DNAK_AZOC5
ID DNAK_AZOC5 Reviewed; 631 AA.
AC A8IPT1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=AZC_0690;
OS Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / LMG
OS 6465 / NBRC 14845 / NCIMB 13405 / ORS 571).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Azorhizobium.
OX NCBI_TaxID=438753;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 / NCIMB
RC 13405 / ORS 571;
RA Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T.,
RA Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B.,
RA Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.;
RT "Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium
RT caulinodans ORS571.";
RL Submitted (APR-2007) 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; AP009384; BAF86688.1; -; Genomic_DNA.
DR RefSeq; WP_012169221.1; NC_009937.1.
DR AlphaFoldDB; A8IPT1; -.
DR SMR; A8IPT1; -.
DR STRING; 438753.AZC_0690; -.
DR EnsemblBacteria; BAF86688; BAF86688; AZC_0690.
DR KEGG; azc:AZC_0690; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_5; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000000270; 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; 1.
DR Pfam; PF00012; HSP70; 1.
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..631
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000072032"
FT REGION 598..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..631
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 198
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 631 AA; 67785 MW; 987F72733DE9066E CRC64;
MSKIIGIDLG TTNSCVAVME GASPKVIENA EGARTTPSIV AFTEDGERLV GQPAKRQGVT
NPERTFFAVK RLIGRRYDDP TVEKDKKLVP YKVVRADNGD AWVESDGKKY SPSQISAFIL
QKMKETAESF LGEKVEKAVI TVPAYFNDAQ RQATKDAGRI AGLEVLRIIN EPTAAALAYG
LDKKNSGTIA VYDLGGGTFD VSVLEIGDGV FEVKSTNGDT FLGGEDFDMR LVNYLADEFK
KEQGIDLRND KLALQRLKEA AEKAKIELSS ATQTEINLPF ITADASGPKH LTMKLTRAKF
EALVEDLIQR TMEPCRLALK DAGLSAGQID EVVLVGGMTR MPKVQEMVKQ FFGKEPHKGV
NPDEVVAIGA AIQAGVLQGD VKDVLLLDVT PLSLGIETLG GVFTRLIDRN TTIPTKKSQV
FSTAEDGQTA VTIRVFQGER EMAADNKILG QFDLVGIPPA PRGVPQIEVT FDIDANGIVQ
VSAKDKGTGK EQQIRIQASG GLNDADIEKM VKDAESHAAD DKKRRALAEA KNHGEALVHS
TEKALSEHGD KVGAAEKGAI ESALGELKTA LTTEDAEAIQ AKTQALAQAS LKLGEAMYSA
QQGGEQPGAA KKDDVVDAEF TEVDDDKKKS A