ID DNAK_MYCGE Reviewed; 595 AA. AC P47547; Q49321; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 27-MAR-2024, entry version 143. 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; Synonyms=hsp70; OrderedLocusNames=MG305; OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37) OS (Mycoplasmoides genitalium). OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae; OC Mycoplasmoides. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 353-460. RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37; RX PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L43967; AAC71527.1; -; Genomic_DNA. DR EMBL; U02204; AAD12493.1; -; Genomic_DNA. DR PIR; G64233; G64233. DR RefSeq; WP_009885883.1; NZ_AAGX01000008.1. DR PDB; 5OBU; X-ray; 2.00 A; A=1-521. DR PDB; 5OBV; X-ray; 2.49 A; A=1-521. DR PDB; 5OBW; X-ray; 1.40 A; A=1-366. DR PDB; 5OBX; X-ray; 1.78 A; A=1-366. DR PDB; 5OBY; X-ray; 1.30 A; A=1-366. DR PDBsum; 5OBU; -. DR PDBsum; 5OBV; -. DR PDBsum; 5OBW; -. DR PDBsum; 5OBX; -. DR PDBsum; 5OBY; -. DR AlphaFoldDB; P47547; -. DR SMR; P47547; -. DR STRING; 243273.MG_305; -. DR KEGG; mge:MG_305; -. DR eggNOG; COG0443; Bacteria. DR HOGENOM; CLU_005965_2_1_14; -. DR InParanoid; P47547; -. DR OrthoDB; 9766019at2; -. DR BioCyc; MGEN243273:G1GJ2-374-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central. DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro. DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central. DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central. DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro. DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central. DR GO; GO:0042026; P:protein refolding; IBA:GO_Central. DR CDD; cd10234; HSPA9-Ssq1-like_NBD; 1. DR Gene3D; 3.30.420.40; -; 2. 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 NCBIfam; TIGR02350; prok_dnaK; 1. DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1. DR PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1. DR Pfam; PF00012; HSP70; 1. DR PRINTS; PR00301; HEATSHOCK70. DR SUPFAM; SSF53067; Actin-like ATPase domain; 2. DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1. DR PROSITE; PS00297; HSP70_1; 1. DR PROSITE; PS00329; HSP70_2; 1. DR PROSITE; PS01036; HSP70_3; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Stress response. FT CHAIN 1..595 FT /note="Chaperone protein DnaK" FT /id="PRO_0000078490" FT MOD_RES 182 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0000250" FT CONFLICT 447..460 FT /note="PKGKPQIEITFSLD -> LKVNPKLRLPLVWM (in Ref. 2)" FT /evidence="ECO:0000305" FT STRAND 9..13 FT /evidence="ECO:0007829|PDB:5OBY" FT STRAND 15..24 FT /evidence="ECO:0007829|PDB:5OBY" FT STRAND 27..30 FT /evidence="ECO:0007829|PDB:5OBY" FT STRAND 38..42 FT /evidence="ECO:0007829|PDB:5OBY" FT STRAND 44..47 FT /evidence="ECO:0007829|PDB:5OBY" FT STRAND 50..54 FT /evidence="ECO:0007829|PDB:5OBY" FT HELIX 55..58 FT /evidence="ECO:0007829|PDB:5OBY" FT TURN 59..63 FT /evidence="ECO:0007829|PDB:5OBY" FT STRAND 67..69 FT /evidence="ECO:0007829|PDB:5OBX" FT HELIX 71..74 FT /evidence="ECO:0007829|PDB:5OBY" FT STRAND 81..84 FT /evidence="ECO:0007829|PDB:5OBY" FT STRAND 90..93 FT /evidence="ECO:0007829|PDB:5OBY" FT HELIX 95..114 FT /evidence="ECO:0007829|PDB:5OBY" FT STRAND 120..125 FT /evidence="ECO:0007829|PDB:5OBY" FT HELIX 131..143 FT /evidence="ECO:0007829|PDB:5OBY" FT STRAND 147..153 FT /evidence="ECO:0007829|PDB:5OBY" FT HELIX 154..161 FT /evidence="ECO:0007829|PDB:5OBY" FT HELIX 164..166 FT /evidence="ECO:0007829|PDB:5OBY" FT STRAND 167..169 FT /evidence="ECO:0007829|PDB:5OBU" FT STRAND 171..178 FT /evidence="ECO:0007829|PDB:5OBY" FT STRAND 183..191 FT /evidence="ECO:0007829|PDB:5OBY" FT STRAND 194..203 FT /evidence="ECO:0007829|PDB:5OBY" FT HELIX 208..226 FT /evidence="ECO:0007829|PDB:5OBY" FT TURN 227..229 FT /evidence="ECO:0007829|PDB:5OBX" FT HELIX 232..234 FT /evidence="ECO:0007829|PDB:5OBY" FT HELIX 236..255 FT /evidence="ECO:0007829|PDB:5OBY" FT STRAND 256..269 FT /evidence="ECO:0007829|PDB:5OBY" FT STRAND 272..281 FT /evidence="ECO:0007829|PDB:5OBY" FT HELIX 282..288 FT /evidence="ECO:0007829|PDB:5OBY" FT HELIX 290..295 FT /evidence="ECO:0007829|PDB:5OBY" FT HELIX 297..307 FT /evidence="ECO:0007829|PDB:5OBY" FT HELIX 311..313 FT /evidence="ECO:0007829|PDB:5OBY" FT STRAND 316..321 FT /evidence="ECO:0007829|PDB:5OBY" FT HELIX 322..325 FT /evidence="ECO:0007829|PDB:5OBY" FT HELIX 327..336 FT /evidence="ECO:0007829|PDB:5OBY" FT TURN 348..350 FT /evidence="ECO:0007829|PDB:5OBY" FT HELIX 351..364 FT /evidence="ECO:0007829|PDB:5OBY" FT STRAND 380..384 FT /evidence="ECO:0007829|PDB:5OBU" FT TURN 385..387 FT /evidence="ECO:0007829|PDB:5OBU" FT STRAND 388..393 FT /evidence="ECO:0007829|PDB:5OBU" FT STRAND 398..411 FT /evidence="ECO:0007829|PDB:5OBU" FT STRAND 417..425 FT /evidence="ECO:0007829|PDB:5OBU" FT HELIX 429..431 FT /evidence="ECO:0007829|PDB:5OBU" FT STRAND 432..440 FT /evidence="ECO:0007829|PDB:5OBU" FT STRAND 453..459 FT /evidence="ECO:0007829|PDB:5OBU" FT STRAND 465..471 FT /evidence="ECO:0007829|PDB:5OBU" FT TURN 472..474 FT /evidence="ECO:0007829|PDB:5OBU" FT STRAND 477..482 FT /evidence="ECO:0007829|PDB:5OBU" FT HELIX 490..502 FT /evidence="ECO:0007829|PDB:5OBU" FT HELIX 504..511 FT /evidence="ECO:0007829|PDB:5OBU" SQ SEQUENCE 595 AA; 65051 MW; 8EB48D058A009FB7 CRC64; MSADNGLIIG IDLGTTNSCV SVMEGGRPVV LENPEGKRTT PSIVSYKNNE IIVGDAAKRQ MVTNPNTIVS IKRLMGTSNK VKVQNADGTT KELSPEQVSA QILSYLKDFA EKKIGKKISR AVITVPAYFN DAERNATKTA GKIAGLNVER IINEPTAAAL AYGIDKASRE MKVLVYDLGG GTFDVSLLDI AEGTFEVLAT AGDNRLGGDD WDNKIIEYIS AYIAKEHQGL NLSKDKMAMQ RLKEAAERAK IELSAQLETI ISLPFLTVTQ KGPVNVELKL TRAKFEELTK PLLERTRNPI SDVIKEAKIK PEEINEILLV GGSTRMPAVQ KLVESMVPGK KPNRSINPDE VVAIGAAIQG GVLRGDVKDV LLLDVTPLTL SIETLGGVAT PLIKRNTTIP VSKSQIFSTA QDNQESVDVV VCQGERPMSR DNKSLGRFNL GGIQPAPKGK PQIEITFSLD ANGILNVKAK DLTTQKENSI TISDNGNLSE EEIQKMIRDA EANKERDNII RERIELRNEG EGIVNTIKEI LASPDAKNFP KEEKEKLEKL TGNIDAAIKA NDYAKLKVEI ENFKKWREEM AKKYNPTGEQ GPQAK //