ID   DNAK_SYNC1              Reviewed;         634 AA.
AC   Q3A8C2;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=Pcar_0107;
OS   Syntrophotalea carbinolica (strain DSM 2380 / NBRC 103641 / GraBd1)
OS   (Pelobacter carbinolicus).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Syntrophotaleaceae; Syntrophotalea.
OX   NCBI_TaxID=338963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2380 / NBRC 103641 / GraBd1;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Pelobacter carbinolicus DSM 2380.";
RL   Submitted (OCT-2005) 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; CP000142; ABA87370.1; -; Genomic_DNA.
DR   RefSeq; WP_011339759.1; NC_007498.2.
DR   AlphaFoldDB; Q3A8C2; -.
DR   SMR; Q3A8C2; -.
DR   STRING; 338963.Pcar_0107; -.
DR   EnsemblBacteria; ABA87370; ABA87370; Pcar_0107.
DR   KEGG; pca:Pcar_0107; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_7; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000002534; 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..634
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000225991"
FT   REGION          599..634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        620..634
FT                   /note="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   634 AA;  68441 MW;  9AE824599891036E CRC64;
     MGKVIGIDLG TTNSCVAVME GGEPVVIANA EGSRTTPSMV AFTENGERLV GQQAKRQAVT
     NPENTLFAIK RLIGRKFDSD AVRRDIQISP FEIVKADNGD AWVDVRDKKY SPPEISAMIL
     QKMKQTAEDY LGEKVTDAVI TVPAYFNDSQ RQATKDAGKI SGLNVLRIIN EPTAASLAYG
     LDKKSEEKIA VFDLGGGTFD ISILELGDGV FEVKSTNGDT FLGGEDFDQH IMDYVADEFK
     KEQGIDLRND KMALQRLKEA CEKAKCELST SMETDINLPF ITADQSGPKH LNLRLTRSKL
     ESICSSLLAK LVEPCRMALK DAGLSASDVD EVLLVGGMTR MPAVQAKVQE IFGKTPNKGV
     NPDEVVAIGA AIQGGVLKGE VKDVLLLDVT PLSLGIETLG SIMTKLIEKN TTIPCKKSQI
     FSTAADNQPA VSVHVLQGER EMAGDNKTIG RFELVGIPPA PRGVPQVEVT FDIDANGILH
     VSAKDLGTGK EQSIRITASS GLSDEEIDKM VKDAEAHSSE DKKKREIIEA RNQADGLAYS
     TEKSLKEHGD KIDEETRNNI QTALDALKAA MEGDDPEDIR QKSEALATAS HKLAEAVYKQ
     TQEGAEAASE AGEQSAGDEG VVDAEFEEVD EQNK