DNAK_CITBB
ID DNAK_CITBB Reviewed; 640 AA.
AC B5EC42;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=Gbem_3505;
OS Citrifermentans bemidjiense (strain ATCC BAA-1014 / DSM 16622 / JCM 12645 /
OS Bem) (Geobacter bemidjiensis).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Citrifermentans.
OX NCBI_TaxID=404380;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1014 / DSM 16622 / JCM 12645 / Bem;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Lovley D., Richardson P.;
RT "Complete sequence of Geobacter bemidjiensis BEM.";
RL Submitted (JUL-2008) 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; CP001124; ACH40498.1; -; Genomic_DNA.
DR RefSeq; WP_012531934.1; NC_011146.1.
DR AlphaFoldDB; B5EC42; -.
DR SMR; B5EC42; -.
DR STRING; 404380.Gbem_3505; -.
DR PRIDE; B5EC42; -.
DR EnsemblBacteria; ACH40498; ACH40498; Gbem_3505.
DR KEGG; gbm:Gbem_3505; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_7; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000008825; 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..640
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000119708"
FT REGION 600..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..640
FT /note="Basic and acidic residues"
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 640 AA; 68485 MW; 978D02F6C94C21D7 CRC64;
MSRVIGIDLG TTNSCVAVME GGEPVVIANA EGSRTTPSMI AFAESGERLV GQQAKRQAVT
NPENTLYAIK RLIGRKFETE AVKKDIAISP FKIVKADNSD AWVEVRGQKY SPPEISAMVL
QKMKKTAEDY LGEAVTDAVI TVPAYFDDSQ RQATKDAGKI AGLNVLRIIN EPTAAALAYG
LDKKKDEKIA VFDLGGGTFD VSILELGEGV FEVKSTNGDT FLGGEDFDQK IIDHIADEFK
KDQGIDLRGD KMALQRLKEA GEKAKCELST SLETDINLPF ITADASGPKH LTMKLTRAKL
ESICAELIAK LEGPCRTALK DAGLSASDID EVILVGGMTR MPIVQKKVQD IFGKLPNRGV
NPDEVVAIGA AIQGGVLRGD VKDVLLLDVT PLSLGIETLG GVLTKLIDKN STIPCRKSQV
FSTAADNQPA VSIHVLQGER EMAADNKTLG NFELSGIPAA PRGVPQIEVT FDIDANGIVH
VSAKDLGTGK EQSIRITASS GLSKEEVEKM VREAEAHAAD DKKKRELIEA KNQADNLIYQ
TEKSLTEFGD KIDASEKQKI EEGVAALKKA LEGSDADEIK KASDSLMQAS HKLAEAVYAK
TQGAGAEGGE QPHGEQEAGG AAKGEKVVDA DFEEVKDDKK