ID   GRPE_TETHA              Reviewed;         191 AA.
AC   Q93R28;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Protein GrpE {ECO:0000255|HAMAP-Rule:MF_01151};
DE   AltName: Full=HSP-70 cofactor {ECO:0000255|HAMAP-Rule:MF_01151};
GN   Name=grpE {ECO:0000255|HAMAP-Rule:MF_01151};
OS   Tetragenococcus halophilus (Pediococcus halophilus).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Tetragenococcus.
OX   NCBI_TaxID=51669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12092841; DOI=10.1271/bbb.66.1176;
RA   Fukuda D., Watanabe M., Aso Y., Sonomoto K., Ishizaki A.;
RT   "The groESL operon of the halophilic lactic acid bacterium Tetragenococcus
RT   halophila.";
RL   Biosci. Biotechnol. Biochem. 66:1176-1180(2002).
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. {ECO:0000255|HAMAP-
CC       Rule:MF_01151}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01151}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01151}.
CC   -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000255|HAMAP-
CC       Rule:MF_01151}.
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DR   EMBL; AB070346; BAB63289.1; -; Genomic_DNA.
DR   RefSeq; WP_014124679.1; NZ_CP046246.1.
DR   AlphaFoldDB; Q93R28; -.
DR   SMR; Q93R28; -.
DR   GeneID; 64053906; -.
DR   OMA; YAYEKIA; -.
DR   OrthoDB; 1906715at2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0051087; F:chaperone binding; IEA:InterPro.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
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; Cytoplasm; Stress response.
FT   CHAIN           1..191
FT                   /note="Protein GrpE"
FT                   /id="PRO_0000113881"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   191 AA;  21731 MW;  5C459A29A259A17B CRC64;
     MSDKKKNAEE FEETFSDKTS EDESTVENET VEENENEDVQ AISEVDDLKA QLDEMEDKYL
     RASAELSNMN NRFRNERQTL QRYRSQDLGK KLLPAIDNLE RAVAIEVEGE QNESLKKGVE
     MTLESLRSAM QEEGIEEISA QGETFDPTLH QAVQTVPATE DHPAETVVEV LQKGYKIYDR
     VLRASMVVVA Q