GRPE_ECOLI
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 03-AUG-2022, entry version 180.
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; Proteobacteria; 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 SWISS-2DPAGE; P09372; -.
DR jPOST; P09372; -.
DR PaxDb; P09372; -.
DR PRIDE; P09372; -.
DR EnsemblBacteria; AAC75663; AAC75663; b2614.
DR EnsemblBacteria; BAA16498; BAA16498; BAA16498.
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 PhylomeDB; P09372; -.
DR BioCyc; EcoCyc:EG10416-MON; -.
DR BioCyc; MetaCyc:EG10416-MON; -.
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:0051087; F:chaperone binding; IEA:InterPro.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
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; 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 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
