ID A0A1I3IYB3_9FLAO Unreviewed; 181 AA.
AC A0A1I3IYB3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Protein GrpE {ECO:0000256|HAMAP-Rule:MF_01151, ECO:0000256|RuleBase:RU000639};
DE AltName: Full=HSP-70 cofactor {ECO:0000256|HAMAP-Rule:MF_01151};
GN Name=grpE {ECO:0000256|HAMAP-Rule:MF_01151};
GN ORFNames=SAMN05443292_2844 {ECO:0000313|EMBL:SFI52931.1};
OS Halpernia frigidisoli.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Halpernia.
OX NCBI_TaxID=1125876 {ECO:0000313|EMBL:SFI52931.1, ECO:0000313|Proteomes:UP000198931};
RN [1] {ECO:0000313|EMBL:SFI52931.1, ECO:0000313|Proteomes:UP000198931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26000 {ECO:0000313|EMBL:SFI52931.1,
RC ECO:0000313|Proteomes:UP000198931};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|RuleBase:RU000639}.
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; FOQT01000005; SFI52931.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3IYB3; -.
DR STRING; 1125876.SAMN05443292_2844; -.
DR OrthoDB; 9812586at2; -.
DR Proteomes; UP000198931; Unassembled WGS sequence.
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.
DR PROSITE; PS01071; 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:UP000198931};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_01151,
KW ECO:0000256|RuleBase:RU000639}.
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 181 AA; 20984 MW; 2E610138310A91D7 CRC64;
MDDNKHINEE EFNSTEETQE ENQTNPEENT ENLTVEKSSE ELAEEKDRYI RLFAEFENYK
KRTVKERNEF FQYASQEMMV SMLSILDDFE RAMKEISKNG NEADLKGIEL IYQKLKSKLT
EKGLKPIEVN VGDVFNVDFH EAITGIPAPT PELKGKIVDV IETGYQLHDK VIRFAKVITG
Q
//