ID Q5FSQ2_GLUOX Unreviewed; 221 AA.
AC Q5FSQ2;
DT 01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=Protein GrpE {ECO:0000256|HAMAP-Rule:MF_01151};
DE AltName: Full=HSP-70 cofactor {ECO:0000256|HAMAP-Rule:MF_01151};
GN Name=grpE {ECO:0000256|HAMAP-Rule:MF_01151};
GN OrderedLocusNames=GOX0820 {ECO:0000313|EMBL:AAW60594.1};
OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=290633 {ECO:0000313|EMBL:AAW60594.1, ECO:0000313|Proteomes:UP000006375};
RN [1] {ECO:0000313|EMBL:AAW60594.1, ECO:0000313|Proteomes:UP000006375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=621H {ECO:0000313|EMBL:AAW60594.1,
RC ECO:0000313|Proteomes:UP000006375};
RX PubMed=15665824; DOI=10.1038/nbt1062;
RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT oxydans.";
RL Nat. Biotechnol. 23:195-200(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:0000256|HAMAP-
CC Rule:MF_01151}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01151}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01151}.
CC -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000256|ARBA:ARBA00009054,
CC ECO:0000256|HAMAP-Rule:MF_01151, ECO:0000256|RuleBase:RU004478}.
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DR EMBL; CP000009; AAW60594.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5FSQ2; -.
DR STRING; 290633.GOX0820; -.
DR KEGG; gox:GOX0820; -.
DR eggNOG; COG0576; Bacteria.
DR HOGENOM; CLU_057217_6_2_5; -.
DR Proteomes; UP000006375; 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:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd00446; GrpE; 1.
DR Gene3D; 3.90.20.20; -; 1.
DR Gene3D; 2.30.22.10; Head domain of nucleotide exchange factor GrpE; 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; GRPE PROTEIN; 1.
DR PANTHER; PTHR21237:SF23; GRPE PROTEIN HOMOLOG, MITOCHONDRIAL; 1.
DR Pfam; PF01025; GrpE; 1.
DR PRINTS; PR00773; GRPEPROTEIN.
DR SUPFAM; SSF58014; Coiled-coil domain of nucleotide exchange factor GrpE; 1.
DR SUPFAM; SSF51064; Head domain of nucleotide exchange factor GrpE; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_01151};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01151};
KW Reference proteome {ECO:0000313|Proteomes:UP000006375};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_01151}.
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 221 AA; 24204 MW; 1F5FAAFF17EFB547 CRC64;
MMARPIAEGR DMTDHNASPE TAHDVPEQGV ETSGHETPGM NETGGETLEE TTPEARIEAL
EAQVAELKDR WVRSEAESQN IRARAKRDIE DARQYAIQKF ARDVVEAAEN LQRGLASLPA
KTEGEDVLIT KLREGIEGTE RSFINILERH GITCEDPTGK PFDANLHQAM AEQPSDQHPS
GHVMQSWTPA WLLKGRLLKP AMVVVAKGGA QAAPQGVDKT V
//
