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Database: UniProt
Entry: A0A2G1XI31_STRCJ
LinkDB: A0A2G1XI31_STRCJ
Original site: A0A2G1XI31_STRCJ 
ID   A0A2G1XI31_STRCJ        Unreviewed;       219 AA.
AC   A0A2G1XI31;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
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=BLA24_18635 {ECO:0000313|EMBL:PHQ50789.1}, CYQ11_14645
GN   {ECO:0000313|EMBL:PPT13953.1};
OS   Streptomyces cinnamoneus (Streptoverticillium cinnamoneum).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces cinnamoneus group.
OX   NCBI_TaxID=53446 {ECO:0000313|EMBL:PHQ50789.1, ECO:0000313|Proteomes:UP000222531};
RN   [1] {ECO:0000313|EMBL:PHQ50789.1, ECO:0000313|Proteomes:UP000222531}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 21532 {ECO:0000313|EMBL:PHQ50789.1,
RC   ECO:0000313|Proteomes:UP000222531};
RX   PubMed=29053243;
RA   Patteson J., Cai W., Johnson R.A., Santa Maria K., Li B.;
RT   "Identification of the Biosynthetic Pathway for the Antibiotic
RT   Bicyclomycin.";
RL   Biochemistry 0:0-0(2017).
RN   [2] {ECO:0000313|EMBL:PPT13953.1, ECO:0000313|Proteomes:UP000239771}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 41675 {ECO:0000313|EMBL:PPT13953.1,
RC   ECO:0000313|Proteomes:UP000239771};
RA   Vior N.M., Lacret R., Chandra G., Dorai-Raj S., Trick M., Truman A.W.;
RT   "Discovery and biosynthesis of the antibiotic bicyclomycin in distant
RT   bacterial classes.";
RL   Submitted (DEC-2017) 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:PHQ50789.1}.
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DR   EMBL; NHZO01000148; PHQ50789.1; -; Genomic_DNA.
DR   EMBL; PKFQ01000001; PPT13953.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G1XI31; -.
DR   OrthoDB; 5191115at2; -.
DR   Proteomes; UP000222531; Unassembled WGS sequence.
DR   Proteomes; UP000239771; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01151};
KW   Reference proteome {ECO:0000313|Proteomes:UP000222531};
KW   Stress response {ECO:0000256|HAMAP-Rule:MF_01151,
KW   ECO:0000256|RuleBase:RU000639}.
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          190..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          57..91
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   219 AA;  23335 MW;  3166BB56E03622C4 CRC64;
     MTEETPGFNE NEKPEGPSDA TTPDDAAQAA GSADKAGPAG PAASGEELVE VGLQAQLDQA
     QAALTERTGD LQRLQAEYQN YRRRVERDRV TVKEIAVANL LSELLPTLDD IGRARDHGEL
     VGGFKSVAES LETVVAKMGL QQFGKEGEPF DPLVHEALMH SYAPDVTETT CVQILQPGYR
     IGERTIRPAR VAVAEPQPGA QGKAEDEASD EESGGPDEG
//
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