ID   DNAK_SULMW              Reviewed;         630 AA.
AC   A8Z5V5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=SMGWSS_091;
OS   Sulcia muelleri (strain GWSS).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Candidatus Sulcia.
OX   NCBI_TaxID=444179;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GWSS;
RX   PubMed=18048332; DOI=10.1073/pnas.0708855104;
RA   McCutcheon J.P., Moran N.A.;
RT   "Parallel genomic evolution and metabolic interdependence in an ancient
RT   symbiosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:19392-19397(2007).
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; CP000770; ABS30506.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8Z5V5; -.
DR   SMR; A8Z5V5; -.
DR   STRING; 444179.SMGWSS_091; -.
DR   PRIDE; A8Z5V5; -.
DR   EnsemblBacteria; ABS30506; ABS30506; SMGWSS_091.
DR   KEGG; smg:SMGWSS_091; -.
DR   HOGENOM; CLU_005965_2_4_10; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000000781; 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; 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_1000079252"
FT   REGION          604..630
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        616..630
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         197
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   630 AA;  69330 MW;  73881810617D7465 CRC64;
     MSKIIGIDLG TTNSCVSVME GNSPVVVPNS EGKRTTPSII AFIEGGETKV GDPAKRQAVT
     NPSKTIFSIK RFMGRNFSEV TEELKNIPYK IIKGENDTPR VSIGNKLYTP QEISAMILQK
     MKKTAEDYLG NEVKQAVITV PAYFNDAQRQ ATKEAGEIAG LNVERIINEP TAAALAYGLD
     KNNQNKKIVV YDLGGGTFDI SILELGDGVF EVLSTSGDTH LGGDDFDKVI IDWLVKEFKV
     EQGVDLSNDS MAYQRLKESA EKAKIELSSS TKTEINLPYI TATPSGPKHL VKTLTRAKFE
     ELSDDLIKRS LYPCKNALKA SNLISKDIDE VILVGGSTRI PKIQEQVEKF FEKIPSKGVN
     PDEVVSIGAA IQGGVLSGDV KDVLLLDVTP LSLGIETLGG VFTKLIDSNT TIPTKKSEIF
     STATDNQSAV TIRVGQGERS MFNDNKEIGR FDLIDIAPAP RGIPQIEVTF DIDANGILNV
     SAKDKSTGKE QSIRIQASSG LSKNEIERMK KEAQENADKD NKIKEEIEKI NSADSIIFQT
     EKQLKEYGNK ISEETKKKLE INLNNLKDAR NSKNISDIDN YINKINNILS SSYQEIYKNN
     ESVKNNESVK NNESVKNNES VKDVDFEEIK