GRPE_CAMJE
ID GRPE_CAMJE Reviewed; 176 AA.
AC O69297; Q0PAD2; Q9PPG1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 103.
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=Cj0758;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10024560; DOI=10.1128/iai.67.3.1194-1200.1999;
RA Thies F., Karch H., Hartung H.P., Giegerich G.;
RT "Cloning and expression of the dnaK gene of Campylobacter jejuni and
RT antigenicity of heat shock protein 70.";
RL Infect. Immun. 67:1194-1200(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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; Y17165; CAA76669.1; -; Genomic_DNA.
DR EMBL; AL111168; CAL34886.1; -; Genomic_DNA.
DR PIR; F81346; F81346.
DR RefSeq; WP_002780052.1; NC_002163.1.
DR RefSeq; YP_002344165.1; NC_002163.1.
DR AlphaFoldDB; O69297; -.
DR SMR; O69297; -.
DR IntAct; O69297; 67.
DR STRING; 192222.Cj0758; -.
DR PaxDb; O69297; -.
DR PRIDE; O69297; -.
DR EnsemblBacteria; CAL34886; CAL34886; Cj0758.
DR GeneID; 905068; -.
DR KEGG; cje:Cj0758; -.
DR PATRIC; fig|192222.6.peg.746; -.
DR eggNOG; COG0576; Bacteria.
DR HOGENOM; CLU_057217_6_3_7; -.
DR OMA; YAYEKIA; -.
DR Proteomes; UP000000799; 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 3: Inferred from homology;
KW Chaperone; Cytoplasm; Reference proteome; Stress response.
FT CHAIN 1..176
FT /note="Protein GrpE"
FT /id="PRO_0000113763"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 3
FT /note="E -> D (in Ref. 1; CAA76669)"
FT /evidence="ECO:0000305"
FT CONFLICT 10
FT /note="N -> T (in Ref. 1; CAA76669)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 176 AA; 20368 MW; 7DCF13E3852E2421 CRC64;
MSEQKQEFEN ENAENSEHLQ DENLQNIEDV EQNKLQKDYD ELKDKYMRAN AEFENIKKRM
EKEKLSAMAY ANESFAKDLL DVLDALEAAV NVECQDEISL KIKEGVQNTL DLFLKKLEKH
GVALIKDEKE FDPNLHEAMF HVDSENHQSG EVVQVLQKGY KIADRVIRPT KVSVAK
