DNAK_MYCMO
ID DNAK_MYCMO Reviewed; 601 AA.
AC Q6KIH7;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=MMOB1130;
OS Mycoplasma mobile (strain ATCC 43663 / 163K / NCTC 11711) (Mesomycoplasma
OS mobile).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mesomycoplasma.
OX NCBI_TaxID=267748;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43663 / 163K / NCTC 11711;
RX PubMed=15289470; DOI=10.1101/gr.2674004;
RA Jaffe J.D., Stange-Thomann N., Smith C., DeCaprio D., Fisher S., Butler J.,
RA Calvo S., Elkins T., FitzGerald M.G., Hafez N., Kodira C.D., Major J.,
RA Wang S., Wilkinson J., Nicol R., Nusbaum C., Birren B., Berg H.C.,
RA Church G.M.;
RT "The complete genome and proteome of Mycoplasma mobile.";
RL Genome Res. 14:1447-1461(2004).
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; AE017308; AAT27599.1; -; Genomic_DNA.
DR RefSeq; WP_011264633.1; NC_006908.1.
DR AlphaFoldDB; Q6KIH7; -.
DR SMR; Q6KIH7; -.
DR STRING; 267748.MMOB1130; -.
DR EnsemblBacteria; AAT27599; AAT27599; MMOB1130.
DR KEGG; mmo:MMOB1130; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_14; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000009072; 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..601
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000225981"
FT REGION 570..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..601
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 601 AA; 66110 MW; 775AEDA73A941B78 CRC64;
MAKEKIIGID LGTTNSVVAI LEDKTPRVLE NPNGKRTTPS VVSFKNDDII VGEVAKRQLE
TNINTIASIK RKMGTSETVK INDKEYKPEE ISAMILSYLK DYAEKKIGSK IKKAVITVPA
YFNNAQREAT KTAGRIAGLS VERIINEPTA AALAFGLDKT DKEQKILVYD LGGGTFDVSV
LELANGTFEV LSTSGDNFLG GDDWDNEIVK WLIGKIKLEH KYDVSKDKMA MARLKEEAEK
AKINLSTTST TSINLPFLAV TDSGPINVEV ELKRSDFEKM TQHLVERTRK PVRDALKEAK
LKSEDLHEVL LVGGSTRIPA VQEMLQHELN KKPNHSINPD EVVAIGAAIQ GAVLSGDIND
VLLLDVTPLT LGIETQGGIA TPLIQRNTTI PTTKSQIFST AADNQSEVTI NVVQGERQMA
ADNKSLGQFN LGGIEKAPRG TPQIEVSFSI DVNGIIKVSA TDKKTNKIQT ITIENSTSLT
EEEIKKMIDD AEKNKEADAK KKEKIDVTVR AETLINQLEK TIKDQGDKID PKEKEQTEKE
ITNIKDLILQ DKIDELKIKL DQIEEVAKAF AQKAASKETS KNEQNEDGSI DAEIKEEDPK
A