ID   DNAK_MYXXD              Reviewed;         607 AA.
AC   P95334; Q1CXT5;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 2.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Chaperone protein DnaK;
DE   AltName: Full=HSP70;
DE   AltName: Full=Heat shock 70 kDa protein;
DE   AltName: Full=Heat shock protein 70;
GN   Name=dnaK; Synonyms=sglK; OrderedLocusNames=MXAN_6671;
OS   Myxococcus xanthus (strain DK1622).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=246197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9765567; DOI=10.1128/jb.180.20.5357-5368.1998;
RA   Weimer R.M., Creighton C.X., Stassinopoulos A., Youderian P.,
RA   Hartzell P.L.;
RT   "A chaperone in the HSP70 family controls production of extracellular
RT   fibrils in Myxococcus xanthus.";
RL   J. Bacteriol. 180:5357-5368(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK1622;
RX   PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA   Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., Eisen J.,
RA   Ronning C.M., Barbazuk W.B., Blanchard M., Field C., Halling C., Hinkle G.,
RA   Iartchuk O., Kim H.S., Mackenzie C., Madupu R., Miller N., Shvartsbeyn A.,
RA   Sullivan S.A., Vaudin M., Wiegand R., Kaplan H.B.;
RT   "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
CC   -!- FUNCTION: Potential chaperone for other proteins involved in social
CC       motility.
CC   -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; U83800; AAC64205.1; -; Genomic_DNA.
DR   EMBL; CP000113; ABF90084.1; -; Genomic_DNA.
DR   RefSeq; WP_011556596.1; NC_008095.1.
DR   AlphaFoldDB; P95334; -.
DR   SMR; P95334; -.
DR   STRING; 246197.MXAN_6671; -.
DR   PRIDE; P95334; -.
DR   EnsemblBacteria; ABF90084; ABF90084; MXAN_6671.
DR   GeneID; 41363869; -.
DR   KEGG; mxa:MXAN_6671; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_7; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000002402; 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..607
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078501"
FT   MOD_RES         201
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        353
FT                   /note="K -> N (in Ref. 1; AAC64205)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   607 AA;  65348 MW;  4296F6E804083717 CRC64;
     MGKVIGIDLG TTNSCVAVME GGEPVVIPNS EGSRTTPSMV GFTDSGERLV GQIAKRQAIT
     NPENTVFAAK RLIGRKFDSP EGKKAIGVSP FKVASSPNGD AWVEIRGKGY SPPEVSAIVL
     MKMKQTAEDY LGEQVSEAVI TVPAYFNDSQ RQATKDAGRI AGLSVLRIIN EPTAAALAYG
     LDKVQDGGTE RIAVYDLGGG TFDISILELN AGVFEVKSTN GDTFLGGEDF DQRLIDYLAK
     RFAESNNGLD LRKDRMALQR LKEAAERAKH ELSSAPETEV NLPFITADAS GPKHLTETVD
     RATFEALVTD LIDRTIEPCR IALKDAGIPA QQINQVLLVG GMTRMPRVQQ KVKEFFGREP
     HKGINPDEVV AVGAAIQGGV LKGEVKDVLL LDVTPLSLGV ETAGGVFTKI IDKNTTIPCK
     KSQVFSTAVD NQPLVSVHVL QGEREMAADN KTLARFELVG IPPAPRGVPQ IEVSFDIDAN
     GIVHVSAKDL GTGKVQQVRV VSNSGLSEAE IQAMISDAQS HASDDKKKKE LAELRNNADG
     LIYTTEKSLE EYASLLSEKD REEIKADLER LKEVLNTSDA AVLKESFQRL EGSAYRIADA
     IYTGQAS