DNAK_LEIXX
ID DNAK_LEIXX Reviewed; 624 AA.
AC Q6AC76;
DT 02-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=Lxx23780;
OS Leifsonia xyli subsp. xyli (strain CTCB07).
OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Leifsonia.
OX NCBI_TaxID=281090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CTCB07;
RX PubMed=15305603; DOI=10.1094/mpmi.2004.17.8.827;
RA Monteiro-Vitorello C.B., Camargo L.E.A., Van Sluys M.A., Kitajima J.P.,
RA Truffi D., do Amaral A.M., Harakava R., de Oliveira J.C.F., Wood D.,
RA de Oliveira M.C., Miyaki C.Y., Takita M.A., da Silva A.C.R., Furlan L.R.,
RA Carraro D.M., Camarotte G., Almeida N.F. Jr., Carrer H., Coutinho L.L.,
RA El-Dorry H.A., Ferro M.I.T., Gagliardi P.R., Giglioti E., Goldman M.H.S.,
RA Goldman G.H., Kimura E.T., Ferro E.S., Kuramae E.E., Lemos E.G.M.,
RA Lemos M.V.F., Mauro S.M.Z., Machado M.A., Marino C.L., Menck C.F.,
RA Nunes L.R., Oliveira R.C., Pereira G.G., Siqueira W., de Souza A.A.,
RA Tsai S.M., Zanca A.S., Simpson A.J.G., Brumbley S.M., Setubal J.C.;
RT "The genome sequence of the Gram-positive sugarcane pathogen Leifsonia xyli
RT subsp. xyli.";
RL Mol. Plant Microbe Interact. 17:827-836(2004).
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; AE016822; AAT90016.1; -; Genomic_DNA.
DR RefSeq; WP_011186995.1; NC_006087.1.
DR AlphaFoldDB; Q6AC76; -.
DR SMR; Q6AC76; -.
DR STRING; 281090.Lxx23780; -.
DR PRIDE; Q6AC76; -.
DR EnsemblBacteria; AAT90016; AAT90016; Lxx23780.
DR KEGG; lxx:Lxx23780; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_11; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000001306; 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; 2.
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..624
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000078479"
FT REGION 496..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 176
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 624 AA; 67360 MW; D366B56F8127476D CRC64;
MSRAVGIDLG TTNSVVSVLE GGEPTVIANA EGFRTTPSVV AFTKDGEVLV GETAKRQAVT
NVDRTLSSVK RHMGTDWKTQ EIDGKKYTAQ EISARILQKL KRDAEQYLGD TVTDAVITVP
AYFNDAERQA TKEAGEIAGL NVLRIINEPT AAALAYGLDK GKEDELILVF DLGGGTFDVS
LLEVGKDDDF STIQVRATAG DNRLGGDDWD QRIVEWLIKR FKESTGVDAS TDKIAKQRLK
EAAEQAKKEL SSSMSTSIQL PYLSLTENGP ANLDETLTRA QFEQMTSDLL DRTKKPFKDV
IKEAGIEVSD IAHVVLVGGS TRMPAVSELV KQETGGQEPN KGVNPDEVVA VGAALQAGVL
KGERKDVLLI DVTPLSLGIE TKGGIMTKLI ERNTAIPTKR SETFTTADDN QPSVAIQVFQ
GEREFTRDNK PLGTFELTGI APAPRGIPQV EVTFDIDANG IVHVSAKDKG TGKEQSMTIT
GGSSLPKDDI ERMVREAEEH AAEDKKRRES AETRNQAEQL VYSIEKLIKD NEEKLPEDIK
NEVQGDVDAL KAALAGEDDE AVKTAYDKLN ESQQKLGQAI YSAAQAAEAP AAAAGEEASA
PSSSTGEEDV IDAEVVEDEE KKQQ