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 27-MAR-2024, entry version 221.
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; Pseudomonadota; 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 EMDB; EMD-2332; -.
DR EMDB; EMD-2333; -.
DR EMDB; EMD-2334; -.
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; 511145-b0015; -.
DR EnsemblBacteria; AAC73126; AAC73126; b0015.
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; CPECAGD; -.
DR OrthoDB; 9779889at2; -.
DR PhylomeDB; P08622; -.
DR BioCyc; EcoCyc:EG10240-MONOMER; -.
DR BioCyc; MetaCyc:EG10240-MONOMER; -.
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:0031072; F:heat shock protein binding; IEA:InterPro.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IDA:EcoliWiki.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:EcoCyc.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IDA:EcoCyc.
DR GO; GO:0051087; F:protein-folding chaperone binding; IPI:CAFA.
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:0043335; P:protein unfolding; IDA:EcoCyc.
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; cd10747; DnaJ_C; 1.
DR CDD; cd10719; DnaJ_zf; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 2.10.230.10; Heat shock protein DnaJ, cysteine-rich domain; 1.
DR Gene3D; 2.60.260.20; Urease metallochaperone UreE, N-terminal domain; 2.
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 NCBIfam; TIGR02349; DnaJ_bact; 1.
DR PANTHER; PTHR43096:SF48; CHAPERONE PROTEIN DNAJ; 1.
DR PANTHER; PTHR43096; DNAJ HOMOLOG 1, MITOCHONDRIAL-RELATED; 1.
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; Chaperone J-domain; 1.
DR SUPFAM; SSF57938; DnaJ/Hsp40 cysteine-rich domain; 1.
DR SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 2.
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
//
