ID   DNAK_STRMK              Reviewed;         640 AA.
AC   B2FMY5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=Smlt1992;
OS   Stenotrophomonas maltophilia (strain K279a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=522373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K279a;
RX   PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA   Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA   Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA   Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA   Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA   Parkhill J., Thomson N.R., Avison M.B.;
RT   "The complete genome, comparative and functional analysis of
RT   Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT   resistance determinants.";
RL   Genome Biol. 9:R74.1-R74.13(2008).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM743169; CAQ45506.1; -; Genomic_DNA.
DR   RefSeq; WP_005409241.1; NC_010943.1.
DR   AlphaFoldDB; B2FMY5; -.
DR   SMR; B2FMY5; -.
DR   STRING; 522373.Smlt1992; -.
DR   PRIDE; B2FMY5; -.
DR   EnsemblBacteria; CAQ45506; CAQ45506; Smlt1992.
DR   KEGG; sml:Smlt1992; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_6; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000008840; 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..640
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119761"
FT   REGION          603..625
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         201
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   640 AA;  68469 MW;  00FF89AE33BE2F4F CRC64;
     MGKIIGIDLG TTNSCVAIMD GGKARVIENS EGDRTTPSIV AYTKDGEVLV GASAKRQAVT
     NPKNTFYAVK RLIGRKFTDA EVQKDIAHVP YSILAHDNGD AWVATSDGKK MAPQEISAKV
     LEKMKKTAED FLGEKVTEAV ITVPAYFNDS QRQATKDAGR IAGLDVKRII NEPTAAALAY
     GLDKGDNKDR KIVVYDLGGG TFDVSVIEIA NVDGEKQFEV LATNGDTFLG GEDFDNRVIE
     YLVEEFNKDQ GIDLRKDPLA LQRLKDAAER AKIELSSAQQ TEVNLPYVTA DASGPKHLNI
     KLTRAKLEAL VDDLIKKSIE PCRVALNDAG LRSSDISEVI LVGGQTRMPK VQQAVTEFFG
     KEPRKDVNPD EAVALGAAIQ GGVLGGDVKD VLLLDVTPLS LGIETMGGVF TKIIEKNTTI
     PTKASQVFST AEDNQSAVTV HVLQGEREQA RFNKSLAKFD LSGIEPAPRG LPQVEVSFDI
     DANGILHVSA KDKKTNKEQK VEIKAGSGLS EEEIARMVAD AEANREEDKK FQELVQARNQ
     ADALIHGTRS AITEHGSKVG GDVIGKVEAA LADLETAMKG DDKAQIEAKS KALEEAGQSL
     FAAASADQGG APGADAGNAG KAQDDVVDAE FTEVKDDKKS