DNAK_RENSM
ID DNAK_RENSM Reviewed; 623 AA.
AC A9WQR3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
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};
GN OrderedLocusNames=RSal33209_1909;
OS Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 /
OS NBRC 15589 / NCIMB 2235).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Renibacterium.
OX NCBI_TaxID=288705;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235;
RX PubMed=18723615; DOI=10.1128/jb.00721-08;
RA Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S.,
RA Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H.,
RA Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.;
RT "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests
RT reductive evolution away from an environmental Arthrobacter ancestor.";
RL J. Bacteriol. 190:6970-6982(2008).
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; CP000910; ABY23642.1; -; Genomic_DNA.
DR RefSeq; WP_012245313.1; NC_010168.1.
DR AlphaFoldDB; A9WQR3; -.
DR SMR; A9WQR3; -.
DR STRING; 288705.RSal33209_1909; -.
DR PRIDE; A9WQR3; -.
DR EnsemblBacteria; ABY23642; ABY23642; RSal33209_1909.
DR KEGG; rsa:RSal33209_1909; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_11; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000002007; 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; 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..623
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000079238"
FT REGION 584..623
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 623 AA; 66567 MW; 23181F5621DF9E7A CRC64;
MSRAVGIDLG TTNSVVSVLE GGEPTVIANA EGGRTTPSVV AFSKSGEVLV GEIAKRQAVN
NIDRTIASVK RHMGTDWTID IDDKKYTAQE ISARTLMKLK NDAESYLGEK VTDAVITVPA
YFNDAERQAT KEAGEIAGLN VLRIVNEPTA AALAYGLDKG KEDELILVFD LGGGTFDVSL
LEVGKDDDGF STIQVRATSG DNRLGGDDWD QRVVDYLLNQ LKVKGIDLSK DKIALQRLRE
AAEQAKKELS SATSTNISLQ YLSVTPDGPV HLDEQLTRAK FQELTSDLLE RTKKPFNDVI
AEAGIKVSDI DHIVLVGGST RMPAVTELVK QLAGGKDPNK GVNPDEVVAV GAALQAGVLK
GERKDVLLID VTPLSLGIET KGGVMTKLIE RNTAIPTKRS ETFTTADDNQ PSVAIQVFQG
EREFTRDNKP LGTFELTGIA PAQRGVPQVE VTFDIDANGI VHVSAKDKGT GKEQSMTITG
GSSLSKEDIE RMVADAEAHA AEDKTRREQA DVRNSAEQLA YSVDKILSEN DDKLPEEVKT
EVKADVESLK AALAGTDEYA VKAASEKLQA SQTKLGEAIY ASTQAEGAAP AGDAAGAPAG
EAKPEEDIVD AEIVDEEPKN EKK