ID U6STJ3_9BACI Unreviewed; 188 AA.
AC U6STJ3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Protein GrpE {ECO:0000256|HAMAP-Rule:MF_01151, ECO:0000256|RuleBase:RU000639};
DE AltName: Full=HSP-70 cofactor {ECO:0000256|HAMAP-Rule:MF_01151};
GN Name=grpE {ECO:0000256|HAMAP-Rule:MF_01151};
GN ORFNames=A33I_04975 {ECO:0000313|EMBL:ERN54702.1};
OS Alkalihalophilus marmarensis DSM 21297.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alkalihalophilus.
OX NCBI_TaxID=1188261 {ECO:0000313|EMBL:ERN54702.1, ECO:0000313|Proteomes:UP000017170};
RN [1] {ECO:0000313|EMBL:ERN54702.1, ECO:0000313|Proteomes:UP000017170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21297 {ECO:0000313|EMBL:ERN54702.1,
RC ECO:0000313|Proteomes:UP000017170};
RX PubMed=24285666;
RA Wernick D.G., Choi K.Y., Tat C.A., Lafontaine Rivera J.G., Liao J.C.;
RT "Genome Sequence of the Extreme Obligate Alkaliphile Bacillus marmarensis
RT Strain DSM 21297.";
RL Genome Announc. 1:e00967-e00913(2013).
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, ECO:0000256|RuleBase:RU000639}.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ERN54702.1}.
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DR EMBL; ATAE01000005; ERN54702.1; -; Genomic_DNA.
DR RefSeq; WP_012958084.1; NZ_ATAE01000005.1.
DR AlphaFoldDB; U6STJ3; -.
DR PATRIC; fig|1188261.3.peg.398; -.
DR Proteomes; UP000017170; Unassembled WGS sequence.
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 CDD; cd00446; GrpE; 1.
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.
DR PROSITE; PS01071; 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 Stress response {ECO:0000256|HAMAP-Rule:MF_01151,
KW ECO:0000256|RuleBase:RU000639}.
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..42
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 188 AA; 21392 MW; A39C228702AECF04 CRC64;
MTEKDTNTLE DELKAEDTEQ EAVDTDQNEA SASDETEVVE AEENPLEAQV AELNNRMLRV
QADYDNFRRR SREEKEAAAK YRSQALIEGL LPVVDNFERA LLVKPESEEA QSLLSGMEMV
YRQLKDTLKN EGVEVIETTG QSFDPHLHQA VMQVSEDGFE SNQIVEELQK GYKLKDRVLR
PSMVKVNA
//
