GRPE_STRCO
ID GRPE_STRCO Reviewed; 225 AA.
AC Q05562;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 25-MAY-2022, entry version 122.
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=SCO3670;
GN ORFNames=SCH44.10c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A3(2) / NRRL B-16638;
RX PubMed=8722574; DOI=10.3109/10425179609010207;
RA Brans A., Loriaux A., Joris B., Dusart J.;
RT "Cloning and sequencing of the dnaK locus in Streptomyces coelicolor
RT A3(2).";
RL DNA Seq. 6:179-184(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-166.
RC STRAIN=A3(2) / NRRL B-16638;
RX PubMed=8344522; DOI=10.1016/0378-1119(93)90358-a;
RA Bucca G., Smith C.P., Alberti M., Seidita G., Passantino R., Puglia A.M.;
RT "Cloning and sequencing of the dnaK region of Streptomyces coelicolor
RT A3(2).";
RL Gene 130:141-144(1993).
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; X77458; CAA54607.1; -; Genomic_DNA.
DR EMBL; L46700; AAB29452.1; -; Genomic_DNA.
DR EMBL; AL939117; CAB91161.1; -; Genomic_DNA.
DR PIR; S41947; PN0643.
DR RefSeq; NP_627863.1; NC_003888.3.
DR RefSeq; WP_003975269.1; NZ_VNID01000003.1.
DR AlphaFoldDB; Q05562; -.
DR SMR; Q05562; -.
DR STRING; 100226.SCO3670; -.
DR GeneID; 1099106; -.
DR KEGG; sco:SCO3670; -.
DR PATRIC; fig|100226.15.peg.3728; -.
DR eggNOG; COG0576; Bacteria.
DR HOGENOM; CLU_057217_4_2_11; -.
DR InParanoid; Q05562; -.
DR OMA; YAYEKIA; -.
DR PhylomeDB; Q05562; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0051087; F:chaperone binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
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..225
FT /note="Protein GrpE"
FT /id="PRO_0000113869"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 225 AA; 23874 MW; 7F61F78C4FB3FA9E CRC64;
MTEETPGFEE KPDVPSGATP DDAEPQAASE EGAAPAGDAS ENAGLVAQLD QVRTALNERT
ADLQRLQAEY QNYRRRVERD RVAVKEVAVA NLLSELLPVL DDVGRAREHG ELVGGFKSVA
ESLETTVAKL GLQQFGKEGE PFDPTIHEAL MHSYAPDVTE TTCVAILQPG YRIGERTIRP
ARVAVAEPQP GAQTVKPAED AAEAQDSSGA EDDAGTKESG GPDEG
