GRPE_ONYPE
ID GRPE_ONYPE Reviewed; 247 AA.
AC Q6YPM0;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
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}; OrderedLocusNames=PAM_705;
OS Onion yellows phytoplasma (strain OY-M).
OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC Candidatus Phytoplasma; Candidatus Phytoplasma asteris.
OX NCBI_TaxID=262768;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OY-M;
RX PubMed=14661021; DOI=10.1038/ng1277;
RA Oshima K., Kakizawa S., Nishigawa H., Jung H.-Y., Wei W., Suzuki S.,
RA Arashida R., Nakata D., Miyata S., Ugaki M., Namba S.;
RT "Reductive evolution suggested from the complete genome sequence of a
RT plant-pathogenic phytoplasma.";
RL Nat. Genet. 36:27-29(2004).
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; AP006628; BAD04790.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6YPM0; -.
DR SMR; Q6YPM0; -.
DR STRING; 262768.PAM_705; -.
DR EnsemblBacteria; BAD04790; BAD04790; PAM_705.
DR KEGG; poy:PAM_705; -.
DR eggNOG; COG0576; Bacteria.
DR HOGENOM; CLU_057217_5_2_14; -.
DR OMA; YAYEKIA; -.
DR OrthoDB; 1415610at2; -.
DR BioCyc; OYEL262768:G1G26-858-MON; -.
DR Proteomes; UP000002523; 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..247
FT /note="Protein GrpE"
FT /id="PRO_0000113829"
FT REGION 31..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 247 AA; 28973 MW; 99AEF8D4F086B964 CRC64;
MFLEKDQDNL DNLETQAKEL HKDCKECKNC QKEETKTTNK DNQKEDETVK NQSNQSNQSN
QTKQTNTKQQ KHQPKENSHL QITKLQTQIK ELQQQLTQQK KSFDEELLKN QAELINFKKR
AQTQKANELK YASSNFITNL LMPLEQLEKV IDMPTQNELL QKYLLGFKLL QQQIKKVLQD
EGVEEIEALN KPFDPALHHA LETVCDPKKP DKTNLAVLQK GYLYKKRILR PTLVKVNEWS
DKNDKNE