DNAK_BREBN
ID DNAK_BREBN Reviewed; 609 AA.
AC C0ZB48;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=BBR47_20300;
OS Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=358681;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=47 / JCM 6285 / NBRC 100599;
RA Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W.,
RA Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S.,
RA Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., Yoshikawa H.,
RA Udaka S., Tanikawa S., Fujita N.;
RT "Brevibacillus brevis strain 47, complete genome.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; AP008955; BAH43007.1; -; Genomic_DNA.
DR RefSeq; WP_012685740.1; NC_012491.1.
DR AlphaFoldDB; C0ZB48; -.
DR SMR; C0ZB48; -.
DR STRING; 358681.BBR47_20300; -.
DR EnsemblBacteria; BAH43007; BAH43007; BBR47_20300.
DR KEGG; bbe:BBR47_20300; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_9; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000001877; 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; 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 3: Inferred from homology;
KW ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1..609
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000133134"
FT REGION 580..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..609
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 173
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 609 AA; 65534 MW; ED224090838D249C CRC64;
MSRVIGIDLG TTNSCVAVME GGEPVVIANA EGNRTTPSVV AFKNGERIVG EAAKRQAITN
PDNTVISIKR HMGSAHKETL EGNQYTPEQI SAMILQKLKA DAEAYLGQSV TQAVITVPAY
FNDSQRQATK DAGKIAGLEV LRIVNEPTAA ALAYGMEKTE DQTVLVFDLG GGTFDVSILE
LSDGFFEVKA TSGDNKLGGD DFDDVVMNYL VSEFKKEHGI DLSKDRMAQQ RLKDAAEKAK
KDLSGVLTTT ISLPFITADA TGPKHLEMNL TRAKFEELSA ELVERTMGPT RQALKDAGLT
PSELDRVILV GGSTRIPAVQ EAIKKFTGKE PHKGVNPDEV VALGAAVQAG VLTGDVKDVV
LLDVTPLSLG IETLGGVFTK LIDRNTTIPT SKSQVFSTAA DNQTSVEIHV LQGERQMAGD
NKSLGRFNLS DIPPAPRGIP QIEVSFDIDA NGIVNVRAKD LGTGKEQRIT ITSNSGLSDD
DIDRMVKDAE LNAEADKQRK EQVEVRNEAD QLVFTTEKTL KEVEGKIDQA EIDRANAAKD
KVKAALEGSN FEEIKTAKDE LSEIIQQISV KLYEQAAQAQ AAQGGGAEGQ EPKKDNVVDA
DYEVVDDKK