(data stored in SCRATCH zone)

SWISSPROT: GRPE_BACSU

ID   GRPE_BACSU              Reviewed;         187 AA.
AC   P15874;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   11-DEC-2019, entry version 132.
DE   RecName: Full=Protein GrpE {ECO:0000255|HAMAP-Rule:MF_01151};
DE   AltName: Full=HSP-70 cofactor {ECO:0000255|HAMAP-Rule:MF_01151};
GN   Name=grpE {ECO:0000255|HAMAP-Rule:MF_01151}; OrderedLocusNames=BSU25480;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / MB11;
RX   PubMed=2108432; DOI=10.1093/nar/18.5.1289;
RA   Wetzstein M., Schumann W.;
RT   "Nucleotide sequence of a Bacillus subtilis gene homologous to the grpE
RT   gene of E. coli located immediately upstream of the dnaK gene.";
RL   Nucleic Acids Res. 18:1289-1289(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / MB11;
RX   PubMed=1339421; DOI=10.1128/jb.174.10.3300-3310.1992;
RA   Wetzstein M., Voelker U., Dedio J., Loebau S., Zuber U., Schiesswohl M.,
RA   Herget C., Hecker M., Schumann W.;
RT   "Cloning, sequencing, and molecular analysis of the dnaK locus from
RT   Bacillus subtilis.";
RL   J. Bacteriol. 174:3300-3310(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-11.
RC   STRAIN=168 / IS58;
RX   PubMed=8012595; DOI=10.1099/00221287-140-4-741;
RA   Voelker U., Engelmann S., Maul B., Riethdorf S., Voelker A., Schmid R.,
RA   Mach H., Hecker M.;
RT   "Analysis of the induction of general stress proteins of Bacillus
RT   subtilis.";
RL   Microbiology 140:741-752(1994).
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:0000255|HAMAP-
CC       Rule:MF_01151}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01151}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000255|HAMAP-
CC       Rule:MF_01151}.
DR   EMBL; X51477; CAA35841.1; -; Genomic_DNA.
DR   EMBL; M84964; AAA22527.1; -; Genomic_DNA.
DR   EMBL; D84432; BAA12463.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14490.1; -; Genomic_DNA.
DR   PIR; S08418; S08418.
DR   RefSeq; NP_390426.1; NC_000964.3.
DR   RefSeq; WP_003230005.1; NZ_JNCM01000036.1.
DR   PDB; 2G61; Model; -; A=1-187.
DR   PDBsum; 2G61; -.
DR   SMR; P15874; -.
DR   STRING; 224308.BSU25480; -.
DR   jPOST; P15874; -.
DR   PaxDb; P15874; -.
DR   PRIDE; P15874; -.
DR   DNASU; 937846; -.
DR   EnsemblBacteria; CAB14490; CAB14490; BSU25480.
DR   GeneID; 937846; -.
DR   KEGG; bsu:BSU25480; -.
DR   PATRIC; fig|224308.179.peg.2769; -.
DR   eggNOG; ENOG4105K90; Bacteria.
DR   eggNOG; COG0576; LUCA.
DR   HOGENOM; HOG000252083; -.
DR   InParanoid; P15874; -.
DR   KO; K03687; -.
DR   OMA; YAYEKIA; -.
DR   PhylomeDB; P15874; -.
DR   BioCyc; BSUB:BSU25480-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IBA:GO_Central.
DR   GO; GO:0051087; F:chaperone binding; IEA:InterPro.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
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   1: Evidence at protein level;
DR   PRODOM; P15874.
DR   SWISS-2DPAGE; P15874.
KW   3D-structure; Chaperone; Cytoplasm; Direct protein sequencing;
KW   Reference proteome; Stress response.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8012595"
FT   CHAIN           2..187
FT                   /note="Protein GrpE"
FT                   /id="PRO_0000113742"
FT   VARIANT         2
FT                   /note="S -> H (in strain: IS58)"
FT   VARIANT         5
FT                   /note="K -> T (in strain: IS58)"
SQ   SEQUENCE   187 AA;  21683 MW;  A004CD3914AA846A CRC64;
     MSEEKQTVEQ NETEEQEIIE EQAAADEQQE ETNESELLQN QINELQGLLE EKENKLLRVQ
     ADFENYKRRS RLEMEASQKY RSQNIVTDLL PALDSFERAL QVEADNEQTK SLLQGMEMVH
     RQLVEALKKE GVEAIEAVGQ EFDPNLHQAV MQAEDENYGS NIVVEEMQKG YKLKDRVIRP
     SMVKVNQ
//

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