ID   GRPE_CAUVN              Reviewed;         208 AA.
AC   B8GXP4; P48195;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Protein GrpE;
DE   AltName: Full=HSP-70 cofactor;
GN   Name=grpE; OrderedLocusNames=CCNA_00153;
OS   Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=565050;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8606155; DOI=10.1128/jb.178.7.1829-1841.1996;
RA   Roberts R.C., Toochinda C., Avedissian M., Baldini R.L., Gomes S.L.,
RA   Shapiro L.;
RT   "Identification of a Caulobacter crescentus operon encoding hrcA, involved
RT   in negatively regulating heat-inducible transcription, and the chaperone
RT   gene grpE.";
RL   J. Bacteriol. 178:1829-1841(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1000 / CB15N;
RX   PubMed=20472802; DOI=10.1128/jb.00255-10;
RA   Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA   Walunas T.L., Crosson S.;
RT   "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL   J. Bacteriol. 192:3678-3688(2010).
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:0000250}.
CC   -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-11 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB01516.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U33324; AAB01516.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP001340; ACL93620.1; -; Genomic_DNA.
DR   RefSeq; WP_012639893.1; NC_011916.1.
DR   RefSeq; YP_002515528.1; NC_011916.1.
DR   AlphaFoldDB; B8GXP4; -.
DR   SMR; B8GXP4; -.
DR   PRIDE; B8GXP4; -.
DR   EnsemblBacteria; ACL93620; ACL93620; CCNA_00153.
DR   GeneID; 7332407; -.
DR   KEGG; ccs:CCNA_00153; -.
DR   PATRIC; fig|565050.3.peg.152; -.
DR   HOGENOM; CLU_057217_6_2_5; -.
DR   OMA; YAYEKIA; -.
DR   OrthoDB; 1906715at2; -.
DR   PhylomeDB; B8GXP4; -.
DR   Proteomes; UP000001364; 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..208
FT                   /note="Protein GrpE"
FT                   /id="PRO_0000378292"
FT   REGION          172..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   208 AA;  22017 MW;  1A68E4C250E326C9 CRC64;
     MTDEQTPAEE MPFEADDAAQ EIEALKLEVA QLKEQALRYA AEAENTKRRA EREMNDARAY
     AIQKFARDLL GAADNLGRAT AHSPKDSTDP AVKNFIIGVE MTEKELQSAF ERNGLKKIDP
     AKGDKFDPHL HQAVTEQPST EVAAGGVLMV MQAGYELMGR LVRPAMVAVA AKGSTGPASP
     DAPAASANPY AGAAAEGDST GGAFDAKA