ID   GRPE_VIBCH              Reviewed;         200 AA.
AC   O30862; O34240; Q9KTP7;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 111.
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=VC_0854;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 122-200.
RC   STRAIN=ATCC 51352 / El Tor MAK757 / Serotype O1;
RA   Ghosh A.;
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 158-199.
RC   STRAIN=ATCC 25870 / Classical Inaba 569B / Serotype O1;
RX   PubMed=10024539; DOI=10.1128/iai.67.3.1025-1033.1999;
RA   Chakrabarti S., Sengupta N., Chowdhury R.;
RT   "Role of DnaK in in vitro and in vivo expression of virulence factors of
RT   Vibrio cholerae.";
RL   Infect. Immun. 67:1025-1033(1999).
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; AE003852; AAF94016.1; -; Genomic_DNA.
DR   EMBL; AF019558; AAB86382.1; -; Genomic_DNA.
DR   EMBL; Y14237; CAA74626.1; -; Genomic_DNA.
DR   PIR; A82273; A82273.
DR   RefSeq; NP_230501.1; NC_002505.1.
DR   RefSeq; WP_000064038.1; NZ_LT906614.1.
DR   AlphaFoldDB; O30862; -.
DR   SMR; O30862; -.
DR   STRING; 243277.VC_0854; -.
DR   DNASU; 2614521; -.
DR   EnsemblBacteria; AAF94016; AAF94016; VC_0854.
DR   GeneID; 57739553; -.
DR   KEGG; vch:VC_0854; -.
DR   PATRIC; fig|243277.26.peg.814; -.
DR   eggNOG; COG0576; Bacteria.
DR   HOGENOM; CLU_057217_6_0_6; -.
DR   OMA; YAYEKIA; -.
DR   BioCyc; VCHO:VC0854-MON; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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..200
FT                   /note="Protein GrpE"
FT                   /id="PRO_0000113891"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        160
FT                   /note="H -> Y (in Ref. 3; CAA74626)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   200 AA;  22659 MW;  92C725BC20ADF4BD CRC64;
     MSNEEIKNKD EQLQQDAVET EAEVVGTDAD IDWNQAADEI DEKEAKIAQL EAALLVSEER
     VKEQQDSVLR ARAEVENMRR RSEQEVDKAR KFALSRFAEE LLPVIDNLER AIQAADGEVE
     AIKPLLEGVE LTHKTFVDTI AKFGLKEINP HGEVFNPEFH QAMSIQESAE HEPNTVMFVM
     QKGYELNGRV LRPAMVMVSK