ID   DNAK_UREP2              Reviewed;         603 AA.
AC   B1AIX8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, 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=UPA3_0355;
OS   Ureaplasma parvum serovar 3 (strain ATCC 27815 / 27 / NCTC 11736).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX   NCBI_TaxID=505682;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27815 / 27 / NCTC 11736;
RA   Methe B.A., Glass J., Waites K., Shrivastava S.;
RT   "Genome sequence of Ureaplasma parvum serovar 3.";
RL   Submitted (FEB-2008) 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; CP000942; ACA32773.1; -; Genomic_DNA.
DR   RefSeq; WP_006688469.1; NC_010503.1.
DR   AlphaFoldDB; B1AIX8; -.
DR   SMR; B1AIX8; -.
DR   PRIDE; B1AIX8; -.
DR   EnsemblBacteria; ACA32773; ACA32773; UPA3_0355.
DR   GeneID; 29672518; -.
DR   KEGG; upa:UPA3_0355; -.
DR   HOGENOM; CLU_005965_2_4_14; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000002162; 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; 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; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375; PTHR19375; 2.
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.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW   Stress response.
FT   CHAIN           1..603
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000079253"
FT   REGION          573..603
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        573..591
FT                   /note="Polar 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   603 AA;  65956 MW;  770750529F44CC04 CRC64;
     MAKEIILGID LGTTNSCVAV IENKKPIVLE NPEGKRTVPS VVSFNGDEVL VGDAAKRKQI
     TNPNTISSIK RLMGTKEKVT VLNKDYTPEE ISAKILTYIK EYAEKKIGAK VNKAVITVPA
     YFDDAQRQAT KNAGIIAGLS VERIINEPTA AALAYGIDKL DKEQKILVFD LGGGTFDVSV
     LDMADGTFEV LSTSGDNHLG GDDWDQVIIN WLLKSIADEF NIDLSKNKMA MQRLKDAAEK
     AKIELSGINT TTISLPFIAM DSSGQPINFE KELNRATFDN LTKNLIERLK KPVLDAMKES
     KLSLVDIDQV LMVGGSTRMP AVQNLVKELT GKEPNHSLNP DEVVAIGAAI QGGVLAGEID
     DILLLDVTPL TLSIETMGGV ATPLIPRNTK IPVSKSQIFS TAADNQPSVD IRIVQGERSL
     AADNKLLGNF ELSGIEPAPR GVPQIEIKFN IDANGIMSVN AKDLKTQKET SITIKDSQGL
     SQDEIDKMIK EAEENKEKDA KVKHERELVN RADSLINQLE QVSKTENVPQ EQKDVFNKQI
     EDLTNARDAQ DYVKLEAEVK KVEDLLTNAA KFAQQAQQQN PDNQNNNKDD VTEATVTDDS
     TKK