DNAK_ALBFT
ID DNAK_ALBFT Reviewed; 651 AA.
AC Q21X09;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=Rfer_1969;
OS Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
OS (Rhodoferax ferrireducens).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=338969;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-621 / DSM 15236 / T118;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236.";
RL Submitted (FEB-2006) 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; CP000267; ABD69694.1; -; Genomic_DNA.
DR RefSeq; WP_011464262.1; NC_007908.1.
DR AlphaFoldDB; Q21X09; -.
DR SMR; Q21X09; -.
DR STRING; 338969.Rfer_1969; -.
DR PRIDE; Q21X09; -.
DR EnsemblBacteria; ABD69694; ABD69694; Rfer_1969.
DR KEGG; rfr:Rfer_1969; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_4; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000008332; 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..651
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059642"
FT REGION 608..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 200
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 651 AA; 69972 MW; 0C2D528E61FD04F6 CRC64;
MGRIIGIDLG TTNSCVAIME GNTPKVIENS EGARTTPSII AYQEDGEVLV GASAKRQAVT
NPKNTLYAVK RLIGRKFTEK EVQKDINLMP YKIAAADNGD AWVEVRGNRM APQQVSADVL
RKMKKTAEDY LGETVTEAVI TVPAYFNDAQ RQATKDAGRI AGLDVKRIIN EPTAAALAYG
LDKTEKGDRK IAVFDLGGGT FDVSIIEIAD VDGEKQFEVL STNGDTFLGG EDFDQRIIDF
VIAEFKKEQG VDLGKDVLAL QRLKEAAEKA KIELSSSAQT DINLPYVTAD ASGPKHLSIK
LTRAKLESLV EELIERTIAP CRTAIKDAGV NVADINDVIL VGGMTRMPKV QEKVKELFGR
EPRKDVNPDE AVAVGAAIQG QVLSGDRKDV LLLDVTPLSL GIETLGGVMT KMITKNTTIP
TKFAQTFSTA DDNQPAVTIK VFQGEREIAA GNKMLGEFNL EGIPPSARGT PQIEVSFDID
ANGILHVGAK DKGTGKENKI TIKANSGLTE AEIQQMVKDA ELNAADDKRK LDLVQAKNQA
DASLHSVKKS LTEYGDKLEA GEKEKIEEAI KHLEEAIKGD DKAHIEEKST ALMTISQKLG
EKMYADMQAK QAAEAGAGDP GAQAAAGAQN TSNQAADDNV VDAEVKEVKK G