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Database: UniProt
Entry: A0A0B0DBZ7_9MICC
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ID   A0A0B0DBZ7_9MICC        Unreviewed;       216 AA.
AC   A0A0B0DBZ7;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 38.
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   ORFNames=AS25_07955 {ECO:0000313|EMBL:KHE74300.1};
OS   Kocuria marina.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Kocuria.
OX   NCBI_TaxID=223184 {ECO:0000313|EMBL:KHE74300.1, ECO:0000313|Proteomes:UP000030664};
RN   [1] {ECO:0000313|EMBL:KHE74300.1, ECO:0000313|Proteomes:UP000030664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SO9-6 {ECO:0000313|EMBL:KHE74300.1,
RC   ECO:0000313|Proteomes:UP000030664};
RA   Castro D.B., Pereira L.B., Silva M.V., Silva B.P., Zanardi B.R., Carlos C.,
RA   Belgini D.R., Limache E.G., Lacerda G.V., Nery M.B., Gomes M.B., Souza S.,
RA   Silva T.M., Rodrigues V.D., Paulino L.C., Vicentini R., Ferraz L.F.,
RA   Ottoboni L.M.;
RT   "High-quality draft genome sequence of Kocuria marina SO9-6, an
RT   actinobacterium isolated from a copper mine.";
RL   Submitted (SEP-2014) 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:KHE74300.1}.
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DR   EMBL; JROM01000022; KHE74300.1; -; Genomic_DNA.
DR   RefSeq; WP_035964091.1; NZ_JROM01000022.1.
DR   AlphaFoldDB; A0A0B0DBZ7; -.
DR   STRING; 223184.AS25_07955; -.
DR   eggNOG; COG0576; Bacteria.
DR   Proteomes; UP000030664; 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   Stress response {ECO:0000256|HAMAP-Rule:MF_01151}.
FT   REGION          1..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   216 AA;  22982 MW;  6D1573A955C7A36C CRC64;
     MSMSDSENTK GHGESVPEDP DHSAQDSTGT ERSEGGEGLT VDDILDTPQS QDAQTGDTQA
     ADAASSQDDA APAGESAAQK LADERLEDLR RLQAEFVNFK NRTAREKDQL RDFVSGEMIT
     ALLPVLDDVD AARKAGDLED GPFAAIATKL EDALGKKGLT RIGEVGEVFD PTVHEAVLQQ
     PTDEVEPDHV SMVLRSGFRV GARVVRAAQV AVATKP
//
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