ID A0A0K1E551_CHOCO Unreviewed; 221 AA.
AC A0A0K1E551;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Protein GrpE {ECO:0000256|RuleBase:RU000639};
GN ORFNames=CMC5_000910 {ECO:0000313|EMBL:AKT35979.1};
OS Chondromyces crocatus.
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae;
OC Chondromyces.
OX NCBI_TaxID=52 {ECO:0000313|EMBL:AKT35979.1, ECO:0000313|Proteomes:UP000067626};
RN [1] {ECO:0000313|EMBL:AKT35979.1, ECO:0000313|Proteomes:UP000067626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cm c5 {ECO:0000313|EMBL:AKT35979.1,
RC ECO:0000313|Proteomes:UP000067626};
RA Zaburannyi N., Bunk B., Maier J., Overmann J., Mueller R.;
RT "Genome analysis of myxobacterium Chondromyces crocatus Cm c5 reveals a
RT high potential for natural compound synthesis and the genetic basis for the
RT loss of fruiting body formation.";
RL Submitted (JUL-2015) 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; CP012159; AKT35979.1; -; Genomic_DNA.
DR RefSeq; WP_050428558.1; NZ_CP012159.1.
DR AlphaFoldDB; A0A0K1E551; -.
DR STRING; 52.CMC5_000910; -.
DR KEGG; ccro:CMC5_000910; -.
DR PATRIC; fig|52.7.peg.99; -.
DR OrthoDB; 9789811at2; -.
DR Proteomes; UP000067626; 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:UP000067626};
KW Stress response {ECO:0000256|RuleBase:RU000639}.
SQ SEQUENCE 221 AA; 23269 MW; DE299E9B0E57C911 CRC64;
MSDLPAQAPA TLESLSSRLD DLLKEVRRQG RAAVAAQAAA ESCLMAVRGL AQEAAPAASR
DRDEEGAPTL REGAMREIGG HWLRALIPIA DAMERVVQHA SEGAVRQRIS RRWWQRLLGA
PEEGASELAA LVEGLRVLDQ QLNASLTELG VNVERPLGEA VDAERHRVVG VSPPRPGFPA
GRVVEVVRVG YALGGAVVRE AEVIASSGPS PESPCAGGNG S
//