GRPE_STRPN
ID GRPE_STRPN Reviewed; 174 AA.
AC Q97S73; Q9X4R3;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=SP_0516;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-117.
RC STRAIN=Rx / CP1200;
RA Kim S.N., Kim S.W., Choi I.H., Rhee D.K.;
RL Submitted (JAN-1999) 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 -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01151}.
CC -!- INTERACTION:
CC Q97S73; P0A2W6: acpS; NbExp=2; IntAct=EBI-2207065, EBI-2207344;
CC Q97S73; P63544: apt; NbExp=2; IntAct=EBI-2207065, EBI-2207316;
CC Q97S73; P95830: dnaJ; NbExp=2; IntAct=EBI-2207065, EBI-2207079;
CC Q97S73; Q97QS2: eno; NbExp=2; IntAct=EBI-2207065, EBI-2207206;
CC Q97S73; Q97SE5: gatC; NbExp=2; IntAct=EBI-2207065, EBI-2207053;
CC Q97S73; Q97NV3: groES; NbExp=2; IntAct=EBI-2207065, EBI-2206949;
CC Q97S73; P65144: infC; NbExp=2; IntAct=EBI-2207065, EBI-2207149;
CC Q97S73; P41354: mutX; NbExp=2; IntAct=EBI-2207065, EBI-2207232;
CC Q97S73; P65887: purA; NbExp=2; IntAct=EBI-2207065, EBI-2206955;
CC Q97S73; Q97SR4: uppS; NbExp=2; IntAct=EBI-2207065, EBI-2206983;
CC Q97S73; Q97QP2: xerS; NbExp=2; IntAct=EBI-2207065, EBI-2207218;
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; AE005672; AAK74674.1; -; Genomic_DNA.
DR EMBL; AF117740; AAD23453.1; -; Genomic_DNA.
DR PIR; A95060; A95060.
DR RefSeq; WP_000046044.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; Q97S73; -.
DR SMR; Q97S73; -.
DR IntAct; Q97S73; 11.
DR STRING; 170187.SP_0516; -.
DR EnsemblBacteria; AAK74674; AAK74674; SP_0516.
DR KEGG; spn:SP_0516; -.
DR eggNOG; COG0576; Bacteria.
DR OMA; YAYEKIA; -.
DR PhylomeDB; Q97S73; -.
DR BioCyc; SPNE170187:G1FZB-531-MON; -.
DR Proteomes; UP000000585; 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 Chaperone; Cytoplasm; Stress response.
FT CHAIN 1..174
FT /note="Protein GrpE"
FT /id="PRO_0000113871"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 20
FT /note="K -> E (in Ref. 2; AAD23453)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="G -> A (in Ref. 2; AAD23453)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 174 AA; 19968 MW; D5F71A0057275574 CRC64;
MAQDIKNEEV EEVQEEEVVK TAEETTPEKS ELDLANERAD EFENKYLRAH AEMQNIQRRA
NEERQNLQRY RSQDLAKAIL PSLDNLERAL AVEGLTDDVK KGLGMVQESL IHALKEEGIE
EIAADGEFDH NYHMAIQTLP ADDEHPVDTI AQVFQKGYKL HDRILRPAMV VVYN
