ID M4YZZ6_9BRAD Unreviewed; 204 AA.
AC M4YZZ6;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 54.
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 ECO:0000313|EMBL:BAM86203.1};
GN ORFNames=S58_01840 {ECO:0000313|EMBL:BAM86203.1};
OS Bradyrhizobium oligotrophicum S58.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1245469 {ECO:0000313|EMBL:BAM86203.1, ECO:0000313|Proteomes:UP000011841};
RN [1] {ECO:0000313|EMBL:BAM86203.1, ECO:0000313|Proteomes:UP000011841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S58 {ECO:0000313|EMBL:BAM86203.1,
RC ECO:0000313|Proteomes:UP000011841};
RX PubMed=23396330; DOI=10.1128/AEM.00009-13;
RA Okubo T., Fukushima S., Itakura M., Oshima K., Longtonglang A.,
RA Teaumroong N., Mitsui H., Hattori M., Hattori R., Hattori T.,
RA Minamisawa K.;
RT "Genome analysis suggests that the soil oligotrophic bacterium Agromonas
RT oligotrophica (Bradyrhizobium oligotrophicum) is a nitrogen-fixing symbiont
RT of Aeschynomene indica.";
RL Appl. Environ. Microbiol. 79:2542-2551(2013).
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; AP012603; BAM86203.1; -; Genomic_DNA.
DR RefSeq; WP_015663343.1; NC_020453.1.
DR AlphaFoldDB; M4YZZ6; -.
DR STRING; 1245469.S58_01840; -.
DR KEGG; aol:S58_01840; -.
DR PATRIC; fig|1245469.3.peg.186; -.
DR eggNOG; COG0576; Bacteria.
DR HOGENOM; CLU_057217_6_2_5; -.
DR OrthoDB; 9789811at2; -.
DR Proteomes; UP000011841; 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 Coiled coil {ECO:0000256|SAM:Coils};
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"
FT COILED 41..68
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 204 AA; 21989 MW; 022A61FC469B28FD CRC64;
MTDPDLHKND PENPAQASEP VVSKPYIMPD DPETGSAEAF AKEAADARDK MLRTLAEMEN
LRKRTAREVA DARLYGITGF ARDVLDIADN LQRALDAVPE ETRANADAGL KSLIEGVELT
ERSLLNTLEK NGVKKFDPTG QKFDPNFQQA MYEVPDPSVP SGTVVQVVQA GFMIGERILR
PALVGVSKGG AKPAPANDQS NSAA
//
