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Chaperone protein DnaK (HSP70) (Heat shock 70 kDa protein) (Heat shock protein 70)

 DNAK_MYCTU              Reviewed;         625 AA.
P9WMJ9; I6QM76; O06301; P0A5B9; P32723;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
12-SEP-2018, entry version 26.
RecName: Full=Chaperone protein DnaK;
AltName: Full=HSP70;
AltName: Full=Heat shock 70 kDa protein;
AltName: Full=Heat shock protein 70;
Name=dnaK; OrderedLocusNames=Rv0350; ORFNames=MTCY13E10.10;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 35801 / TMC 107 / Erdman;
Lathigra R., Alexander B., Stover C.K., Coadwell J., Young R.A.,
Young D.B.;
Submitted (FEB-1991) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=MTCC300;
Dhakal J., Agrawal R.K., Brah G.S., Ramneek V., Pawar H.N., Kaur D.,
Minhas P., Mothwal U., Saini N., Mahajan K.;
Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[4]
INDUCTION BY SIGH.
STRAIN=ATCC 25618 / H37Rv;
PubMed=11567012; DOI=10.1128/JB.183.20.6119-6125.2001;
Raman S., Song T., Puyang X., Bardarov S., Jacobs W.R. Jr.,
Husson R.N.;
"The alternative sigma factor SigH regulates major components of
oxidative and heat stress responses in Mycobacterium tuberculosis.";
J. Bacteriol. 183:6119-6125(2001).
[5]
FUNCTION IN INFECTION.
PubMed=15809303; DOI=10.1074/jbc.M411379200;
Bulut Y., Michelsen K.S., Hayrapetian L., Naiki Y., Spallek R.,
Singh M., Arditi M.;
"Mycobacterium tuberculosis heat shock proteins use diverse Toll-like
receptor pathways to activate pro-inflammatory signals.";
J. Biol. Chem. 280:20961-20967(2005).
[6]
SUBCELLULAR LOCATION.
STRAIN=ATCC 35801 / TMC 107 / Erdman;
PubMed=19470749; DOI=10.1128/IAI.00143-09;
Hickey T.B., Thorson L.M., Speert D.P., Daffe M., Stokes R.W.;
"Mycobacterium tuberculosis Cpn60.2 and DnaK are located on the
bacterial surface, where Cpn60.2 facilitates efficient bacterial
association with macrophages.";
Infect. Immun. 77:3389-3401(2009).
[7]
SUBCELLULAR LOCATION.
STRAIN=H37Rv;
PubMed=21364279; DOI=10.1172/JCI44261;
Prados-Rosales R., Baena A., Martinez L.R., Luque-Garcia J.,
Kalscheuer R., Veeraraghavan U., Camara C., Nosanchuk J.D.,
Besra G.S., Chen B., Jimenez J., Glatman-Freedman A., Jacobs W.R. Jr.,
Porcelli S.A., Casadevall A.;
"Mycobacteria release active membrane vesicles that modulate immune
responses in a TLR2-dependent manner in mice.";
J. Clin. Invest. 121:1471-1483(2011).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
-!- FUNCTION: Acts as a chaperone. {ECO:0000255|HAMAP-Rule:MF_00332}.
-!- FUNCTION: Recombinant extracellular protein activates expression
of NF-kappa-B in immortalized human dermal endothelial cells in a
TLR2- and TLR4-dependent manner. Activation occurs via MYD88-
dependent and -independent pathways and requires TIRAP, TRIF and
TRAM (some experiments done in mouse cells, mice do not usually
catch tuberculosis) (PubMed:15809303).
{ECO:0000269|PubMed:15809303}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Secreted, capsule
{ECO:0000269|PubMed:19470749}. Cell surface
{ECO:0000269|PubMed:19470749}. Extracellular vesicle, Bacterial
extracellular vesicle {ECO:0000269|PubMed:21364279}. Note=Although
thought of as a cytoplasmic chaperone this protein is routinely
found extracellularly in the absence of cell lysis
(PubMed:19470749). Present in extracytoplasmic vesicles
(PubMed:21364279). {ECO:0000269|PubMed:19470749,
ECO:0000269|PubMed:21364279}.
-!- INDUCTION: By stress conditions e.g. heat shock and oxidative
stress under control of SigH. There is another promoter.
{ECO:0000269|PubMed:11567012}.
-!- SIMILARITY: Belongs to the heat shock protein 70 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA41306.1; Type=Frameshift; Positions=552; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; X58406; CAA41306.1; ALT_FRAME; Genomic_DNA.
EMBL; JX026662; AFM37299.1; -; Genomic_DNA.
EMBL; AL123456; CCP43080.1; -; Genomic_DNA.
PIR; G70574; G70574.
RefSeq; NP_214864.1; NC_000962.3.
RefSeq; WP_003401814.1; NZ_KK339370.1.
ProteinModelPortal; P9WMJ9; -.
SMR; P9WMJ9; -.
IntAct; P9WMJ9; 1.
STRING; 83332.Rv0350; -.
PaxDb; P9WMJ9; -.
PRIDE; P9WMJ9; -.
EnsemblBacteria; CCP43080; CCP43080; Rv0350.
GeneID; 885946; -.
KEGG; mtu:Rv0350; -.
TubercuList; Rv0350; -.
eggNOG; ENOG4105CFG; Bacteria.
eggNOG; COG0443; LUCA.
KO; K04043; -.
OMA; ISIKRHM; -.
PhylomeDB; P9WMJ9; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0097691; C:bacterial extracellular vesicle; IDA:UniProtKB.
GO; GO:0042603; C:capsule; IDA:CAFA.
GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
GO; GO:0005618; C:cell wall; IDA:MTBBASE.
GO; GO:0005829; C:cytosol; IDA:MTBBASE.
GO; GO:0005576; C:extracellular region; IDA:MTBBASE.
GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0001968; F:fibronectin binding; IPI:CAFA.
GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
GO; GO:0035375; F:zymogen binding; IPI:CAFA.
GO; GO:0071451; P:cellular response to superoxide; IEP:MTBBASE.
GO; GO:0044044; P:interaction with host via substance in symbiont surface; IDA:CAFA.
GO; GO:0010756; P:positive regulation of plasminogen activation; IDA:CAFA.
GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; IDA:CAFA.
GO; GO:0046777; P:protein autophosphorylation; IDA:MTBBASE.
GO; GO:0006457; P:protein folding; IEA:InterPro.
GO; GO:0046677; P:response to antibiotic; IEP:MTBBASE.
GO; GO:0046688; P:response to copper ion; IEP:MTBBASE.
GO; GO:0009408; P:response to heat; IEP:MTBBASE.
Gene3D; 1.20.1270.10; -; 1.
Gene3D; 2.60.34.10; -; 1.
HAMAP; MF_00332; DnaK; 1.
InterPro; IPR012725; Chaperone_DnaK.
InterPro; IPR018181; Heat_shock_70_CS.
InterPro; IPR029048; HSP70_C_sf.
InterPro; IPR029047; HSP70_peptide-bd_sf.
InterPro; IPR013126; Hsp_70_fam.
PANTHER; PTHR19375; PTHR19375; 2.
Pfam; PF00012; HSP70; 2.
PRINTS; PR00301; HEATSHOCK70.
SUPFAM; SSF100920; SSF100920; 1.
SUPFAM; SSF100934; SSF100934; 1.
TIGRFAMs; TIGR02350; prok_dnaK; 1.
PROSITE; PS00297; HSP70_1; 1.
PROSITE; PS00329; HSP70_2; 1.
PROSITE; PS01036; HSP70_3; 1.
1: Evidence at protein level;
ATP-binding; Chaperone; Complete proteome; Cytoplasm;
Nucleotide-binding; Phosphoprotein; Reference proteome; Secreted;
Stress response.
CHAIN 1 625 Chaperone protein DnaK.
/FTId=PRO_0000078499.
MOD_RES 175 175 Phosphothreonine; by autocatalysis.
{ECO:0000250}.
CONFLICT 153 154 LA -> PG (in Ref. 1; CAA41306).
{ECO:0000305}.
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


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