ID   DNAK_XANP2              Reviewed;         631 AA.
AC   A7IC65;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=Xaut_0350;
OS   Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Xanthobacteraceae; Xanthobacter.
OX   NCBI_TaxID=78245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1158 / Py2;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA   Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Tapia R., Brainard J., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Ensigns S.A., Richardson P.;
RT   "Complete sequence of chromosome of Xanthobacter autotrophicus Py2.";
RL   Submitted (JUL-2007) 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; CP000781; ABS65608.1; -; Genomic_DNA.
DR   RefSeq; WP_011996008.1; NC_009720.1.
DR   AlphaFoldDB; A7IC65; -.
DR   SMR; A7IC65; -.
DR   STRING; 78245.Xaut_0350; -.
DR   PRIDE; A7IC65; -.
DR   EnsemblBacteria; ABS65608; ABS65608; Xaut_0350.
DR   KEGG; xau:Xaut_0350; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_5; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   PhylomeDB; A7IC65; -.
DR   Proteomes; UP000002417; 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..631
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119778"
FT   REGION          601..631
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        612..631
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   631 AA;  67616 MW;  05FCEADF1CD0E7D6 CRC64;
     MAKIIGIDLG TTNSCVAVME GSTPKVIENA EGARTTPSIV AFTEDGERLV GQPAKRQSVT
     NPERTFFAVK RLIGRRYDDP TVEKDKHLVP YSIVRADNGD AWVEADGKKY SPSQISAFVL
     QKMKETAESF LGEKVEKAVI TVPAYFNDAQ RQATKDAGRI AGLEVLRIIN EPTAAALAYG
     LDKKSAGTIA VYDLGGGTFD VSVLEIGDGV FEVKSTNGDT FLGGEDFDMR LVTYLADEFK
     KEQGIDLRND KLALQRLKEA AEKAKIELSS ATQTEINLPF ITADATGPKH LTLKLTRAKF
     EALVDDLIQR TVEPCRLALK DAGLTAGQID EVVLVGGMTR MPKVQEVVKQ FFGKEPHKGV
     NPDEVVAIGA AVQAGVLQGD VKDVLLLDVT PLSLGIETLG GVFTRLIDRN TTIPTKKSQT
     FSTAEDGQTA VTIRVFQGER EMAADNKMLG QFDLMGIPPA PRGVPQVEVT FDIDANGIVQ
     VSAKDKGTGK EQQIRIQASG GLNDADIEKM VKDAEAHAAE DKKRRALVEA KNHAEALVHS
     TEKAVAEHGD KVGAVEKGAI EAALADLKST LEGDDVEAIT AKTNTLAQAS LKLGEAMYAA
     QQPGAEGAAK PADDVVDAEF TEVDDDKKKS A