DNAK_NITMU
ID DNAK_NITMU Reviewed; 644 AA.
AC Q2Y6U0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=Nmul_A2239;
OS Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosospira.
OX NCBI_TaxID=323848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25196 / NCIMB 11849 / C 71;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC
RT 25196.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000103; ABB75531.1; -; Genomic_DNA.
DR RefSeq; WP_011381537.1; NZ_FNVK01000006.1.
DR AlphaFoldDB; Q2Y6U0; -.
DR SMR; Q2Y6U0; -.
DR STRING; 323848.Nmul_A2239; -.
DR PRIDE; Q2Y6U0; -.
DR EnsemblBacteria; ABB75531; ABB75531; Nmul_A2239.
DR KEGG; nmu:Nmul_A2239; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_4; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000002718; 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..644
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059618"
FT REGION 589..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..644
FT /note="Basic and acidic residues"
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 644 AA; 69779 MW; 67D5CC07757E2847 CRC64;
MGKIIGIDLG TTNSCVAVME SGKPKVIENS EGARTTPSIV AYTEDGEILV GASAKRQAVT
NPKNTLFAVK RLIGRRFNEE MVQRDIKMVP YTIIKADNND AWIEVRGKKV APPEVSAQVL
MKMKKTAEDY LGEPVTEAVI TVPAYFNDSQ RQATKDAGRI AGLEVKRIIN EPTAAALAFG
MDKKEGDRKI AVYDLGGGTF DISIIEIAEV EGEHQFEVLA TNGDTFLGGE DFDARIIEYL
VDEFKKENGI DLKKDMLALQ RLKDSAEKAK IELSSSQQTE VNLPYITADA SGPKHLAVRI
TRAKLESLVE DLITRTVEPC RIAIKDAGIK ISDIDDVILV GGQTRMPKVQ EKVKEIFAKE
PRKDVNPDEA VAVGAAIQGG VLQGAVKDVL LLDVTPLSLG IETLGGVMTK LIQKNTTIPT
KANQVFSTAD DNQTAVTIHV LQGEREMASG NKSLGQFNLA DIPPAPRGMP QIEVTFDIDS
NGILHVSAKD KATGKESKIK IQASSGLSEE EVQRMVKDAE AHAEEDHKAM ELVTARNQCD
AMIHSVQKTM KEHGDKLADE EKSKIESALK EAEDALKSGD KETIEAKTQA LAEASHKLAE
KMYSQGQGPQ AGPGEEPSGQ SGGTEKPVEG EVVDAEFEEV KNKK