ID D5BWE4_NITHN Unreviewed; 214 AA.
AC D5BWE4;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Protein GrpE {ECO:0000256|RuleBase:RU000639};
GN OrderedLocusNames=Nhal_2516 {ECO:0000313|EMBL:ADE15601.1};
OS Nitrosococcus halophilus (strain Nc4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Nitrosococcus.
OX NCBI_TaxID=472759 {ECO:0000313|EMBL:ADE15601.1, ECO:0000313|Proteomes:UP000001844};
RN [1] {ECO:0000313|Proteomes:UP000001844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nc4 {ECO:0000313|Proteomes:UP000001844};
RG US DOE Joint Genome Institute;
RA Campbell M.A., Malfatti S.A., Chain P.S.G., Heidelberg J.F., Ward B.B.,
RA Klotz M.G.;
RT "Complete genome sequence of Nitrosococcus halophilus Nc4, a salt-adapted,
RT aerobic obligate ammonia-oxidizing sulfur purple bacterium.";
RL Submitted (APR-2010) 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.
CC {ECO:0000256|RuleBase:RU000639}.
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DR EMBL; CP001798; ADE15601.1; -; Genomic_DNA.
DR RefSeq; WP_013033461.1; NC_013960.1.
DR AlphaFoldDB; D5BWE4; -.
DR STRING; 472759.Nhal_2516; -.
DR KEGG; nhl:Nhal_2516; -.
DR eggNOG; COG0576; Bacteria.
DR HOGENOM; CLU_112003_0_0_6; -.
DR OrthoDB; 129423at2; -.
DR Proteomes; UP000001844; Chromosome.
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 Gene3D; 2.30.22.10; Head domain of nucleotide exchange factor GrpE; 1.
DR InterPro; IPR000740; GrpE.
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 SUPFAM; SSF51064; Head domain of nucleotide exchange factor GrpE; 1.
DR PROSITE; PS01071; GRPE; 1.
PE 4: Predicted;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU000639};
KW Reference proteome {ECO:0000313|Proteomes:UP000001844};
KW Stress response {ECO:0000256|RuleBase:RU000639}.
SQ SEQUENCE 214 AA; 24765 MW; 32D486FA5305F7D4 CRC64;
MDQAVKEELI AQFRAYLEQA GDEPALEEEA FSLLAELSGL RTEVKRESRQ VKEALEQFKS
VFATLQAGNE SLSRELESRR AAEKTLWRQT LRPLLLELLD LRDRLEAGLE LEIPSRRPLL
PGLCRRQNQL LESLREGQGM TLRRLDRILG DYRVRALEVL DKPLDPHTMR VLEVEFRPDQ
AQGIVTGELR KGFLWDEELL RPAEVKVNKR DDKP
//
