(data stored in ACNUC7421 zone)

SWISSPROT: Q5LWF4_RUEPO

ID   Q5LWF4_RUEPO            Unreviewed;       187 AA.
AC   Q5LWF4;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 90.
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   ECO:0000313|EMBL:AAV93341.1};
GN   OrderedLocusNames=SPO0010 {ECO:0000313|EMBL:AAV93341.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV93341.1, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV93341.1, ECO:0000313|Proteomes:UP000001023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E.,
RA   Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2] {ECO:0000313|EMBL:AAV93341.1, ECO:0000313|Proteomes:UP000001023}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
CC   -!- FUNCTION: Participates actively in the response to hyperosmotic
CC       and heat shock by preventing the aggregation of stress-denatured
CC       proteins, in association with DnaK and GrpE. It is the nucleotide
CC       exchange factor for DnaK and may function as a thermosensor.
CC       Unfolded proteins bind initially to DnaJ; upon interaction with
CC       the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting
CC       in the formation of a stable complex. GrpE releases ADP from DnaK;
CC       ATP binding to DnaK triggers the release of the substrate protein,
CC       thus completing the reaction cycle. Several rounds of ATP-
CC       dependent interactions between DnaJ, DnaK and GrpE are required
CC       for fully efficient folding. {ECO:0000256|HAMAP-Rule:MF_01151,
CC       ECO:0000256|RuleBase:RU000639, ECO:0000256|SAAS:SAAS00067045}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01151,
CC       ECO:0000256|SAAS:SAAS00066998}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01151,
CC       ECO:0000256|SAAS:SAAS00067044}.
CC   -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000256|HAMAP-
CC       Rule:MF_01151, ECO:0000256|RuleBase:RU004478,
CC       ECO:0000256|SAAS:SAAS00562011}.
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DR   EMBL; CP000031; AAV93341.1; -; Genomic_DNA.
DR   RefSeq; WP_011045782.1; NC_003911.12.
DR   STRING; 246200.SPO0010; -.
DR   EnsemblBacteria; AAV93341; AAV93341; SPO0010.
DR   KEGG; sil:SPO0010; -.
DR   eggNOG; ENOG4105K90; Bacteria.
DR   eggNOG; COG0576; LUCA.
DR   HOGENOM; HOG000252083; -.
DR   KO; K03687; -.
DR   OMA; YAYEKIA; -.
DR   OrthoDB; 1906715at2; -.
DR   BioCyc; RPOM246200:G1G48-10-MONOMER; -.
DR   Proteomes; UP000001023; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0051087; F:chaperone binding; IEA:InterPro.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   CDD; cd00446; GrpE; 1.
DR   Gene3D; 2.30.22.10; -; 1.
DR   Gene3D; 3.90.20.20; -; 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; PTHR21237; 1.
DR   Pfam; PF01025; GrpE; 1.
DR   PRINTS; PR00773; GRPEPROTEIN.
DR   SUPFAM; SSF51064; SSF51064; 1.
DR   SUPFAM; SSF58014; SSF58014; 1.
DR   PROSITE; PS01071; GRPE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q5LWF4.
DR   SWISS-2DPAGE; Q5LWF4.
KW   Chaperone {ECO:0000256|HAMAP-Rule:MF_01151,
KW   ECO:0000256|RuleBase:RU000639, ECO:0000256|SAAS:SAAS00132311};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001023};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01151,
KW   ECO:0000256|SAAS:SAAS00066909};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001023};
KW   Stress response {ECO:0000256|HAMAP-Rule:MF_01151,
KW   ECO:0000256|RuleBase:RU000639, ECO:0000256|SAAS:SAAS00132302}.
FT   COILED       11     48       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   187 AA;  20662 MW;  9A007E00DC95DD30 CRC64;
     MAKPNNEEFL DDIATAEAEE LAEEMAEISD EAAELDTLRA ERDAFKDKFM RALADAENVR
     KRGERARREA EQYGGSKLAR DMLPVYDNMK RALETVTDEQ RAVSGALIEG IELTMRALLD
     VFGKHGIQVL SPQVGDRFDP QMHEAMFEAP VPGTKAGDII QVSAEGFMLH DRLLRPAQVG
     VSSMPAG
//

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