ID   GRPE_LACAC              Reviewed;         194 AA.
AC   Q84BU5; Q5FJP3; Q93G05;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 3.
DT   03-AUG-2022, entry version 89.
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=LBA1248;
OS   Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=272621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CRL 639;
RA   Lorca G.L., Raya R.R., Font de Valdez G.;
RT   "Molecular characterization of the dnaK operon of Lactobacillus acidophilus
RT   CRL 639.";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SBT2062;
RA   Aoyama K., Uenishi H., Nakajima H.;
RT   "Characterization of Lactobacillus acidophilus dnaK.";
RL   Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700396 / NCK56 / N2 / NCFM;
RX   PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA   Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA   McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA   Hamrick A., Cano R., Klaenhammer T.R.;
RT   "Complete genome sequence of the probiotic lactic acid bacterium
RT   Lactobacillus acidophilus NCFM.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
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; AF300646; AAK97220.1; -; Genomic_DNA.
DR   EMBL; AB059359; BAC66859.1; -; Genomic_DNA.
DR   EMBL; CP000033; AAV43081.1; -; Genomic_DNA.
DR   RefSeq; WP_003547792.1; NC_006814.3.
DR   RefSeq; YP_194112.1; NC_006814.3.
DR   AlphaFoldDB; Q84BU5; -.
DR   SMR; Q84BU5; -.
DR   STRING; 272621.LBA1248; -.
DR   PRIDE; Q84BU5; -.
DR   EnsemblBacteria; AAV43081; AAV43081; LBA1248.
DR   GeneID; 56942839; -.
DR   KEGG; lac:LBA1248; -.
DR   PATRIC; fig|272621.13.peg.1183; -.
DR   eggNOG; COG0576; Bacteria.
DR   HOGENOM; CLU_057217_6_3_9; -.
DR   OMA; YAYEKIA; -.
DR   BioCyc; LACI272621:G1G49-1231-MON; -.
DR   Proteomes; UP000006381; 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..194
FT                   /note="Protein GrpE"
FT                   /id="PRO_0000113797"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        112
FT                   /note="D -> E (in Ref. 1; AAK97220)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        117..122
FT                   /note="QLKKGV -> PIEKGF (in Ref. 1; AAK97220)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        136..137
FT                   /note="HG -> SR (in Ref. 1; AAK97220)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        162..169
FT                   /note="ENDDQKDH -> DDDQKDHT (in Ref. 1; AAK97220)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   194 AA;  22058 MW;  0635C976CA2930F0 CRC64;
     MSKEEFPSEK NLDKEENTSK PKKAVKKEAA KGEETKKNNE NQKLAKEIAD LKEKNKDLED
     KYLRSEAEIQ NMQNRYTKER AQLIKYESQS LAKDVLPAMD NLERALSVEA DDDVSKQLKK
     GVQMTLDALV KAMKDHGVVE IEADGVKFDP TLHQAVQTVA AENDDQKDHV VQVLQKGYQY
     KDRTLRPAMV VVAQ