ID   DNAK_NEIMB              Reviewed;         642 AA.
AC   Q9K0N4;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 121.
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; OrderedLocusNames=NMB0554;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=NZ98/254 / Serogroup B;
RX   PubMed=16645985; DOI=10.1002/pmic.200500821;
RA   Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.;
RT   "Proteomic analysis of a meningococcal outer membrane vesicle vaccine
RT   prepared from the group B strain NZ98/254.";
RL   Proteomics 6:3400-3413(2006).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: Present in outer membrane vesicle formulations which are
CC       used as vaccines in human.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; AE002098; AAF40982.1; -; Genomic_DNA.
DR   PIR; H81185; H81185.
DR   RefSeq; NP_273598.1; NC_003112.2.
DR   RefSeq; WP_002225573.1; NC_003112.2.
DR   AlphaFoldDB; Q9K0N4; -.
DR   SMR; Q9K0N4; -.
DR   STRING; 122586.NMB0554; -.
DR   PaxDb; Q9K0N4; -.
DR   EnsemblBacteria; AAF40982; AAF40982; NMB0554.
DR   KEGG; nme:NMB0554; -.
DR   PATRIC; fig|122586.8.peg.709; -.
DR   HOGENOM; CLU_005965_2_1_4; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000000425; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0031240; C:external side of cell outer membrane; IDA:CAFA.
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:0002020; F:protease binding; IPI:CAFA.
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   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Stress response.
FT   CHAIN           1..642
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078503"
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:0000250"
SQ   SEQUENCE   642 AA;  68792 MW;  235696C763BD5805 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 EDLITRSIEP CKIALKDAGL STGDIDDVIL VGGQSRMPKV QEAVKAFFGK
     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