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DNAK_NEIG1
ID   DNAK_NEIG1              Reviewed;         642 AA.
AC   Q5F6W5;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=NGO1429;
OS   Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=242231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700825 / FA 1090;
RA   Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA   Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA   Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA   Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT   "The complete genome sequence of Neisseria gonorrhoeae.";
RL   Submitted (MAR-2003) 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; AE004969; AAW90072.1; -; Genomic_DNA.
DR   RefSeq; WP_003689283.1; NC_002946.2.
DR   RefSeq; YP_208484.1; NC_002946.2.
DR   AlphaFoldDB; Q5F6W5; -.
DR   SMR; Q5F6W5; -.
DR   STRING; 242231.NGO_1429; -.
DR   EnsemblBacteria; AAW90072; AAW90072; NGO_1429.
DR   KEGG; ngo:NGO_1429; -.
DR   PATRIC; fig|242231.10.peg.1687; -.
DR   HOGENOM; CLU_005965_2_1_4; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000000535; 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; 1.
DR   Pfam; PF00012; HSP70; 1.
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..642
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000225984"
FT   REGION          609..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        621..642
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         200
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   642 AA;  68863 MW;  6BC051EC0E5334CB CRC64;
     MAKVIGIDLG TTNSCLAISE NGQTKVIENA EGARTTPSII AYLDGGEILV GAPAKRQAVT
     NAKNTIYAAK RLIGHKFEDK EVQRDIESMP FEIIKADNGD AWVKAQGKEL SPPQISAEVL
     RKMKEAAEAY LGEKVTEAVI TVPAYFNDSQ RQATKDAGRI AGLDVKRIIN EPTAAALAFG
     MDKGDNKDRK IAVYDLGGGT FDISIIEIAN LDGDKQFEVL ATNGDTFLGG EDFDQRLIDY
     IIDEFKKEQG IDLKQDVMAL QRLKEAAEKA KIELSSGQQT EINLPYITMD ATGPKHLAMK
     ITRAKFESLV EDLIARSIEP CRTALKDAGL STGDIDDVIL VGGQSRMPKV QEAVKDFFGK
     EPRKDVNPDE AVAVGAAIQG EVLSGGRSDV LLLDVTPLSL GIETMGGVMT KLIQKNTTIP
     TKASQVFSTA EDNQSAVTIH VLQGERERAS ANKSLGQFNL GDIAPAPRGM PQIEVTFDID
     ANGILHVSAK DKGTGKAANI TIQGSSGLSE EEIERMVKDA EANAEEDKKL TELVASRNQA
     EALIHSVKKS LADYGDKLDA AEKEKIEAAL KEAEEAVKGD DKTAIDAKAE ALGTASQKLG
     EMVYAQAQAE AQAGEGAQAN ASAKKDDDVV DADFEEVKDD KK
 
 
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