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DNAK_MESFL
ID   DNAK_MESFL              Reviewed;         592 AA.
AC   Q6F149;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=Mfl415;
OS   Mesoplasma florum (strain ATCC 33453 / NBRC 100688 / NCTC 11704 / L1)
OS   (Acholeplasma florum).
OC   Bacteria; Tenericutes; Mollicutes; Entomoplasmatales; Entomoplasmataceae;
OC   Mesoplasma.
OX   NCBI_TaxID=265311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33453 / NBRC 100688 / NCTC 11704 / L1;
RA   Birren B.W., Stange-Thomann N., Hafez N., DeCaprio D., Fisher S.,
RA   Butler J., Elkins T., Kodira C.D., Major J., Wang S., Nicol R., Nusbaum C.;
RL   Submitted (JUN-2004) 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; AE017263; AAT75774.1; -; Genomic_DNA.
DR   RefSeq; WP_011183314.1; NC_006055.1.
DR   RefSeq; YP_053658.1; NC_006055.1.
DR   AlphaFoldDB; Q6F149; -.
DR   SMR; Q6F149; -.
DR   STRING; 265311.Mfl415; -.
DR   EnsemblBacteria; AAT75774; AAT75774; Mfl415.
DR   GeneID; 2898222; -.
DR   KEGG; mfl:Mfl415; -.
DR   PATRIC; fig|265311.5.peg.416; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_14; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000006647; 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; 2.
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.
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..592
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000225977"
FT   REGION          571..592
FT                   /note="Disordered"
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   592 AA;  64393 MW;  EEF00236C41C7D14 CRC64;
     MAKERIIGID LGTTNSVVSI MEGGQPIILE NPEGQRTTPS VVAFKNEDII VGGAAKRQAV
     TNPNVVISVK SKMGTNEKID INGKKYTPEQ ISAEILRYMK KYAEEKVGEK ITKAVITVPA
     YFNDSQRKAT KDAGKIAGLD VERIINEPTA AALAYGLEKK DKEEKVLVYD LGGGTFDVSI
     LELADGTFEV LSTSGDNKLG GDNFDTQIIN WLIEKIKTES GVDLKNDKMA LQRLKDEAEK
     AKINLSSQLE VEINLPFIAM NENGPVSFST QFSRTEFDKI TKDLVERTSK PVKDALQAAK
     LSASDIDEVL LVGGSTRIPA VQKIVKELLG KEPNRSINPD EVVAMGAAIQ GGVLAGDVTD
     VLLLDVTPLS LGIETMGGVM TKLIDRNTTI PTEKSQIFST AVDNQPAVDI NVLQGERPMA
     ADNKSLGQFQ LTGIKPAPKG TPQIEVTFKI DVNGIVSVIA KDKATNEEKS ITISNSGALS
     DADIEKMIKE AEANAEADEI KRKNIELKHK AESYVAIIES SLTQEGQEIP QEQKEQAEKM
     VAEVKELIEK EDYEALETKV NELEQMIQMA SQFAQAQTAQ PEEGNSDSEE NK
 
 
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