GRPE_MYXXD
ID GRPE_MYXXD Reviewed; 255 AA.
AC P95333; Q1CXT4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Protein GrpE {ECO:0000255|HAMAP-Rule:MF_01151};
DE AltName: Full=HSP-70 cofactor {ECO:0000255|HAMAP-Rule:MF_01151};
GN Name=grpE {ECO:0000255|HAMAP-Rule:MF_01151}; Synonyms=grpS;
GN OrderedLocusNames=MXAN_6672;
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9765567; DOI=10.1128/jb.180.20.5357-5368.1998;
RA Weimer R.M., Creighton C.X., Stassinopoulos A., Youderian P.,
RA Hartzell P.L.;
RT "A chaperone in the HSP70 family controls production of extracellular
RT fibrils in Myxococcus xanthus.";
RL J. Bacteriol. 180:5357-5368(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622;
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., Eisen J.,
RA Ronning C.M., Barbazuk W.B., Blanchard M., Field C., Halling C., Hinkle G.,
RA Iartchuk O., Kim H.S., Mackenzie C., Madupu R., Miller N., Shvartsbeyn A.,
RA Sullivan S.A., Vaudin M., Wiegand R., Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
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:0000255|HAMAP-
CC Rule:MF_01151}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01151}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01151}.
CC -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000255|HAMAP-
CC Rule:MF_01151}.
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DR EMBL; U83800; AAC64204.1; -; Genomic_DNA.
DR EMBL; CP000113; ABF93128.1; -; Genomic_DNA.
DR AlphaFoldDB; P95333; -.
DR SMR; P95333; -.
DR STRING; 246197.MXAN_6672; -.
DR EnsemblBacteria; ABF93128; ABF93128; MXAN_6672.
DR KEGG; mxa:MXAN_6672; -.
DR eggNOG; COG0576; Bacteria.
DR HOGENOM; CLU_057217_5_1_7; -.
DR OMA; YAYEKIA; -.
DR Proteomes; UP000002402; 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:0051087; F:chaperone binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd00446; GrpE; 1.
DR Gene3D; 2.30.22.10; -; 1.
DR Gene3D; 3.90.20.20; -; 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; PTHR21237; 1.
DR Pfam; PF01025; GrpE; 1.
DR PRINTS; PR00773; GRPEPROTEIN.
DR SUPFAM; SSF51064; SSF51064; 1.
DR SUPFAM; SSF58014; SSF58014; 1.
DR PROSITE; PS01071; GRPE; 1.
PE 3: Inferred from homology;
KW Chaperone; Cytoplasm; Reference proteome; Stress response.
FT CHAIN 1..255
FT /note="Protein GrpE"
FT /id="PRO_0000113905"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 58
FT /note="S -> T (in Ref. 1; AAC64204)"
FT /evidence="ECO:0000305"
FT CONFLICT 74..75
FT /note="ER -> NP (in Ref. 1; AAC64204)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="Q -> L (in Ref. 1; AAC64204)"
FT /evidence="ECO:0000305"
FT CONFLICT 142..143
FT /note="GV -> AL (in Ref. 1; AAC64204)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="A -> P (in Ref. 1; AAC64204)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 255 AA; 27411 MW; 46EF5914CD9F1045 CRC64;
MTVIEVEASG PSTPVEAEAS ASPADTTSPP SDAEATPSED VAALRQEVES LKAQLEFSQA
KGRETMERLR EAHERAKEAQ ERTVRHAADL ENYRKRAQKE KEEVQRFGSE KLLKDLLPVM
DNLDRAIDAA AKSPDLDSFE KGVAMTRKSF EDALGRHGVK GFSAKGQVFD PRVHEAIQQV
ETADVPAGHV AYEVVRGFYL NERLVRPAMV VVARAPAEPV AAAEPPAVAE PATATTDTEA
PAAPAQSENS SGGSQ
