DNAK_UREU1
ID DNAK_UREU1 Reviewed; 600 AA.
AC B5ZBE9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=UUR10_0346;
OS Ureaplasma urealyticum serovar 10 (strain ATCC 33699 / Western).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX NCBI_TaxID=565575;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33699 / Western;
RA Shrivastava S., Methe B.A., Glass J., White K., Duffy L.B.;
RT "Genome sequence of Ureaplasma urealyticum serovar 10 ATCC-33699.";
RL Submitted (OCT-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; CP001184; ACI60208.1; -; Genomic_DNA.
DR RefSeq; WP_012560313.1; NC_011374.1.
DR AlphaFoldDB; B5ZBE9; -.
DR SMR; B5ZBE9; -.
DR STRING; 565575.UUR10_0346; -.
DR PRIDE; B5ZBE9; -.
DR EnsemblBacteria; ACI60208; ACI60208; UUR10_0346.
DR GeneID; 45015893; -.
DR KEGG; uue:UUR10_0346; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_14; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000002018; 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..600
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000119773"
FT REGION 572..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..588
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 600 AA; 65646 MW; C5A58662BCD947B7 CRC64;
MTKEIILGID LGTTNSCVAV IENKKPIVLE NPEGKRTVPS VVSFNGDEVL VGDAAKRKQI
TNPNTVSSIK RLMGTKEKVT ILNKEYTPEE ISAKILSYIK DYAEKKLGTK INKAVITVPA
YFDDAQRQAT KNAGIIAGLT VERIINEPTA AALAYGIDKL DKEQKILVFD LGGGTFDVSV
LDMADGTFEV LSTSGDNHLG GDDWDQVIIN WLLKSIADEF NIDLSKNKMA MQRLKDAAEK
AKIELSGVNT TTISLPFIAM DSSGQPINFE KELNRATFDN LTKNLIERLK KPVLDAMKES
KLSLADIDQV LMVGGSTRMP AVQNLVKELT GKEPNHSLNP DEVVAIGAAI QGGVLAGEID
DILLLDVTPL TLSIETMGGV ATPLIPRNTK IPVSKSQVFS TAADNQPSVD IRIVQGERSL
AADNKLLGNF ELSGIEPAPR GVPQIEIKFN IDANGIMSVN AKDLKTQKET SITIKDSQGL
SQEEIDKMIK EAEENKEKDA KVKHERELVN RADSLINQLE QVVKTENVPQ EQKDAFNKQI
EELTNARDAQ DYTKLEAEVK KVEDLLANAA KFAQQTQQQD PNNQKDDVTE ATVTDDSTKK