ID   DNAK_KOCRD              Reviewed;         623 AA.
AC   B2GGP0;
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=KRH_03980;
OS   Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Kocuria.
OX   NCBI_TaxID=378753;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9341 / DSM 348 / NBRC 103217 / DC2201;
RX   PubMed=18408034; DOI=10.1128/jb.01853-07;
RA   Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S.,
RA   Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Complete genome sequence of the soil actinomycete Kocuria rhizophila.";
RL   J. Bacteriol. 190:4139-4146(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}.
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DR   EMBL; AP009152; BAG28745.1; -; Genomic_DNA.
DR   RefSeq; WP_012397472.1; NC_010617.1.
DR   AlphaFoldDB; B2GGP0; -.
DR   SMR; B2GGP0; -.
DR   STRING; 378753.KRH_03980; -.
DR   PRIDE; B2GGP0; -.
DR   EnsemblBacteria; BAG28745; BAG28745; KRH_03980.
DR   KEGG; krh:KRH_03980; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_11; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000008838; 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; 2.
DR   Pfam; PF00012; HSP70; 2.
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..623
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119716"
FT   REGION          497..521
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          585..623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..514
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         175
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   623 AA;  66363 MW;  470C16F3235BA7F2 CRC64;
     MSRAVGIDLG TTNSVVAVLE GGEPVVIANA EGNRTTPSVV AFSKDGETLV GDVAKRQAVT
     NVDRTVASVK RHMGTDWTTE IDGKKYTPQE ISARTLMKLK ADAESYLGDT VTDAVITVPA
     YFNDAERQAT KEAGEIAGMN VLRIVNEPTA AALAYGLEKG KEDELILVFD LGGGTFDVSL
     LEVGKDEDDF STIQVRATAG DNRLGGDDWD QRIVDWLLEQ VKSKTGADLS KDKIALQRLK
     EAAEQAKKEL SSATSTTISL QYLSVTPEGP VHLDEKLSRA KFEDLTKDLL ARTEKPFKDV
     ISEAGINVSD IDHVVLVGGS TRMPAVVEKV TELAGKAPNK GVNPDEVVAI GAAIQAGVLK
     GDRKDVLLID VTPLSLGIET KGGVMTKLIE RNTAIPTKRS ETFTTAEDNQ PSVSIQVFQG
     EREFTRDNKN LGTFELTGIA PAPRGMPQIE VTFDIDANGI VHVSAKDKGT GKEQSMTITG
     GTSLSKEDID RMVKDAEANA DADKQRREAA DRRNNAEQTA YSVEKLIKDD EGAIPEDVKS
     EVQADVDAVK AALEGDDDDA VKTAFEKLQS SQTKIGEALY AQSQAEGAAG AGAGAAGAEG
     AQAKEDDDIV DAEVVDDDND GKK