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DNAK_CAUVC
ID   DNAK_CAUVC              Reviewed;         631 AA.
AC   P20442;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Chaperone protein DnaK;
DE   AltName: Full=HSP70;
DE   AltName: Full=Heat shock 70 kDa protein;
DE   AltName: Full=Heat shock protein 70;
GN   Name=dnaK; OrderedLocusNames=CC_0010;
OS   Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=190650;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2345134; DOI=10.1128/jb.172.6.3051-3059.1990;
RA   Gomes S.L., Gober J.W., Shapiro L.;
RT   "Expression of the Caulobacter heat shock gene dnaK is developmentally
RT   controlled during growth at normal temperatures.";
RL   J. Bacteriol. 172:3051-3059(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19089 / CB15;
RX   PubMed=11259647; DOI=10.1073/pnas.061029298;
RA   Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA   Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA   Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA   Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA   Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA   Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT   "Complete genome sequence of Caulobacter crescentus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC   -!- INDUCTION: By heat shock.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; M55224; AAA62723.1; -; Genomic_DNA.
DR   EMBL; AE005673; AAK21998.1; -; Genomic_DNA.
DR   PIR; A35388; A35388.
DR   PIR; B87250; B87250.
DR   RefSeq; NP_418830.1; NC_002696.2.
DR   AlphaFoldDB; P20442; -.
DR   SMR; P20442; -.
DR   STRING; 190650.CC_0010; -.
DR   PRIDE; P20442; -.
DR   EnsemblBacteria; AAK21998; AAK21998; CC_0010.
DR   KEGG; ccr:CC_0010; -.
DR   PATRIC; fig|190650.5.peg.11; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_3_5; -.
DR   OMA; ISIKRHM; -.
DR   BioCyc; CAULO:CC0010-MON; -.
DR   Proteomes; UP000001816; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 2.60.34.10; -; 1.
DR   HAMAP; MF_00332; DnaK; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR012725; Chaperone_DnaK.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR029048; HSP70_C_sf.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375; PTHR19375; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF100920; SSF100920; 1.
DR   SUPFAM; SSF100934; SSF100934; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   TIGRFAMs; TIGR02350; prok_dnaK; 1.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Stress response.
FT   CHAIN           1..631
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078440"
FT   MOD_RES         198
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        92..98
FT                   /note="EIVKGPT -> RSSRARA (in Ref. 1; AAA62723)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        260
FT                   /note="Missing (in Ref. 1; AAA62723)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        397
FT                   /note="E -> D (in Ref. 1; AAA62723)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        441
FT                   /note="P -> A (in Ref. 1; AAA62723)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        449
FT                   /note="L -> Q (in Ref. 1; AAA62723)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        492
FT                   /note="Q -> H (in Ref. 2; AAK21998)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   631 AA;  67616 MW;  16C27D84CD85CD55 CRC64;
     MSKIIGIDLG TTNSCVAIMD GKTPKVIENA EGARTTPSVV AFLEDGERLI GQPAKRQAVT
     NPTNTLFAIK RLIGRTASDP VVEKDKGMVP YEIVKGPTGD AWVKAHGKDY SPQEVSAFIL
     QKMKEAAEAH LGEPVTKAVI TVPAYFNDAQ RQATKDAGKI AGLEVLRIIN EPTAAALAYG
     LDKNDGKKIA VYDLGGGTFD VSILEIGDGV FEVKSTNGDT FLGGEDFDLR IVDYLADEFK
     KEQGVDLRKD KLALQRLREE AEKAKKELSS TAQYEVNLPF ISMNASGPLH LNIKLSRAKL
     EALVDDLIAR TIGPCEQALK DAGLKKSDID EVILVGGMSR MPKVQQAVQD FFGREPHKGV
     NPDEVVALGA AVQAGVLQGD VKDVLLLDVT PLTLGIETLG GVFTPLIERN TTIPTKRSQT
     FSTADDNQSA VTIRVFQGER PMAQDNKMLG QFDLVGIPPA PRGVPQIEVT FDIDANGIVQ
     VHAKDKATNK EQSIRIQANG GLSDSDIERM VKEAEANKAA DEKKKQLVEA KNQGEAILHS
     TEKALAEHGD KVGAAEKTAI ETGITELKTA LEGEDVEAIQ AKTQALIQAS MKLGEAMYAA
     QQGSAEGGDA KADDGVVDAE FEEVDDNKPA A
 
 
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