DNAK_NITOC
ID DNAK_NITOC Reviewed; 640 AA.
AC Q3J7D8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=Noc_2811;
OS Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB
OS 11848 / C-107).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Nitrosococcus.
OX NCBI_TaxID=323261;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB 11848 / C-107;
RX PubMed=16957257; DOI=10.1128/aem.00463-06;
RA Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J.,
RA Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., Poret-Peterson A.T.,
RA Vergez L.M., Ward B.B.;
RT "Complete genome sequence of the marine, chemolithoautotrophic, ammonia-
RT oxidizing bacterium Nitrosococcus oceani ATCC 19707.";
RL Appl. Environ. Microbiol. 72:6299-6315(2006).
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; CP000127; ABA59258.1; -; Genomic_DNA.
DR RefSeq; WP_002811989.1; NC_007484.1.
DR AlphaFoldDB; Q3J7D8; -.
DR SMR; Q3J7D8; -.
DR STRING; 323261.Noc_2811; -.
DR PRIDE; Q3J7D8; -.
DR EnsemblBacteria; ABA59258; ABA59258; Noc_2811.
DR KEGG; noc:Noc_2811; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000006838; 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..640
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000225986"
FT REGION 603..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 199
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 640 AA; 69953 MW; 6CCFEAAAAD0E74B2 CRC64;
MGKIIGIDLG TTNSCVALME GNKPRVIENA EGDRTTPSVV AFTKEGETLV GQSAKRQAIT
NPQNTLYAIK RLIGRRFDEE VVQRDIKMVP YKIVKADNGD AWVEATGKKM APPEVSANVL
RKMKKTAEDY LGEEVEAAVI TVPAYFNDSQ RQATKDAGRI AGLEVKRIIN EPTAAALAYG
LDKKRGDQKI AVYDLGGGTF DVSIIEIAEV EGEHQFEVLS TNGDTFLGGE DFDKRIIDYI
AEEFKKEQSI DLRGDPLAMQ RLKDAAEKAK IELSSSQQTE VNLPYVTADA SGPKHLNVRI
TRAKLESLVE DLINRTIGPC KTALQDAKLS ASDIDEVILV GGQTRMPKVQ EAAKEFFGKE
PRKDVNPDEA VAVGAAIQAG VLGGEVKEVL LLDVTPLSLG IETLGGVMTK LIEKNTTIPT
RKTQVFSTAE DNQTAVTVHV LQGEREQAVG NKSLGRFDLV GIPPAHRGMP QIEVTFDIDA
NGILNVSAKD KATGKEQSIV IKASSGLAEG EIERMVSDAE AHVEEDRKFR ELVDLRNQGD
NLIHATEKSM EELGDKLEAN EKSEIEKTIG ELKTAMKEDN KEVIEARIKD LTDASAKMAE
RLYTQQAEEP QPQKEEGKAA EEDVVDAEFE EVKEDKNKAS