DNAK_CYTH3
ID DNAK_CYTH3 Reviewed; 632 AA.
AC Q11QH3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=CHU_3101;
OS Cytophaga hutchinsonii (strain ATCC 33406 / DSM 1761 / CIP 103989 / NBRC
OS 15051 / NCIMB 9469 / D465).
OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae;
OC Cytophaga.
OX NCBI_TaxID=269798;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33406 / DSM 1761 / CIP 103989 / NBRC 15051 / NCIMB 9469 / D465;
RX PubMed=17400776; DOI=10.1128/aem.00225-07;
RA Xie G., Bruce D.C., Challacombe J.F., Chertkov O., Detter J.C., Gilna P.,
RA Han C.S., Lucas S., Misra M., Myers G.L., Richardson P., Tapia R.,
RA Thayer N., Thompson L.S., Brettin T.S., Henrissat B., Wilson D.B.,
RA McBride M.J.;
RT "Genome sequence of the cellulolytic gliding bacterium Cytophaga
RT hutchinsonii.";
RL Appl. Environ. Microbiol. 73:3536-3546(2007).
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; CP000383; ABG60341.1; -; Genomic_DNA.
DR RefSeq; WP_011586450.1; NZ_FPJX01000017.1.
DR AlphaFoldDB; Q11QH3; -.
DR SMR; Q11QH3; -.
DR STRING; 269798.CHU_3101; -.
DR PRIDE; Q11QH3; -.
DR EnsemblBacteria; ABG60341; ABG60341; CHU_3101.
DR KEGG; chu:CHU_3101; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_10; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000001822; 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; 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..632
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059548"
FT REGION 595..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 632 AA; 68182 MW; 02E61516FDC6194C CRC64;
MGKIIGIDLG TTNSCVAVME GSEAVVIPNS EGKRTTPSIV AFLENGERKV GDPAKRQAIT
NPTNTISSIK RFMGKKFSES KSEADRATYK LEAGSNDTPR VRIADRQYTP QELSAMILQK
MKTTAEEYLG HEVKEAVITV PAYFNDAERQ ATKEAGQIAG LEVKRIINEP TAAALAYGMD
KKGKDMTVAV FDLGGGTFDV SVLELGDGVF EVKSTNGDVH LGGDNFDEVI IDWLAGEFKS
EEGLDLRQDP MALQRLKEAA EKAKIELSSS ASTEINLPYI MPVNGMPKHL VKTLTRAKFE
QLADSLIKRT LDPCKQALKD AGLSIGQIDE VILVGGSTRI PRIQEEVEKF FGKKPSKGVN
PDEVVALGAA IQGGVLTGEV TDVLLLDVIP LSLGIETMGG VFTKLIEANT TIPSKKSEVF
STASDNQPSV EIHVLQGERA FAKDNRSIGR FHLGDIPPAP RNVPQIEVTF DIDANGILNV
SAKDKGTGKE QKIRIEASSG LSADEIERMR NEAKANEGKD REEKEKIEKI NQADSMIFQT
EKQLKEFGDK LSAGNKSAIE ASLEDLKKAF EAKDISAIDT AMAAINTAWQ AASQEMYSAE
QGAGQPGADA GQSGPSDSVT DVEFEEVDGD KK