ID A0A0F4PIC4_9GAMM Unreviewed; 195 AA.
AC A0A0F4PIC4;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=CWC05_17680 {ECO:0000313|EMBL:TMP85620.1}, TW72_17565
GN {ECO:0000313|EMBL:KJY96153.1};
OS Pseudoalteromonas ruthenica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=151081 {ECO:0000313|EMBL:KJY96153.1, ECO:0000313|Proteomes:UP000033664};
RN [1] {ECO:0000313|EMBL:KJY96153.1, ECO:0000313|Proteomes:UP000033664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S3137 {ECO:0000313|EMBL:KJY96153.1,
RC ECO:0000313|Proteomes:UP000033664};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
RN [2] {ECO:0000313|EMBL:TMP85620.1, ECO:0000313|Proteomes:UP000305874}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2897 {ECO:0000313|EMBL:TMP85620.1,
RC ECO:0000313|Proteomes:UP000305874};
RA Paulsen S., Gram L.K.;
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000305874}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2897 {ECO:0000313|Proteomes:UP000305874};
RA Sonnenschein E.C., Bech P.K.;
RT "Co-occurence of chitin degradation, pigmentation and bioactivity in marine
RT Pseudoalteromonas.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:TMP85620.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S2897 {ECO:0000313|EMBL:TMP85620.1};
RA Sonnenschein E.C., Bech P.K.;
RT "Co-occurence of chitin degradation, pigmentation and bioactivity in marine
RT Pseudoalteromonas.";
RL Submitted (SEP-2019) 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, 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:KJY96153.1}.
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DR EMBL; JXXZ01000019; KJY96153.1; -; Genomic_DNA.
DR EMBL; PNCG01000022; TMP85620.1; -; Genomic_DNA.
DR RefSeq; WP_022946174.1; NZ_PPSV01000018.1.
DR AlphaFoldDB; A0A0F4PIC4; -.
DR STRING; 151081.TW72_17565; -.
DR GeneID; 58230306; -.
DR PATRIC; fig|151081.8.peg.3233; -.
DR eggNOG; COG0576; Bacteria.
DR OrthoDB; 9789811at2; -.
DR Proteomes; UP000033664; Unassembled WGS sequence.
DR Proteomes; UP000305874; 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 Reference proteome {ECO:0000313|Proteomes:UP000033664};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_01151,
KW ECO:0000256|RuleBase:RU000639}.
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 195 AA; 21446 MW; F2DC29A6328BE15C CRC64;
MSEQTQAKEN EQDNPQEAVE QEQASEQQAQ GDDNSAEAEI AALHAELEAA KQTIEDQKDS
VVRAAAEVEN IRRRAAQDVD KAHKFALEKF AGDLLPVLDN LERAIEFADK DNEAIKPMLE
GVEMTAKSFV EALGKFNVEV VEPQGETFNP DLHQAMSMQP SEDVAPNTVL AVMQKGYTLN
GRLLRPAMVM VSKAP
//