ID G8QHM1_AZOOP Unreviewed; 185 AA.
AC G8QHM1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
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 OrderedLocusNames=Dsui_3080 {ECO:0000313|EMBL:AEV27414.1};
OS Azospira oryzae (strain ATCC BAA-33 / DSM 13638 / PS) (Dechlorosoma
OS suillum).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Azospira.
OX NCBI_TaxID=640081 {ECO:0000313|EMBL:AEV27414.1, ECO:0000313|Proteomes:UP000005633};
RN [1] {ECO:0000313|EMBL:AEV27414.1, ECO:0000313|Proteomes:UP000005633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-33 / DSM 13638 / PS
RC {ECO:0000313|Proteomes:UP000005633};
RX PubMed=22535943; DOI=10.1128/JB.00124-12;
RA Byrne-Bailey K.G., Coates J.D.;
RT "Complete genome sequence of the anaerobic perchlorate-reducing bacterium
RT Azospira suillum strain PS.";
RL J. Bacteriol. 194:2767-2768(2012).
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; CP003153; AEV27414.1; -; Genomic_DNA.
DR RefSeq; WP_014238094.1; NZ_CAJHOC010000002.1.
DR AlphaFoldDB; G8QHM1; -.
DR STRING; 640081.Dsui_3080; -.
DR KEGG; dsu:Dsui_3080; -.
DR eggNOG; COG0576; Bacteria.
DR HOGENOM; CLU_057217_6_1_4; -.
DR OrthoDB; 9789811at2; -.
DR Proteomes; UP000005633; 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.
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..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 185 AA; 20343 MW; 4E5F2CC64994F063 CRC64;
MQDQNKPQEP LELGGDANAP ESVAQPAAGQ TDTTPSLEEL LRQAELNAQE HHDAWLRAKA
ETENMRRRAQ EDIAKASKFA IEKFAESLLP VKDTLEMALA DTNPDSLRVG VDMTLKNLLS
AFEKSGVKEE NPVGQKFDPN KHQAIGMVES EQEPNTVVNV LQKGYLIADR VLRPAMVMVA
KGKDA
//