GRPE_THET8
ID GRPE_THET8 Reviewed; 177 AA.
AC Q56236; P74895; Q5SI84;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 113.
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}; OrderedLocusNames=TTHA1490;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9349721; DOI=10.1016/s0167-4781(97)00071-7;
RA Osipiuk J., Joachimiak A.;
RT "Cloning, sequencing, and expression of dnaK-operon proteins from the
RT thermophilic bacterium Thermus thermophilus.";
RL Biochim. Biophys. Acta 1353:253-265(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8663379; DOI=10.1074/jbc.271.29.17343;
RA Motohashi K., Yohda M., Endo I., Yoshida M.;
RT "A novel factor required for the assembly of the DnaK and DnaJ chaperones
RT of Thermus thermophilus.";
RL J. Biol. Chem. 271:17343-17348(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Seidel R.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-8, AND POTASSIUM
RP REQUIREMENT.
RX PubMed=9276481; DOI=10.1016/s0014-5793(97)00847-8;
RA Motohashi K., Yohda M., Odaka M., Yoshida M.;
RT "K+ is an indispensable cofactor for GrpE stimulation of ATPase activity of
RT DnaK/DnaJ complex from Thermus thermophilus.";
RL FEBS Lett. 412:633-636(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Note=Required to stimulate the ATPase activity of DnaK.;
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01151}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000255|HAMAP-
CC Rule:MF_01151}.
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DR EMBL; L57504; AAB04677.1; -; Genomic_DNA.
DR EMBL; D84222; BAA12281.1; -; Genomic_DNA.
DR EMBL; Y07826; CAA69160.1; -; Genomic_DNA.
DR EMBL; AB012390; BAA81742.1; -; Genomic_DNA.
DR EMBL; AB032368; BAA96088.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD71313.1; -; Genomic_DNA.
DR RefSeq; WP_011228714.1; NC_006461.1.
DR RefSeq; YP_144756.1; NC_006461.1.
DR PDB; 3A6M; X-ray; 3.23 A; A/B=1-177.
DR PDBsum; 3A6M; -.
DR AlphaFoldDB; Q56236; -.
DR SMR; Q56236; -.
DR STRING; 300852.55772872; -.
DR EnsemblBacteria; BAD71313; BAD71313; BAD71313.
DR GeneID; 3169984; -.
DR KEGG; ttj:TTHA1490; -.
DR PATRIC; fig|300852.9.peg.1465; -.
DR eggNOG; COG0576; Bacteria.
DR HOGENOM; CLU_057217_6_3_0; -.
DR OMA; YAYEKIA; -.
DR PhylomeDB; Q56236; -.
DR EvolutionaryTrace; Q56236; -.
DR Proteomes; UP000000532; Chromosome.
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 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Direct protein sequencing;
KW Reference proteome; Stress response.
FT CHAIN 1..177
FT /note="Protein GrpE"
FT /id="PRO_0000113884"
FT CONFLICT 18..22
FT /note="GQEAQ -> ARRPM (in Ref. 2; BAA12281)"
FT /evidence="ECO:0000305"
FT TURN 5..7
FT /evidence="ECO:0007829|PDB:3A6M"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:3A6M"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:3A6M"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:3A6M"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:3A6M"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:3A6M"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:3A6M"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:3A6M"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:3A6M"
FT TURN 44..51
FT /evidence="ECO:0007829|PDB:3A6M"
FT HELIX 52..87
FT /evidence="ECO:0007829|PDB:3A6M"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:3A6M"
FT HELIX 93..113
FT /evidence="ECO:0007829|PDB:3A6M"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:3A6M"
FT STRAND 131..140
FT /evidence="ECO:0007829|PDB:3A6M"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:3A6M"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:3A6M"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:3A6M"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:3A6M"
SQ SEQUENCE 177 AA; 20027 MW; 50AB3E3AA00DB17A CRC64;
MEERNHENTL EKDLEAVGQE AQALEERLKA AEEELKGLKD KYLRLLADFD NYRKRMEEEL
KAREREGVLK ALRALLPVLD DLDRALEFAE ASPESIRQGV RAIRDGFFRI LAGLGVEEVP
GEGEAFDPRY HEAVGLLPGE PGKVAKVFQR GFRMGEALVR PARVAVGEEK REEADLE
