ID A0A1E8FM55_9MICC Unreviewed; 228 AA.
AC A0A1E8FM55;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=BIU82_12280 {ECO:0000313|EMBL:OFI36836.1};
OS Arthrobacter sp. SW1.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1920889 {ECO:0000313|EMBL:OFI36836.1, ECO:0000313|Proteomes:UP000176251};
RN [1] {ECO:0000313|EMBL:OFI36836.1, ECO:0000313|Proteomes:UP000176251}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SW1 {ECO:0000313|EMBL:OFI36836.1,
RC ECO:0000313|Proteomes:UP000176251};
RA Shaligram S.M., Kumbhare S.V., Pawar S., Dhotre D., Muddeshwar M.G.,
RA Kapley A.;
RT "Genomic insights of Arthrobacter sp. strain SW1 for secondary metabolite
RT production.";
RL Submitted (SEP-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OFI36836.1}.
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DR EMBL; MJLT01000067; OFI36836.1; -; Genomic_DNA.
DR RefSeq; WP_070350764.1; NZ_MJLT01000067.1.
DR AlphaFoldDB; A0A1E8FM55; -.
DR STRING; 1920889.BIU82_12280; -.
DR OrthoDB; 5191115at2; -.
DR Proteomes; UP000176251; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01151};
KW Reference proteome {ECO:0000313|Proteomes:UP000176251};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_01151,
KW ECO:0000256|RuleBase:RU000639}.
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 87..114
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 228 AA; 24518 MW; C5207E7E34F8AA6C CRC64;
MPHHGNESEH SGSEQGKPVI RDNRKVDPET GAARHPQQDS PVVEPVETGQ PASPVVEPVE
TEGDALSQAE EILNGVEVPA EESVATGASA QAEAAELRND LLRLQAEYVN YRKRVERDRA
VAGEMAVIGV LNSLLPVLDD IDAARQHGDL EDGPFAAIAA KLENALKTYG LERIDATGVE
FDPTIHEALI QQAGQDIEVD TVSQVLRSGY RSKERVLRAA QVIVSVPA
//
