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DNAK_NEIM0
ID   DNAK_NEIM0              Reviewed;         642 AA.
AC   A9M296;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=NMCC_0500;
OS   Neisseria meningitidis serogroup C (strain 053442).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=374833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=053442;
RX   PubMed=18031983; DOI=10.1016/j.ygeno.2007.10.004;
RA   Peng J., Yang L., Yang F., Yang J., Yan Y., Nie H., Zhang X., Xiong Z.,
RA   Jiang Y., Cheng F., Xu X., Chen S., Sun L., Li W., Shen Y., Shao Z.,
RA   Liang X., Xu J., Jin Q.;
RT   "Characterization of ST-4821 complex, a unique Neisseria meningitidis
RT   clone.";
RL   Genomics 91:78-87(2008).
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; CP000381; ABX72700.1; -; Genomic_DNA.
DR   RefSeq; WP_002243335.1; NC_010120.1.
DR   AlphaFoldDB; A9M296; -.
DR   SMR; A9M296; -.
DR   MoonProt; A9M296; -.
DR   EnsemblBacteria; ABX72700; ABX72700; NMCC_0500.
DR   KEGG; nmn:NMCC_0500; -.
DR   HOGENOM; CLU_005965_2_1_4; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000001177; 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_1000079234"
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;  68878 MW;  0C1C1574F383E192 CRC64;
     MAKVIGIDLG TTNSCLAISE NGQTKVIENA EGARTTPSVI AYLDGGEILV GAPAKRQAVT
     NAKNTIYAAK RLIGHKFEDK EVQRDIESMP FEIIKANNGD AWVKAQGKEL SPPQISAEVL
     RKMKEAAEAY LGEKVTEAVI TVPAYFNDSQ RQATKDAGRI AGLDVKRIIN EPTAAALAFG
     MDKGDNKDRK VAVYDLGGGT FDISIIEIAN LDGDKQFEVL ATNGDTFLGG EDFDQRLIDY
     IIDEFKKEQG IDLKQDVMAL QRLKEAAEKA KIELSSGQQT EINLPYITMD ATGPKHLAMK
     ITRAKFESLV EDLIARSIEP CRTALKDAGL 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 DKTAIDAKAE ALGTASQKLG
     EMVYAQAQAE AQAGESEQAN ASAKKDDDVV DADFEEVKDD KK
 
 
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