ID   GRPE_PARL1              Reviewed;         213 AA.
AC   A7HZ43;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 66.
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=Plav_3578;
OS   Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Parvibaculaceae; Parvibaculum.
OX   NCBI_TaxID=402881;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS-1 / DSM 13023 / NCIMB 13966;
RX   PubMed=22675581; DOI=10.4056/sigs.2215005;
RA   Schleheck D., Weiss M., Pitluck S., Bruce D., Land M.L., Han S.,
RA   Saunders E., Tapia R., Detter C., Brettin T., Han J., Woyke T., Goodwin L.,
RA   Pennacchio L., Nolan M., Cook A.M., Kjelleberg S., Thomas T.;
RT   "Complete genome sequence of Parvibaculum lavamentivorans type strain (DS-
RT   1(T)).";
RL   Stand. Genomic Sci. 5:298-310(2011).
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; CP000774; ABS65176.1; -; Genomic_DNA.
DR   RefSeq; WP_012112436.1; NC_009719.1.
DR   AlphaFoldDB; A7HZ43; -.
DR   SMR; A7HZ43; -.
DR   STRING; 402881.Plav_3578; -.
DR   EnsemblBacteria; ABS65176; ABS65176; Plav_3578.
DR   KEGG; pla:Plav_3578; -.
DR   eggNOG; COG0576; Bacteria.
DR   HOGENOM; CLU_057217_0_2_5; -.
DR   OMA; YAYEKIA; -.
DR   OrthoDB; 1906715at2; -.
DR   Proteomes; UP000006377; 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..213
FT                   /note="Protein GrpE"
FT                   /id="PRO_1000164209"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   213 AA;  23138 MW;  BAD07155BDF271E4 CRC64;
     MSDEKKPEAE TSESLQKREE KLAETLASEP AAQGEAEDAA AAGPDVAALE AEISDLRNRL
     LRAAADMENN RKRAEREKQD AQRYAAANFA RDMLEVSDNL RRAIATLKED ERAEAAESVK
     AMIEGVEMTD RQLVTIFERH GIREITPQPG ERFDPNLHEA MFEVPGTDQP AGTVVHVLGA
     GYMIGDRLLR AARVGVAKAD DGAAKGGKVD TIA