DNAK_MYCBP
ID DNAK_MYCBP Reviewed; 625 AA.
AC A1KFH2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=BCG_0389;
OS Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=410289;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCG / Pasteur 1173P2;
RX PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA Barrell B.G., Parkhill J., Cole S.T.;
RT "Genome plasticity of BCG and impact on vaccine efficacy.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
RN [2]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH HUMAN
RP CD209.
RC STRAIN=BCG / Pasteur 1173P2;
RX PubMed=21203928; DOI=10.1007/s13238-010-0101-3;
RA Carroll M.V., Sim R.B., Bigi F., Jaekel A., Antrobus R., Mitchell D.A.;
RT "Identification of four novel DC-SIGN ligands on Mycobacterium bovis BCG.";
RL Protein Cell 1:859-870(2010).
RN [3]
RP SUBCELLULAR LOCATION.
RC STRAIN=BCG / Pasteur 1173P2;
RX PubMed=21364279; DOI=10.1172/jci44261;
RA Prados-Rosales R., Baena A., Martinez L.R., Luque-Garcia J., Kalscheuer R.,
RA Veeraraghavan U., Camara C., Nosanchuk J.D., Besra G.S., Chen B.,
RA Jimenez J., Glatman-Freedman A., Jacobs W.R. Jr., Porcelli S.A.,
RA Casadevall A.;
RT "Mycobacteria release active membrane vesicles that modulate immune
RT responses in a TLR2-dependent manner in mice.";
RL J. Clin. Invest. 121:1471-1483(2011).
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000255|HAMAP-Rule:MF_00332}.
CC -!- FUNCTION: In vitro binds to human CD209 (DC-SIGN) and may help mediate
CC adherence to host cells (PubMed:21203928).
CC {ECO:0000269|PubMed:21203928}.
CC -!- SUBUNIT: Able to bind to host (human) CD209 in vitro (PubMed:21203928).
CC {ECO:0000269|PubMed:21203928}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Extracellular vesicle,
CC bacterial extracellular vesicle {ECO:0000269|PubMed:21364279}.
CC Note=Also present in extracytoplasmic vesicles (PubMed:21364279).
CC Although thought of as a cytoplasmic chaperone this protein is
CC routinely found extracellularly in the absence of cell lysis
CC (PubMed:21364279) (By similarity). {ECO:0000250|UniProtKB:P9WMJ9,
CC ECO:0000269|PubMed:21364279}.
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; AM408590; CAL70374.1; -; Genomic_DNA.
DR RefSeq; WP_003401814.1; NC_008769.1.
DR AlphaFoldDB; A1KFH2; -.
DR SMR; A1KFH2; -.
DR PRIDE; A1KFH2; -.
DR GeneID; 45424316; -.
DR KEGG; mbb:BCG_0389; -.
DR HOGENOM; CLU_005965_2_3_11; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000001472; Chromosome.
DR GO; GO:0097691; C:bacterial extracellular vesicle; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 2.
DR Pfam; PF00012; HSP70; 2.
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 1: Evidence at protein level;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Phosphoprotein;
KW Stress response.
FT CHAIN 1..625
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059606"
FT REGION 586..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 175
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 625 AA; 66831 MW; 23935906094D1A91 CRC64;
MARAVGIDLG TTNSVVSVLE GGDPVVVANS EGSRTTPSIV AFARNGEVLV GQPAKNQAVT
NVDRTVRSVK RHMGSDWSIE IDGKKYTAPE ISARILMKLK RDAEAYLGED ITDAVITTPA
YFNDAQRQAT KDAGQIAGLN VLRIVNEPTA AALAYGLDKG EKEQRILVFD LGGGTFDVSL
LEIGEGVVEV RATSGDNHLG GDDWDQRVVD WLVDKFKGTS GIDLTKDKMA MQRLREAAEK
AKIELSSSQS TSINLPYITV DADKNPLFLD EQLTRAEFQR ITQDLLDRTR KPFQSVIADT
GISVSEIDHV VLVGGSTRMP AVTDLVKELT GGKEPNKGVN PDEVVAVGAA LQAGVLKGEV
KDVLLLDVTP LSLGIETKGG VMTRLIERNT TIPTKRSETF TTADDNQPSV QIQVYQGERE
IAAHNKLLGS FELTGIPPAP RGIPQIEVTF DIDANGIVHV TAKDKGTGKE NTIRIQEGSG
LSKEDIDRMI KDAEAHAEED RKRREEADVR NQAETLVYQT EKFVKEQREA EGGSKVPEDT
LNKVDAAVAE AKAALGGSDI SAIKSAMEKL GQESQALGQA IYEAAQAASQ ATGAAHPGGE
PGGAHPGSAD DVVDAEVVDD GREAK
