ID A0A0C3N9U7_9PORP Unreviewed; 191 AA.
AC A0A0C3N9U7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
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:PXZ44124.1};
GN ORFNames=BA92_13115 {ECO:0000313|EMBL:KIO42807.1}, DMB45_05525
GN {ECO:0000313|EMBL:PXZ44124.1};
OS Sanguibacteroides justesenii.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Sanguibacteroides.
OX NCBI_TaxID=1547597 {ECO:0000313|EMBL:KIO42807.1, ECO:0000313|Proteomes:UP000031980};
RN [1] {ECO:0000313|EMBL:KIO42807.1, ECO:0000313|Proteomes:UP000031980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OUH 308042 {ECO:0000313|EMBL:KIO42807.1,
RC ECO:0000313|Proteomes:UP000031980};
RA Sydenham T.V., Hasman H., Justensen U.S.;
RT "Porphyromonadaceae bacterium OUH 308042 = ATCC BAA-2681 = DSM 28342 draft
RT genome.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PXZ44124.1, ECO:0000313|Proteomes:UP000248308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OUH 969102 {ECO:0000313|EMBL:PXZ44124.1,
RC ECO:0000313|Proteomes:UP000248308};
RX PubMed=25814588;
RA Sydenham T.V., Hasman H., Justesen U.S.;
RT "Draft Genome Sequences of Sanguibacteroides justesenii, gen. nov., sp.
RT nov., Strains OUH 308042T (= ATCC BAA-2681T) and OUH 334697 (= ATCC BAA-
RT 2682), Isolated from Blood Cultures from Two Different Patients.";
RL Genome Announc. 3:e00005-15(2015).
RN [3] {ECO:0000313|EMBL:PXZ44124.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OUH 969102 {ECO:0000313|EMBL:PXZ44124.1};
RA Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA Wayne K.J., Tettelin H., Glass J.I., Rusch D., Podicherti R., Tsui H.-C.T.,
RA Winkler M.E.;
RL Submitted (MAY-2018) 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. {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}.
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:KIO42807.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JPIU01000049; KIO42807.1; -; Genomic_DNA.
DR EMBL; QJPL01000003; PXZ44124.1; -; Genomic_DNA.
DR RefSeq; WP_041503047.1; NZ_QJPL01000003.1.
DR AlphaFoldDB; A0A0C3N9U7; -.
DR OrthoDB; 9812586at2; -.
DR Proteomes; UP000031980; Unassembled WGS sequence.
DR Proteomes; UP000248308; 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.
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:UP000031980};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_01151}.
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 191 AA; 21862 MW; 8430ACE259238645 CRC64;
MSEEKKRKQE EELIGAQHVS ESKGEGHEES SKKKDKSCKK EEKQLEEMGQ KLMEMNDKYL
RLSAEFDNYR KRTLKERMEL TKTAGEQVLT GILPVVDNFE RALASMEKAT DVRALKEGVD
LIYANFKDFL MRNGVKVIET ENVDFNTDLH EAVTTIPAPT EEQKGKVIDC IEKGYTLNDK
VIRFAKVVVG E
//
