ID   GRPE_STRP6              Reviewed;         190 AA.
AC   Q5XAD5; P63190; P82581; Q99YC8;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Protein GrpE;
DE   AltName: Full=HSP-70 cofactor;
GN   Name=grpE; OrderedLocusNames=M6_Spy1493;
OS   Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=286636;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-946 / MGAS10394;
RX   PubMed=15272401; DOI=10.1086/422697;
RA   Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA   Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT   "Progress toward characterization of the group A Streptococcus metagenome:
RT   complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL   J. Infect. Dis. 190:727-738(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 47-55; 95-118 AND 180-190, AND MASS SPECTROMETRY.
RC   STRAIN=JRS4 / Serotype M6;
RA   Hogan D.A., Du P., Stevenson T.I., Whitton M., Kilby G.W., Rogers J.,
RA   VanBogelen R.A.;
RT   "Two-dimensional gel electrophoresis map of Streptococcus pyogenes
RT   proteins.";
RL   Submitted (MAY-2000) to UniProtKB.
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=22054.54; Method=Electrospray;
CC       Evidence={ECO:0000269|Ref.2};
CC   -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000305}.
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DR   EMBL; CP000003; AAT87628.1; -; Genomic_DNA.
DR   RefSeq; WP_002983313.1; NC_006086.1.
DR   AlphaFoldDB; Q5XAD5; -.
DR   SMR; Q5XAD5; -.
DR   EnsemblBacteria; AAT87628; AAT87628; M6_Spy1493.
DR   KEGG; spa:M6_Spy1493; -.
DR   HOGENOM; CLU_057217_6_3_9; -.
DR   OMA; YAYEKIA; -.
DR   Proteomes; UP000001167; 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; Direct protein sequencing; Stress response.
FT   CHAIN           1..190
FT                   /note="Protein GrpE"
FT                   /id="PRO_0000113875"
FT   REGION          21..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..44
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   190 AA;  22055 MW;  5636051FC3BAE27E CRC64;
     MAVFNKLFKR RHSVSEEIKK DDLQEEVEAT ETEETVEEVI EETPEKSELE LANERADEFE
     NKYLRAHAEM QNIQRRSSEE RQQLQRYRSQ DLAKAILPSL DNLERALAVE GLTDDVKKGL
     EMTRDSLIQA LKEEGVEEVE VDSFDHNFHM AVQTLPADDE HPADSIAEVF QKGYKLHERL
     LRPAMVVVYN