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DNAJ_ECOLI
ID   DNAJ_ECOLI              Reviewed;         376 AA.
AC   P08622;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 213.
DE   RecName: Full=Chaperone protein DnaJ;
DE   AltName: Full=HSP40;
DE   AltName: Full=Heat shock protein J;
GN   Name=dnaJ; Synonyms=groP; OrderedLocusNames=b0015, JW0014;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-6.
RX   PubMed=3003084; DOI=10.1016/s0021-9258(17)36007-6;
RA   Ohki M., Tamura F., Nishimura S., Uchida H.;
RT   "Nucleotide sequence of the Escherichia coli dnaJ gene and purification of
RT   the gene product.";
RL   J. Biol. Chem. 261:1778-1781(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=3003085; DOI=10.1016/s0021-9258(17)36008-8;
RA   Bardwell J.C.A., Tilly K., Craig E., King J., Zylicz M., Georgopoulos C.;
RT   "The nucleotide sequence of the Escherichia coli K12 dnaJ+ gene. A gene
RT   that encodes a heat shock protein.";
RL   J. Biol. Chem. 261:1782-1785(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA   Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA   Mizobuchi K., Nakata A.;
RT   "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT   2.4 min region.";
RL   Nucleic Acids Res. 20:3305-3308(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   FUNCTION.
RX   PubMed=1826368; DOI=10.1073/pnas.88.7.2874;
RA   Liberek K., Marszalek J., Ang D., Georgopoulos C., Zylicz M.;
RT   "Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate
RT   ATPase activity of DnaK.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:2874-2878(1991).
RN   [7]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
RN   [8]
RP   FUNCTION.
RX   PubMed=15302880; DOI=10.1074/jbc.m402405200;
RA   Zietkiewicz S., Krzewska J., Liberek K.;
RT   "Successive and synergistic action of the Hsp70 and Hsp100 chaperones in
RT   protein disaggregation.";
RL   J. Biol. Chem. 279:44376-44383(2004).
RN   [9]
RP   ROLE IN HEAT-SHOCK RESPONSE.
RX   PubMed=15044009; DOI=10.1016/s0014-5793(04)00190-5;
RA   Siegenthaler R.K., Grimshaw J.P., Christen P.;
RT   "Immediate response of the DnaK molecular chaperone system to heat shock.";
RL   FEBS Lett. 562:105-110(2004).
RN   [10]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX   PubMed=14726952; DOI=10.1038/sj.embor.7400067;
RA   Genevaux P., Keppel F., Schwager F., Langendijk-Genevaux P.S., Hartl F.U.,
RA   Georgopoulos C.;
RT   "In vivo analysis of the overlapping functions of DnaK and trigger
RT   factor.";
RL   EMBO Rep. 5:195-200(2004).
RN   [11]
RP   INTERACTION WITH DNAK.
RX   PubMed=14729677; DOI=10.1074/jbc.m308782200;
RA   Watanabe Y.H., Yoshida M.;
RT   "Trigonal DnaK-DnaJ complex versus free DnaK and DnaJ: heat stress converts
RT   the former to the latter, and only the latter can do disaggregation in
RT   cooperation with ClpB.";
RL   J. Biol. Chem. 279:15723-15727(2004).
RN   [12]
RP   ROLE IN PLASMID DNA REPLICATION.
RX   PubMed=15485812; DOI=10.1074/jbc.m407531200;
RA   Zzaman S., Reddy J.M., Bastia D.;
RT   "The DnaK-DnaJ-GrpE chaperone system activates inert wild type pi initiator
RT   protein of R6K into a form active in replication initiation.";
RL   J. Biol. Chem. 279:50886-50894(2004).
RN   [13]
RP   MUTAGENESIS OF HIS-33.
RX   PubMed=8106526; DOI=10.1016/s0021-9258(17)37706-2;
RA   Wall D., Zylicz M., Georgopoulos C.;
RT   "The NH2-terminal 108 amino acids of the Escherichia coli DnaJ protein
RT   stimulate the ATPase activity of DnaK and are sufficient for lambda
RT   replication.";
RL   J. Biol. Chem. 269:5446-5451(1994).
RN   [14]
RP   MUTAGENESIS OF ASP-35.
RX   PubMed=9860950; DOI=10.1073/pnas.95.26.15223;
RA   Suh W.-C., Burkholder W.F., Lu C.Z., Zhao X., Gottesman M.E., Gross C.A.;
RT   "Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone
RT   DnaJ.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:15223-15228(1998).
RN   [15]
RP   MUTAGENESIS OF ARG-19; GLU-20; 25-TYR--GLN-38; LYS-41; GLU-42; GLU-44;
RP   46-LYS--GLU-49; LYS-51; GLU-52; TYR-54; GLU-55; 58-THR--ARG-63; ASP-67 AND
RP   GLN-68.
RX   PubMed=12454054; DOI=10.1093/genetics/162.3.1045;
RA   Genevaux P., Schwager F., Georgopoulos C., Kelley W.L.;
RT   "Scanning mutagenesis identifies amino acid residues essential for the in
RT   vivo activity of the Escherichia coli DnaJ (Hsp40) J-domain.";
RL   Genetics 162:1045-1053(2002).
RN   [16]
RP   MUTAGENESIS OF CYS-144; CYS-147; CYS-161; CYS-164; CYS-183; CYS-186;
RP   CYS-197 AND CYS-200.
RX   PubMed=12941935; DOI=10.1074/jbc.m307491200;
RA   Linke K., Wolfram T., Bussemer J., Jakob U.;
RT   "The roles of the two zinc binding sites in DnaJ.";
RL   J. Biol. Chem. 278:44457-44466(2003).
RN   [17]
RP   MUTAGENESIS OF CYS-161; CYS-164; CYS-183 AND CYS-186.
RX   PubMed=15683252; DOI=10.1021/bi0480943;
RA   Shi Y.-Y., Tang W., Hao S.-F., Wang C.-C.;
RT   "Contributions of cysteine residues in Zn2 to zinc fingers and thiol-
RT   disulfide oxidoreductase activities of chaperone DnaJ.";
RL   Biochemistry 44:1683-1689(2005).
RN   [18]
RP   STRUCTURE BY NMR OF 1-108.
RX   PubMed=8764403; DOI=10.1006/jmbi.1996.0395;
RA   Pellechia M., Szyperski T., Wall D., Georgopoulos C., Wuethrich K.;
RT   "NMR structure of the J-domain and the Gly/Phe-rich region of the
RT   Escherichia coli DnaJ chaperone.";
RL   J. Mol. Biol. 260:236-250(1996).
RN   [19]
RP   STRUCTURE BY NMR OF 1-105.
RX   PubMed=10210198; DOI=10.1110/ps.8.1.203;
RA   Huang K., Flanagan J.M., Prestegard J.H.;
RT   "The influence of C-terminal extension on the structure of the 'J-domain'
RT   in E. coli DnaJ.";
RL   Protein Sci. 8:203-214(1999).
RN   [20]
RP   STRUCTURE BY NMR OF 131-209.
RX   PubMed=10891270; DOI=10.1006/jmbi.2000.3923;
RA   Martinez-Yamout M., Legge G.B., Zhang O., Wright P.E., Dyson H.J.;
RT   "Solution structure of the cysteine-rich domain of the Escherichia coli
RT   chaperone protein DnaJ.";
RL   J. Mol. Biol. 300:805-818(2000).
CC   -!- FUNCTION: Interacts with DnaK and GrpE to disassemble a protein complex
CC       at the origins of replication of phage lambda and several plasmids.
CC       Participates actively in the response to hyperosmotic and heat shock by
CC       preventing the aggregation of stress-denatured proteins and by
CC       disaggregating proteins, also in an autonomous, DnaK-independent
CC       fashion. Unfolded proteins bind initially to DnaJ; upon interaction
CC       with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting
CC       in the formation of a stable complex. GrpE releases ADP from DnaK; ATP
CC       binding to DnaK triggers the release of the substrate protein, thus
CC       completing the reaction cycle. Several rounds of ATP-dependent
CC       interactions between DnaJ, DnaK and GrpE are required for fully
CC       efficient folding. {ECO:0000269|PubMed:15044009,
CC       ECO:0000269|PubMed:15302880, ECO:0000269|PubMed:15485812,
CC       ECO:0000269|PubMed:1826368}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 2 Zn(2+) ions per monomer.;
CC   -!- SUBUNIT: Homodimer.
CC   -!- INTERACTION:
CC       P08622; P0A6Y8: dnaK; NbExp=8; IntAct=EBI-545285, EBI-542092;
CC       P08622; P06993: malT; NbExp=5; IntAct=EBI-545285, EBI-542934;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: By heat shock under the control of the HtpR regulatory
CC       protein.
CC   -!- DOMAIN: The J domain is necessary and sufficient to stimulate DnaK
CC       ATPase activity. Zinc center 1 plays an important role in the
CC       autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2
CC       is essential for interaction with DnaK and for DnaJ activity.
CC   -!- DISRUPTION PHENOTYPE: Single dnaJ and double dnaK-dnaJ disruption are
CC       non-essential; synthetic lethality is seen in a triple tig-dnaK-dnaJ
CC       disruption, although this depends on temperature (triple disruptions
CC       grow slowly at 20 and 34 degrees Celsius but not at 43 degrees) and
CC       strain background. {ECO:0000269|PubMed:14726952}.
CC   -!- SIMILARITY: Belongs to the DnaJ family. {ECO:0000305}.
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DR   EMBL; M12544; AAA00009.1; -; Genomic_DNA.
DR   EMBL; M12565; AAA23693.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73126.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAB96590.1; -; Genomic_DNA.
DR   PIR; A92572; HHECDJ.
DR   RefSeq; NP_414556.1; NC_000913.3.
DR   RefSeq; WP_001118476.1; NZ_LN832404.1.
DR   PDB; 1BQ0; NMR; -; A=2-104.
DR   PDB; 1BQZ; NMR; -; A=2-78.
DR   PDB; 1EXK; NMR; -; A=131-209.
DR   PDB; 1XBL; NMR; -; A=2-108.
DR   PDB; 5NRO; X-ray; 3.25 A; B=1-105.
DR   PDBsum; 1BQ0; -.
DR   PDBsum; 1BQZ; -.
DR   PDBsum; 1EXK; -.
DR   PDBsum; 1XBL; -.
DR   PDBsum; 5NRO; -.
DR   AlphaFoldDB; P08622; -.
DR   SMR; P08622; -.
DR   BioGRID; 4259725; 278.
DR   BioGRID; 849156; 3.
DR   DIP; DIP-9460N; -.
DR   IntAct; P08622; 101.
DR   MINT; P08622; -.
DR   STRING; 511145.b0015; -.
DR   jPOST; P08622; -.
DR   PaxDb; P08622; -.
DR   PRIDE; P08622; -.
DR   EnsemblBacteria; AAC73126; AAC73126; b0015.
DR   EnsemblBacteria; BAB96590; BAB96590; BAB96590.
DR   GeneID; 944753; -.
DR   KEGG; ecj:JW0014; -.
DR   KEGG; eco:b0015; -.
DR   PATRIC; fig|1411691.4.peg.2269; -.
DR   EchoBASE; EB0236; -.
DR   eggNOG; COG0484; Bacteria.
DR   HOGENOM; CLU_017633_0_7_6; -.
DR   InParanoid; P08622; -.
DR   OMA; DLHCTVT; -.
DR   PhylomeDB; P08622; -.
DR   BioCyc; EcoCyc:EG10240-MON; -.
DR   BioCyc; MetaCyc:EG10240-MON; -.
DR   EvolutionaryTrace; P08622; -.
DR   PRO; PR:P08622; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0016020; C:membrane; IDA:EcoliWiki.
DR   GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0051087; F:chaperone binding; IPI:CAFA.
DR   GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IDA:EcoliWiki.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IDA:EcoCyc.
DR   GO; GO:0016989; F:sigma factor antagonist activity; IDA:EcoCyc.
DR   GO; GO:0051082; F:unfolded protein binding; IDA:CAFA.
DR   GO; GO:0008270; F:zinc ion binding; IDA:EcoliWiki.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IDA:CAFA.
DR   GO; GO:0006260; P:DNA replication; IMP:EcoliWiki.
DR   GO; GO:0006457; P:protein folding; IDA:EcoliWiki.
DR   GO; GO:0042026; P:protein refolding; IDA:EcoliWiki.
DR   GO; GO:0065003; P:protein-containing complex assembly; IDA:CAFA.
DR   GO; GO:0009408; P:response to heat; IMP:EcoCyc.
DR   GO; GO:0016032; P:viral process; IDA:EcoCyc.
DR   CDD; cd06257; DnaJ; 1.
DR   CDD; cd10719; DnaJ_zf; 1.
DR   Gene3D; 1.10.287.110; -; 1.
DR   HAMAP; MF_01152; DnaJ; 1.
DR   InterPro; IPR012724; DnaJ.
DR   InterPro; IPR002939; DnaJ_C.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR018253; DnaJ_domain_CS.
DR   InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR   InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR   InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR   InterPro; IPR036869; J_dom_sf.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF01556; DnaJ_C; 1.
DR   Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; SSF46565; 1.
DR   SUPFAM; SSF49493; SSF49493; 2.
DR   SUPFAM; SSF57938; SSF57938; 1.
DR   TIGRFAMs; TIGR02349; DnaJ_bact; 1.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS51188; ZF_CR; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chaperone; Cytoplasm; Direct protein sequencing;
KW   DNA replication; Metal-binding; Reference proteome; Repeat;
KW   Stress response; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:3003084"
FT   CHAIN           2..376
FT                   /note="Chaperone protein DnaJ"
FT                   /id="PRO_0000070777"
FT   DOMAIN          3..72
FT                   /note="J"
FT   REPEAT          144..151
FT                   /note="CXXCXGXG motif"
FT   REPEAT          161..168
FT                   /note="CXXCXGXG motif"
FT   REPEAT          183..190
FT                   /note="CXXCXGXG motif"
FT   REPEAT          197..204
FT                   /note="CXXCXGXG motif"
FT   ZN_FING         131..209
FT                   /note="CR-type"
FT   BINDING         144
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   BINDING         147
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   BINDING         161
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   BINDING         164
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   BINDING         183
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   BINDING         186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   BINDING         197
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   BINDING         200
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   MUTAGEN         19..20
FT                   /note="RE->AA: No effect."
FT   MUTAGEN         25
FT                   /note="Y->A: Loss of activity."
FT   MUTAGEN         26
FT                   /note="K->A: Loss of activity."
FT   MUTAGEN         27
FT                   /note="R->A: No effect."
FT   MUTAGEN         28
FT                   /note="L->A: No effect."
FT   MUTAGEN         29
FT                   /note="A->G: No effect."
FT   MUTAGEN         30..31
FT                   /note="MK->AA: No effect."
FT   MUTAGEN         32
FT                   /note="Y->A: No effect."
FT   MUTAGEN         33
FT                   /note="H->Q: Loss of ability to stimulate DnaK ATPase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:8106526"
FT   MUTAGEN         34
FT                   /note="P->F: Loss of function."
FT   MUTAGEN         35
FT                   /note="D->N: Loss of ability to bind DnaK."
FT                   /evidence="ECO:0000269|PubMed:9860950"
FT   MUTAGEN         36
FT                   /note="R->A: Decrease in chaperone function."
FT   MUTAGEN         37
FT                   /note="N->A: Decrease in chaperone function."
FT   MUTAGEN         38
FT                   /note="Q->A: No effect."
FT   MUTAGEN         41..42
FT                   /note="KE->AA: No effect."
FT   MUTAGEN         44
FT                   /note="E->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:12454054"
FT   MUTAGEN         46
FT                   /note="K->A: No effect."
FT   MUTAGEN         47
FT                   /note="F->A: Loss of function."
FT   MUTAGEN         48..49
FT                   /note="KE->AA: No effect."
FT   MUTAGEN         51..52
FT                   /note="KE->AA: No effect."
FT   MUTAGEN         54
FT                   /note="Y->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:12454054"
FT   MUTAGEN         55
FT                   /note="E->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:12454054"
FT   MUTAGEN         58..59
FT                   /note="TD->AA: No effect."
FT   MUTAGEN         60..61
FT                   /note="SQ->AA: No effect."
FT   MUTAGEN         62..63
FT                   /note="KR->AA: No effect."
FT   MUTAGEN         67..68
FT                   /note="DQ->AA: No effect."
FT   MUTAGEN         144
FT                   /note="C->S: Loss of DnaK-independent chaperone activity;
FT                   when associated with S-147; S-197 and S-200."
FT                   /evidence="ECO:0000269|PubMed:12941935"
FT   MUTAGEN         147
FT                   /note="C->S: Loss of DnaK-independent chaperone activity;
FT                   when associated with S-144; S-197 and S-200."
FT                   /evidence="ECO:0000269|PubMed:12941935"
FT   MUTAGEN         161
FT                   /note="C->H: No effect on chaperone function; when
FT                   associated with H-183."
FT                   /evidence="ECO:0000269|PubMed:12941935,
FT                   ECO:0000269|PubMed:15683252"
FT   MUTAGEN         161
FT                   /note="C->S: Loss of function; when associated with S-164;
FT                   S-183 and S-186."
FT                   /evidence="ECO:0000269|PubMed:12941935,
FT                   ECO:0000269|PubMed:15683252"
FT   MUTAGEN         164
FT                   /note="C->H: No effect on chaperone function; when
FT                   associated with H-183."
FT                   /evidence="ECO:0000269|PubMed:12941935,
FT                   ECO:0000269|PubMed:15683252"
FT   MUTAGEN         164
FT                   /note="C->S: Loss of function; when associated with S-161;
FT                   S-183 and S-186."
FT                   /evidence="ECO:0000269|PubMed:12941935,
FT                   ECO:0000269|PubMed:15683252"
FT   MUTAGEN         183
FT                   /note="C->H: No effect on chaperone function. Same effect;
FT                   when associated with H-161 or H-164."
FT                   /evidence="ECO:0000269|PubMed:12941935,
FT                   ECO:0000269|PubMed:15683252"
FT   MUTAGEN         183
FT                   /note="C->S: Loss of function; when associated with S-161;
FT                   S-164 and S-186."
FT                   /evidence="ECO:0000269|PubMed:12941935,
FT                   ECO:0000269|PubMed:15683252"
FT   MUTAGEN         186
FT                   /note="C->H: No effect on chaperone function."
FT                   /evidence="ECO:0000269|PubMed:12941935,
FT                   ECO:0000269|PubMed:15683252"
FT   MUTAGEN         186
FT                   /note="C->S: Loss of function; when associated with S-161;
FT                   S-164 and S-184."
FT                   /evidence="ECO:0000269|PubMed:12941935,
FT                   ECO:0000269|PubMed:15683252"
FT   MUTAGEN         197
FT                   /note="C->S: Loss of DnaK-independent chaperone activity;
FT                   when associated with S-144; S-147 and S-200."
FT                   /evidence="ECO:0000269|PubMed:12941935"
FT   MUTAGEN         200
FT                   /note="C->S: Loss of DnaK-independent chaperone activity;
FT                   when associated with S-144; S-147 and S-197."
FT                   /evidence="ECO:0000269|PubMed:12941935"
FT   HELIX           6..10
FT                   /evidence="ECO:0007829|PDB:5NRO"
FT   STRAND          13..15
FT                   /evidence="ECO:0007829|PDB:1XBL"
FT   HELIX           18..32
FT                   /evidence="ECO:0007829|PDB:5NRO"
FT   HELIX           34..37
FT                   /evidence="ECO:0007829|PDB:5NRO"
FT   TURN            38..40
FT                   /evidence="ECO:0007829|PDB:1BQ0"
FT   HELIX           41..58
FT                   /evidence="ECO:0007829|PDB:5NRO"
FT   HELIX           60..64
FT                   /evidence="ECO:0007829|PDB:5NRO"
FT   TURN            66..68
FT                   /evidence="ECO:0007829|PDB:1BQ0"
FT   TURN            70..72
FT                   /evidence="ECO:0007829|PDB:1BQ0"
FT   TURN            132..134
FT                   /evidence="ECO:0007829|PDB:1EXK"
FT   STRAND          141..143
FT                   /evidence="ECO:0007829|PDB:1EXK"
FT   HELIX           145..147
FT                   /evidence="ECO:0007829|PDB:1EXK"
FT   TURN            148..150
FT                   /evidence="ECO:0007829|PDB:1EXK"
FT   STRAND          154..156
FT                   /evidence="ECO:0007829|PDB:1EXK"
FT   TURN            162..166
FT                   /evidence="ECO:0007829|PDB:1EXK"
FT   STRAND          167..174
FT                   /evidence="ECO:0007829|PDB:1EXK"
FT   STRAND          177..182
FT                   /evidence="ECO:0007829|PDB:1EXK"
FT   TURN            184..188
FT                   /evidence="ECO:0007829|PDB:1EXK"
FT   STRAND          189..192
FT                   /evidence="ECO:0007829|PDB:1EXK"
FT   STRAND          194..196
FT                   /evidence="ECO:0007829|PDB:1EXK"
FT   HELIX           198..200
FT                   /evidence="ECO:0007829|PDB:1EXK"
FT   STRAND          203..207
FT                   /evidence="ECO:0007829|PDB:1EXK"
SQ   SEQUENCE   376 AA;  41100 MW;  05FA762EF9844532 CRC64;
     MAKQDYYEIL GVSKTAEERE IRKAYKRLAM KYHPDRNQGD KEAEAKFKEI KEAYEVLTDS
     QKRAAYDQYG HAAFEQGGMG GGGFGGGADF SDIFGDVFGD IFGGGRGRQR AARGADLRYN
     MELTLEEAVR GVTKEIRIPT LEECDVCHGS GAKPGTQPQT CPTCHGSGQV QMRQGFFAVQ
     QTCPHCQGRG TLIKDPCNKC HGHGRVERSK TLSVKIPAGV DTGDRIRLAG EGEAGEHGAP
     AGDLYVQVQV KQHPIFEREG NNLYCEVPIN FAMAALGGEI EVPTLDGRVK LKVPGETQTG
     KLFRMRGKGV KSVRGGAQGD LLCRVVVETP VGLNERQKQL LQELQESFGG PTGEHNSPRS
     KSFFDGVKKF FDDLTR
 
 
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