DNAK_DESAL
ID DNAK_DESAL Reviewed; 639 AA.
AC B8FGS3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=Dalk_3615;
OS Desulfatibacillum aliphaticivorans.
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulfatibacillum.
OX NCBI_TaxID=218208;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK-01;
RX PubMed=21651686; DOI=10.1111/j.1462-2920.2011.02516.x;
RA Callaghan A.V., Morris B.E., Pereira I.A., McInerney M.J., Austin R.N.,
RA Groves J.T., Kukor J.J., Suflita J.M., Young L.Y., Zylstra G.J., Wawrik B.;
RT "The genome sequence of Desulfatibacillum alkenivorans AK-01: a blueprint
RT for anaerobic alkane oxidation.";
RL Environ. Microbiol. 14:101-113(2012).
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; CP001322; ACL05303.1; -; Genomic_DNA.
DR RefSeq; WP_015948360.1; NC_011768.1.
DR AlphaFoldDB; B8FGS3; -.
DR SMR; B8FGS3; -.
DR PRIDE; B8FGS3; -.
DR EnsemblBacteria; ACL05303; ACL05303; Dalk_3615.
DR KEGG; dal:Dalk_3615; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_3_7; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000000739; 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..639
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000119697"
FT REGION 599..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 198
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 639 AA; 68026 MW; FD470020CACD5CE7 CRC64;
MGKVIGIDLG TTNSCVAVME GKEPKVLTNP DGGRTTPSIV GISSSGERLV GQIAKRQAIT
NPQNTVFAVK RLIGRKFASQ QVKDDMNVLP YQIVDGDNGD AYIELQGKKY SPQEISSFIL
AYIKKAAEEY LGETVTDAVI TVPAYFNDSQ RQATKDAGKI AGLNVLRIIN EPTAASLAYG
LDKKSDEKIA VFDLGGGTFD VSILEIGEGV FEVKSTNGDT HLGGEDFDLL VIDYLADEFK
KDQGIDLRSD KMALQRLKEA AEKAKMELST SVETEVNLPF ITADASGPKH LNVKLTRAKL
ESLVSDLLDK LEGPCVTALK DAGMSASEVD EVILVGGMTR MPAVQERVKK IFGKEPHKGV
NPDEVVAIGA GIQGGVLMGD VKDVLLLDVT PLSLGIETLG GVMTKLIEKN TTIPTKKSQV
FSTAADNQPA VSIHVLQGER EMATGNKTLG RFELVGIPPA PRGVPQIEVT FDIDANGIVS
VSAKDQGTGK EQSIKITASS GLTEEEIEQM VKDAELHAEE DKKKKELADA RNNADALVYA
TEKSLKDLGD KIDASTKENV EAAVEKLKKA LEGEDVEEIK RLSEELTTAS HKLAEAMYQQ
ASAEGQAGAA GDPGAGQGAA GGAAPDDDVV DADFEEVKD