ID W8PEI7_9PSED Unreviewed; 188 AA.
AC W8PEI7;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=BK654_22995 {ECO:0000313|EMBL:ROM73495.1}, CD58_04135
GN {ECO:0000313|EMBL:AHL32123.1};
OS Pseudomonas brassicacearum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=930166 {ECO:0000313|EMBL:AHL32123.1, ECO:0000313|Proteomes:UP000019521};
RN [1] {ECO:0000313|EMBL:AHL32123.1, ECO:0000313|Proteomes:UP000019521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DF41 {ECO:0000313|EMBL:AHL32123.1,
RC ECO:0000313|Proteomes:UP000019521};
RX PubMed=24812222;
RA Loewen P.C., Switala J., Fernando W.G., de Kievit T.;
RT "Genome Sequence of Pseudomonas brassicacearum DF41.";
RL Genome Announc. 2:e00390-14(2014).
RN [2] {ECO:0000313|EMBL:ROM73495.1, ECO:0000313|Proteomes:UP000285519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=36D4 {ECO:0000313|EMBL:ROM73495.1,
RC ECO:0000313|Proteomes:UP000285519};
RA Tao X.-Y., Taylor C.G.;
RT "Comparative genome analysis of multiple Pseudomonas spp. focuses on
RT biocontrol and plant growth promoting traits.";
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; CP007410; AHL32123.1; -; Genomic_DNA.
DR EMBL; MOBE01000014; ROM73495.1; -; Genomic_DNA.
DR RefSeq; WP_025211777.1; NZ_MOBE01000014.1.
DR AlphaFoldDB; W8PEI7; -.
DR KEGG; pbc:CD58_04135; -.
DR PATRIC; fig|930166.5.peg.790; -.
DR eggNOG; COG0576; Bacteria.
DR OrthoDB; 9789811at2; -.
DR Proteomes; UP000019521; Chromosome.
DR Proteomes; UP000285519; 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 Stress response {ECO:0000256|HAMAP-Rule:MF_01151,
KW ECO:0000256|RuleBase:RU000639}.
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 188 AA; 20995 MW; 44CA82873BF3CABC CRC64;
MADEQTQDTQ NLDANQAPQD SGDDLAARVQ VLEEQLAGAQ DQALRVAADL QNVRRRAEQD
VEKAHKFALE RFASDLLPII DSLERGLELS NPDDENIRPM REGIELTLKM FQDTLKRYQL
EAIDPHGEPF NAEHHQAMAM QESADVEPNS VLKVFQKGYL LNGRLLRPAM VVVSKTPAPV
SPSIDEQA
//