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