ID A0A0D5MBG9_9GAMM Unreviewed; 357 AA.
AC A0A0D5MBG9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=KO116_P200076 {ECO:0000313|EMBL:AJY53183.1};
OS Halomonas sp. KO116.
OG Plasmid unnamed2 {ECO:0000313|EMBL:AJY53183.1,
OG ECO:0000313|Proteomes:UP000028645}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1504981 {ECO:0000313|EMBL:AJY53183.1, ECO:0000313|Proteomes:UP000028645};
RN [1] {ECO:0000313|EMBL:AJY53183.1, ECO:0000313|Proteomes:UP000028645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KO116 {ECO:0000313|EMBL:AJY53183.1,
RC ECO:0000313|Proteomes:UP000028645};
RC PLASMID=Plasmid unnamed2 {ECO:0000313|Proteomes:UP000028645};
RX PubMed=25953187;
RA O'Dell K.B., Woo H.L., Utturkar S., Klingeman D., Brown S.D., Hazen T.C.;
RT "Genome Sequence of Halomonas sp. Strain KO116, an Ionic Liquid-Tolerant
RT Marine Bacterium Isolated from a Lignin-Enriched Seawater Microcosm.";
RL Genome Announc. 3:0-0(2015).
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 ---------------------------------------------------------------------------
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; CP011054; AJY53183.1; -; Genomic_DNA.
DR RefSeq; WP_052703879.1; NZ_CP011054.1.
DR AlphaFoldDB; A0A0D5MBG9; -.
DR KEGG; hak:KO116_P200076; -.
DR eggNOG; COG0576; Bacteria.
DR HOGENOM; CLU_775612_0_0_6; -.
DR OrthoDB; 9789811at2; -.
DR Proteomes; UP000028645; Plasmid unnamed2.
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:0051082; F:unfolded protein 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; IPR002939; DnaJ_C.
DR InterPro; IPR000740; GrpE.
DR InterPro; IPR013805; GrpE_coiled_coil.
DR InterPro; IPR009012; GrpE_head.
DR InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR PANTHER; PTHR21237; GRPE PROTEIN; 1.
DR PANTHER; PTHR21237:SF23; GRPE PROTEIN HOMOLOG, MITOCHONDRIAL; 1.
DR Pfam; PF01556; DnaJ_C; 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 SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 1.
DR PROSITE; PS01071; GRPE; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_01151};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01151};
KW Plasmid {ECO:0000313|EMBL:AJY53183.1};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_01151,
KW ECO:0000256|RuleBase:RU000639}.
FT DOMAIN 72..191
FT /note="Chaperone DnaJ C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01556"
FT COILED 202..236
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 357 AA; 39326 MW; 7463905211628E7F CRC64;
MKKGKSIYDI AVTVDVTLDT IVNNGPDEGI KVSYLRNIEC RVCSSFRKSS SGIKHCKVCL
DTQIENISHT ATLTTPPPHI DNRGMTLYYK EHGHYSPETN SYGLLCASFN ISKESGVLIE
GKDIVKPLWI TPFQAKIGGK IPIGGSFNGR PNIIVRPDQL SHGNRIRIKD MGGYQINDKE
RGHLYFAVNI KDDDQHAPSD DEIAAVKRIE ELELLIENLQ LNVSHLKTQN ANLIDTVEES
ATSSEASWNA QGALKVIEDL LPSIDSLEKA LENMCAPGDQ AHREGVTMIL DLQRKALAKH
GVVPIPALGH KFNPHQHEAV AVSHDTGRAK NIVTDVLQEG YTHADRLLRP ALVRVSG
//
