ID D0J8P4_BLASP Unreviewed; 183 AA.
AC D0J8P4;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Protein GrpE {ECO:0000256|HAMAP-Rule:MF_01151};
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:ACX83715.1};
GN OrderedLocusNames=BPLAN_080 {ECO:0000313|EMBL:ACX83715.1};
OS Blattabacterium sp. subsp. Periplaneta americana (strain BPLAN)
OS (Periplaneta americana symbiotic bacterium).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Blattabacteriaceae; Blattabacterium.
OX NCBI_TaxID=600809 {ECO:0000313|EMBL:ACX83715.1, ECO:0000313|Proteomes:UP000002225};
RN [1] {ECO:0000313|EMBL:ACX83715.1, ECO:0000313|Proteomes:UP000002225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BPLAN {ECO:0000313|EMBL:ACX83715.1,
RC ECO:0000313|Proteomes:UP000002225};
RX PubMed=19880743; DOI=10.1073/pnas.0907504106;
RA Sabree Z.L., Kambhampati S., Moran N.A.;
RT "Nitrogen recycling and nutritional provisioning by Blattabacterium, the
RT cockroach endosymbiont.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19521-19526(2009).
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}.
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; CP001429; ACX83715.1; -; Genomic_DNA.
DR RefSeq; WP_012821243.1; NC_013418.2.
DR AlphaFoldDB; D0J8P4; -.
DR STRING; 600809.BPLAN_080; -.
DR KEGG; bpi:BPLAN_080; -.
DR eggNOG; COG0576; Bacteria.
DR HOGENOM; CLU_057217_5_2_10; -.
DR OrthoDB; 9812586at2; -.
DR Proteomes; UP000002225; 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 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.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_01151};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01151};
KW Reference proteome {ECO:0000313|Proteomes:UP000002225};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_01151}.
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 183 AA; 21526 MW; 2C991844BA4841F9 CRC64;
MNINQKNIDS QDEKNPVDLS EMENSCQEKT EHSLKEVEIF KEKLEKEKDK FLRLFAEFEN
YKKRIQKERF DLFRSVHQQI IIDLIPILDD FERGLKELKK SKDEALIQGV SLIQEKLIKI
LKEKGLNKIK IKKGDDFNTD FHEAITQIPA TTENLKGKIM EIIESGYILQ ERVIRHAKVI
TGK
//
