DNAK_RHIWR
ID DNAK_RHIWR Reviewed; 630 AA.
AC A5V5P9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Chaperone protein DnaK {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=HSP70 {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock 70 kDa protein {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock protein 70 {ECO:0000255|HAMAP-Rule:MF_00332};
GN Name=dnaK {ECO:0000255|HAMAP-Rule:MF_00332}; OrderedLocusNames=Swit_1250;
OS Rhizorhabdus wittichii (strain DSM 6014 / CCUG 31198 / JCM 15750 / NBRC
OS 105917 / EY 4224 / RW1) (Sphingomonas wittichii).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Rhizorhabdus.
OX NCBI_TaxID=392499;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6014 / CCUG 31198 / JCM 15750 / NBRC 105917 / EY 4224 / RW1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Halden R.U., Miller T.R., Salzberg S.L., Eisen J.A.,
RA Richardson P.;
RT "Complete sequence of chromosome of Sphingomonas wittichii RW1.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000255|HAMAP-Rule:MF_00332}.
CC -!- INDUCTION: By stress conditions e.g. heat shock. {ECO:0000255|HAMAP-
CC Rule:MF_00332}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000255|HAMAP-Rule:MF_00332}.
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DR EMBL; CP000699; ABQ67615.1; -; Genomic_DNA.
DR RefSeq; WP_011952093.1; NC_009511.1.
DR AlphaFoldDB; A5V5P9; -.
DR SMR; A5V5P9; -.
DR STRING; 392499.Swit_1250; -.
DR PRIDE; A5V5P9; -.
DR EnsemblBacteria; ABQ67615; ABQ67615; Swit_1250.
DR KEGG; swi:Swit_1250; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_5; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000001989; 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 3: Inferred from homology;
KW ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1..630
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059674"
FT REGION 604..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 198
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 630 AA; 67371 MW; 408B9AB3595946B9 CRC64;
MAKVIGIDLG TTNSCVAVME GGKPKVIENA EGARTTPSIV AFAKDGERLI GQPAKRQAVT
NPDNTIFAVK RLIGRRFDDP ITRKDTELVP YHIVKGPNGD AWVQAGGEDY SPSQISAFTL
QKMKETAESY LGETVTQAVI TVPAYFNDAQ RQATKDAGKI AGLEVLRIIN EPTAAALAYG
LEKNDGKTIA VYDLGGGTFD ISILEIGDGV FEVKSTNGDT FLGGEDFDAK LVEFFAADFQ
KAEGIDLTKD RLALQRLKEA AEKAKIELSS AQTTEVNLPF ITADATGPKH LVKSLTRADL
ERLVEPLIQR SIEPVKKALA DAGLKAADID EVVMVGGMTR MPKVREVVKS YFGKEPHTGV
NPDEVVAMGA AIQAGVLQGD VKDVLLLDVT PLSLGIETLG GVFTRMIDRN TTIPTKKSQT
YSTADDNQNA VTIRVFQGER EMAADNKMLG QFDLIGIPPA PRGVPQIEVT FDIDANGIVN
VSAKDKGTGK EQQIKIQASG GLSDADIDGM VKDAEKFAEE DKKRRAAAEA KNNAESLIHT
TERQLQEHGD KVDGGLKSEI EAAIADAKTA VEGGDADAMT EKAQALAQVA MKLGQAIYEK
EQAAAAAPGE EAPKDDDVVD AEFSEVDDKK