DNAK_WOLSU
ID DNAK_WOLSU Reviewed; 631 AA.
AC Q7MA35;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=WS0494;
OS Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC
OS 11488 / FDC 602W) (Vibrio succinogenes).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Wolinella.
OX NCBI_TaxID=273121;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC
RC 11488 / FDC 602W;
RX PubMed=14500908; DOI=10.1073/pnas.1932838100;
RA Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O.,
RA Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B.,
RA Meyer F., Lederer H., Schuster S.C.;
RT "Complete genome sequence and analysis of Wolinella succinogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003).
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; BX571658; CAE09632.1; -; Genomic_DNA.
DR RefSeq; WP_011138432.1; NC_005090.1.
DR AlphaFoldDB; Q7MA35; -.
DR SMR; Q7MA35; -.
DR STRING; 273121.WS0494; -.
DR PRIDE; Q7MA35; -.
DR EnsemblBacteria; CAE09632; CAE09632; WS0494.
DR KEGG; wsu:WS0494; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_7; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000000422; 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..631
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000078588"
FT REGION 600..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..631
FT /note="Basic and acidic residues"
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 631 AA; 68391 MW; 099732E0959E6306 CRC64;
MGKVLGIDLG TTNSAMAVFE GNEGKIIANK EGRNTTPSVV AFTDKGEILV GDPAKRQAIT
NPQKTIYSIK RIMGLMMSED KAKEAQKRLP YKVVDRNGAC AVEIADKVYT PQEISAKILM
KLKEDAEAYL GEEVSEAVIT VPAYFNDAQR KATKEAGTIA GLNVLRIINE PTSAALAYGL
DKKHAEKIVV YDLGGGTFDV TVLETGDNVV EVLATGGDAF LGGDDFDNRI IDWAAKEFEA
ENGIDLKKDV MALQRLKDAA ENAKKELSSA NETEINLPFI TADATGPKHL VKKISRAKFE
SLIDDLIEQT IQKIDFVIKD AGLAKSDIAE VVMVGGSTRI PKVQQRVKDF IGKELNKSVN
PDEVVALGAA IQGGVLKGDV KDVLLLDVTP LSLGIETLGG VMTKIIDRGT TIPVKKSQVF
STAEDNQPAV TIQVLQGERE LARDNKSLGM FELSGIPAAP RGVPQIEVTF DIDANGILTV
SAKDKATGKS QEIKITGSSG LSDSEIEKMV KDAELHKEED SKRKSMIEAK NQADSLLYQT
EKSLGEFKDQ LEESERTKIE SAINDLKETL KKENLTKEEI DEKVKALTEV SHKLAEAMYK
KENPQAADAQ QGNTANAGKK KDDDVIDAEV E