GRPE_STRMU
ID GRPE_STRMU Reviewed; 179 AA.
AC O06941;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 121.
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=SMU_81;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GS-5;
RX PubMed=9282745; DOI=10.1046/j.1365-2958.1997.4671835.x;
RA Jayaraman G.C., Penders J.E., Burne R.A.;
RT "Transcriptional analysis of the Streptococcus mutans hrcA, grpE and dnaK
RT genes and regulation of expression in response to heat shock and
RT environmental acidification.";
RL Mol. Microbiol. 25:329-341(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(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; U78296; AAC45611.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN57866.1; -; Genomic_DNA.
DR RefSeq; NP_720560.1; NC_004350.2.
DR RefSeq; WP_002263416.1; NC_004350.2.
DR AlphaFoldDB; O06941; -.
DR SMR; O06941; -.
DR STRING; 210007.SMU_81; -.
DR PRIDE; O06941; -.
DR EnsemblBacteria; AAN57866; AAN57866; SMU_81.
DR KEGG; smu:SMU_81; -.
DR PATRIC; fig|210007.7.peg.70; -.
DR eggNOG; COG0576; Bacteria.
DR HOGENOM; CLU_057217_6_3_9; -.
DR OMA; YAYEKIA; -.
DR PhylomeDB; O06941; -.
DR Proteomes; UP000002512; 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..179
FT /note="Protein GrpE"
FT /id="PRO_0000113870"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 10
FT /note="I -> Y (in Ref. 1; AAC45611)"
FT /evidence="ECO:0000305"
FT CONFLICT 60..73
FT /note="QNIQRRANEERQSL -> PKTFSVALMKSDKVC (in Ref. 1;
FT AAC45611)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="A -> R (in Ref. 1; AAC45611)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="P -> A (in Ref. 1; AAC45611)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="L -> H (in Ref. 1; AAC45611)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 179 AA; 20576 MW; B118B7C9DCA7272D CRC64;
MSKKDKKEEI KEEVEATEPT TEESVEEVAE ETSENKELQE ALERAEDFEN KYLRAHAEMQ
NIQRRANEER QSLQRYRSQD LAKAILPSLD NLERALAVEG LTDDVKKGLE MVQESLIQAL
KEEGVEEVEL ENFDPNLHMA VQTLDADDDH PADSIAQVLQ KGYQLHERLL RPAMVVVYN
