
DR   KEGG; eco:b2614; -.
DR   PATRIC; fig|1411691.4.peg.4126; -.
DR   EchoBASE; EB0411; -.
DR   eggNOG; COG0576; Bacteria.
DR   HOGENOM; CLU_057217_6_0_6; -.
DR   InParanoid; P09372; -.
DR   OMA; YAYEKIA; -.
DR   OrthoDB; 9789811at2; -.
DR   PhylomeDB; P09372; -.
DR   BioCyc; EcoCyc:EG10416-MONOMER; -.
DR   BioCyc; MetaCyc:EG10416-MONOMER; -.
DR   EvolutionaryTrace; P09372; -.
DR   PRO; PR:P09372; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; HDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR   GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IDA:EcoCyc.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IDA:EcoCyc.
DR   GO; GO:0043335; P:protein unfolding; IDA:EcoCyc.
DR   GO; GO:0065003; P:protein-containing complex assembly; IMP:CAFA.
DR   GO; GO:0009408; P:response to heat; IDA:EcoCyc.
DR   CDD; cd00446; GrpE; 1.
DR   DisProt; DP00103; -.
DR   Gene3D; 3.90.20.20; -; 1.
DR   Gene3D; 2.30.22.10; Head domain of nucleotide exchange factor GrpE; 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; GRPE PROTEIN; 1.
DR   PANTHER; PTHR21237:SF23; GRPE PROTEIN HOMOLOG, MITOCHONDRIAL; 1.
DR   Pfam; PF01025; GrpE; 1.
DR   PRINTS; PR00773; GRPEPROTEIN.
DR   SUPFAM; SSF58014; Coiled-coil domain of nucleotide exchange factor GrpE; 1.
DR   SUPFAM; SSF51064; Head domain of nucleotide exchange factor GrpE; 1.
DR   PROSITE; PS01071; GRPE; 1.
DR   SWISS-2DPAGE; P09372; -.
PE   1: Evidence at protein level;
KW   3D-structure; Chaperone; Cytoplasm; Reference proteome; Stress response.
FT   CHAIN           1..197
FT                   /note="Protein GrpE"
FT                   /id="PRO_0000113782"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..40
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            183
FT                   /note="Interaction with DnaK"
FT   MUTAGEN         73
FT                   /note="R->A: Great decrease in ability to interact with
FT                   DnaK."
FT                   /evidence="ECO:0000269|PubMed:15136046"
FT   MUTAGEN         74
FT                   /note="R->A: Great decrease in ability to interact with
FT                   DnaK."
FT                   /evidence="ECO:0000269|PubMed:15136046"
FT   MUTAGEN         82
FT                   /note="K->A: Great decrease in ability to interact with
FT                   DnaK."
FT                   /evidence="ECO:0000269|PubMed:15136046"
FT   MUTAGEN         86
FT                   /note="F->A: No effect in ability to interact with DnaK."
FT                   /evidence="ECO:0000269|PubMed:12885238"
FT   MUTAGEN         104
FT                   /note="R->A: No effect in ability to interact with DnaK."
FT                   /evidence="ECO:0000269|PubMed:15136046"
FT   MUTAGEN         107
FT                   /note="E->A: No effect in ability to interact with DnaK."
FT                   /evidence="ECO:0000269|PubMed:15136046"
FT   MUTAGEN         108
FT                   /note="V->A: No effect in ability to interact with DnaK."
FT                   /evidence="ECO:0000269|PubMed:15136046"
FT   MUTAGEN         122
FT                   /note="G->D: Temperature-sensitive phenotype."
FT                   /evidence="ECO:0000269|PubMed:9103205"
FT   MUTAGEN         149
FT                   /note="L->A: No effect in ability to interact with DnaK."
FT                   /evidence="ECO:0000269|PubMed:15136046"
FT   MUTAGEN         151
FT                   /note="P->A: No effect in ability to interact with DnaK."
FT                   /evidence="ECO:0000269|PubMed:15136046"
FT   MUTAGEN         155
FT                   /note="Q->A: No effect in ability to interact with DnaK."
FT                   /evidence="ECO:0000269|PubMed:15136046"
FT   MUTAGEN         157
FT                   /note="I->A: No effect in ability to interact with DnaK."
FT                   /evidence="ECO:0000269|PubMed:15136046"
FT   MUTAGEN         159
FT                   /note="M->A: No effect in ability to interact with DnaK."
FT                   /evidence="ECO:0000269|PubMed:15136046"
FT   MUTAGEN         174
FT                   /note="M->A: No effect in ability to interact with DnaK."
FT                   /evidence="ECO:0000269|PubMed:15136046"
FT   MUTAGEN         183
FT                   /note="R->A: Loss of ability to interact with DnaK."
FT                   /evidence="ECO:0000269|PubMed:12885238,
FT                   ECO:0000269|PubMed:15136046"
FT   MUTAGEN         186
FT                   /note="R->A: No effect in ability to interact with DnaK."
FT                   /evidence="ECO:0000269|PubMed:8890154"
FT   MUTAGEN         189
FT                   /note="M->A: No effect in ability to interact with DnaK."
FT                   /evidence="ECO:0000269|PubMed:8890154"
FT   MUTAGEN         192
FT                   /note="V->A: Loss of ability to interact with DnaK."
FT                   /evidence="ECO:0000269|PubMed:12885238,
FT                   ECO:0000269|PubMed:15136046"
FT   HELIX           39..85
FT                   /evidence="ECO:0007829|PDB:1DKG"
FT   HELIX           88..90
FT                   /evidence="ECO:0007829|PDB:1DKG"
FT   HELIX           91..94
FT                   /evidence="ECO:0007829|PDB:1DKG"
FT   HELIX           96..107
FT                   /evidence="ECO:0007829|PDB:1DKG"
FT   HELIX           117..134
FT                   /evidence="ECO:0007829|PDB:1DKG"
FT   TURN            135..138
FT                   /evidence="ECO:0007829|PDB:1DKG"
FT   STRAND          139..142
FT                   /evidence="ECO:0007829|PDB:1DKG"
FT   STRAND          146..148
FT                   /evidence="ECO:0007829|PDB:1DKG"
FT   STRAND          153..161
FT                   /evidence="ECO:0007829|PDB:1DKG"
FT   STRAND          163..165
FT                   /evidence="ECO:0007829|PDB:1DKG"
FT   STRAND          169..175
FT                   /evidence="ECO:0007829|PDB:1DKG"
FT   STRAND          177..180
FT                   /evidence="ECO:0007829|PDB:1DKG"
FT   STRAND          183..186
FT                   /evidence="ECO:0007829|PDB:1DKG"
FT   STRAND          188..194
FT                   /evidence="ECO:0007829|PDB:1DKG"
SQ   SEQUENCE   197 AA;  21798 MW;  CDC4CD9D08AD4BEF CRC64;
     MSSKEQKTPE GQAPEEIIMD QHEEIEAVEP EASAEQVDPR DEKVANLEAQ LAEAQTRERD
     GILRVKAEME NLRRRTELDI EKAHKFALEK FINELLPVID SLDRALEVAD KANPDMSAMV
     EGIELTLKSM LDVVRKFGVE VIAETNVPLD PNVHQAIAMV ESDDVAPGNV LGIMQKGYTL
     NGRTIRAAMV TVAKAKA
//