DNAK_UREPA
ID DNAK_UREPA Reviewed; 603 AA.
AC Q9PQF2;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Chaperone protein DnaK;
DE AltName: Full=HSP70;
DE AltName: Full=Heat shock 70 kDa protein;
DE AltName: Full=Heat shock protein 70;
GN Name=dnaK; OrderedLocusNames=UU339;
OS Ureaplasma parvum serovar 3 (strain ATCC 700970).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX NCBI_TaxID=273119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700970;
RX PubMed=11048724; DOI=10.1038/35037619;
RA Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y.,
RA Cassell G.H.;
RT "The complete sequence of the mucosal pathogen Ureaplasma urealyticum.";
RL Nature 407:757-762(2000).
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; AF222894; AAF30748.1; -; Genomic_DNA.
DR RefSeq; WP_006688469.1; NC_002162.1.
DR AlphaFoldDB; Q9PQF2; -.
DR SMR; Q9PQF2; -.
DR STRING; 273119.UU339; -.
DR EnsemblBacteria; AAF30748; AAF30748; UU339.
DR GeneID; 29672518; -.
DR KEGG; uur:UU339; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_14; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000000423; 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 Reference proteome; Stress response.
FT CHAIN 1..603
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000078580"
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:0000250"
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