ID   DNAK_NEIMF              Reviewed;         642 AA.
AC   A1KSG3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=NMC0495;
OS   Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM
OS   15464 / FAM18).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=272831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700532 / DSM 15464 / FAM18;
RX   PubMed=17305430; DOI=10.1371/journal.pgen.0030023;
RA   Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C.,
RA   Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K.,
RA   Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S.,
RA   Quail M.A., Achtman M., Barrell B.G., Saunders N.J., Parkhill J.;
RT   "Meningococcal genetic variation mechanisms viewed through comparative
RT   analysis of serogroup C strain FAM18.";
RL   PLoS Genet. 3:230-240(2007).
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; AM421808; CAM09793.1; -; Genomic_DNA.
DR   RefSeq; WP_002221371.1; NC_008767.1.
DR   AlphaFoldDB; A1KSG3; -.
DR   SMR; A1KSG3; -.
DR   PRIDE; A1KSG3; -.
DR   EnsemblBacteria; CAM09793; CAM09793; NMC0495.
DR   KEGG; nmc:NMC0495; -.
DR   HOGENOM; CLU_005965_2_1_4; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000002286; 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   Stress response.
FT   CHAIN           1..642
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059614"
FT   REGION          608..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        620..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;  68880 MW;  2153A2639A75A28D CRC64;
     MAKVIGIDLG TTNSCLAISE NGQTKVIENA EGARTTPSVI AYLDGGEILV GAPAKRQAVT
     NAKNTIYAAK RLIGHKFEDK EVQRDIESMP FEIIKANNGD AWVKAQGKEL SPPQISAEVL
     RKMKEAAEAY LGEKVTEAVI TVPAYFNDSQ RQATKDAGRI AGLDVKRIIN EPTAAALAFG
     MDKGDNKDRK VAVYDLGGGT FDISIIEIAN LDGDKQFEVL ATNGDTFLGG EDFDQRLIDH
     IIAEFKKEQG IDLKQDVMAL QRLKEAAEKA KIELSSGQQT EINLPYITMD ATGPKHLAMK
     ITRAKFESLV EDLIARSIEP CRTALKDAGL STSDIDDVIL VGGQSRMPKV QEAVRDFFGK
     EPRKDVNPDE AVAVGAAIQG EVLSGGRSDV LLLDVTPLSL GIETMGGVMT KLIQKNTTIP
     TKASQVFSTA EDNQSAVTIH VLQGERERAS ANKSLGQFNL GDIAPAPRGM PQIEVTFDID
     ANGILHVSAK DKGTGKAANI TIQGSSGLSE EEIERMVKDA EANAEEDKKL TELVASRNQA
     EALIHSVKKS LADYGDKLDA AEKEKIEAAL KEAEEAVKGD DKAAIDAKTE ALGAASQKLG
     EMVYAQAQAE AQAGESEQAN ASAKKDDDVV DADFEEVKDD KK