(data stored in SCRATCH zone)

SWISSPROT: A4AVK6_MARSH

ID   A4AVK6_MARSH            Unreviewed;       186 AA.
AC   A4AVK6;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 66.
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   OrderedLocusNames=FB2170_01140 {ECO:0000313|EMBL:EAR00228.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00228.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00228.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
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|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; CP002157; EAR00228.1; -; Genomic_DNA.
DR   RefSeq; WP_013304923.1; NC_014472.1.
DR   STRING; 313603.FB2170_01140; -.
DR   EnsemblBacteria; EAR00228; EAR00228; FB2170_01140.
DR   KEGG; fbc:FB2170_01140; -.
DR   eggNOG; ENOG4107XPB; Bacteria.
DR   eggNOG; COG0576; LUCA.
DR   HOGENOM; HOG000252083; -.
DR   KO; K03687; -.
DR   OMA; YAYEKIA; -.
DR   OrthoDB; 1906715at2; -.
DR   BioCyc; MSP313603:G1GNS-492-MONOMER; -.
DR   Proteomes; UP000001602; 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.
PE   3: Inferred from homology;
DR   PRODOM; A4AVK6.
DR   SWISS-2DPAGE; A4AVK6.
KW   Chaperone {ECO:0000256|HAMAP-Rule:MF_01151,
KW   ECO:0000256|SAAS:SAAS00132311}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01151,
KW   ECO:0000256|SAAS:SAAS00066909};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602};
KW   Stress response {ECO:0000256|HAMAP-Rule:MF_01151,
KW   ECO:0000256|SAAS:SAAS00132302}.
FT   COILED       30     60       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   186 AA;  21235 MW;  0D25D296DCFBCBD7 CRC64;
     MGKKDKAKEV NEPISEEQMN IDIENGQEGA SKEEQNLSVE EKLQEELAKE KDKFLRLFAE
     FENYKRRTSK ERMDLFKTAG QEVIVSLLPV LDDFERALKE LSKSEDKEMF KGVELINGKL
     RETLKSKGME DVGTKEGDTF DAEIHDAITQ IPAPNKKLKG KIIDVVERGY KLGDRIIRHP
     KVVVGN
//

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