ID   GRPE_BARHE              Reviewed;         220 AA.
AC   Q6G563;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=BH00560;
OS   Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS   (Rochalimaea henselae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=283166;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT   of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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; BX897699; CAF26872.1; -; Genomic_DNA.
DR   RefSeq; WP_011180019.1; NZ_LRIJ02000001.1.
DR   AlphaFoldDB; Q6G563; -.
DR   SMR; Q6G563; -.
DR   STRING; 283166.BH00560; -.
DR   PaxDb; Q6G563; -.
DR   PRIDE; Q6G563; -.
DR   EnsemblBacteria; CAF26872; CAF26872; BH00560.
DR   KEGG; bhe:BH00560; -.
DR   eggNOG; COG0576; Bacteria.
DR   OMA; YAYEKIA; -.
DR   Proteomes; UP000000421; 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; Stress response.
FT   CHAIN           1..220
FT                   /note="Protein GrpE"
FT                   /id="PRO_0000113745"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   220 AA;  23925 MW;  FB8FEA2A5393C467 CRC64;
     MSDEKNKFTD ASFENCDLKN PSDRDALKQA ADKFLKAHAA EADADVKGGG EALVDPLAAL
     QDENKELKDQ LLRLAADMEN LRRRTARDVA DAKAYSIANF ARDMLSVSDN LNRALDAIPE
     GAKENDAGLK TLAEGVEMTE RAMIAALERH GVQKIHPEGQ KFDPHFHQAM FEIPNSDVPD
     NTVQQVVQAG YIIGERVLRP AIVGVAKGGA KDISVESDSD