ID   DNAK_RHOCA              Reviewed;         637 AA.
AC   Q52701;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Chaperone protein DnaK;
DE   AltName: Full=HSP70;
DE   AltName: Full=Heat shock 70 kDa protein;
DE   AltName: Full=Heat shock protein 70;
GN   Name=dnaK;
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33303 / B10;
RA   Nickel C.M.;
RL   Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; U57637; AAC45473.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q52701; -.
DR   SMR; Q52701; -.
DR   PRIDE; Q52701; -.
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   Stress response.
FT   CHAIN           1..637
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078531"
FT   REGION          531..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          602..637
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         197
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   637 AA;  68630 MW;  9A3A57B92418F4E1 CRC64;
     MAKVIGIDLG TTNSCVAIMD GSQPRVIENS EGARTTPSIV AYTDNERLVG QPAKRQAVTN
     PTNTVFAVKR LIGRRTTDAE VEKDKKLVPY NIVDGGNGDA WVEVRGEKFS PAQVSAVILQ
     KMKETAESYL GETVTQAVIT VPAYFNDAQR QATKDAGKIA GLEVLRIINE PTAAALAYGL
     DKKDSKTIAV YDLGGGTFDI SVLEIDDGLF EVKSTNGDTF LGGEDFDMRI VNYLADEFKK
     EHGVDLTKDK MALQRLKEAA EKAKIELSSA SQTEINQPFI SMNAATGVPL HMVMKLTRAK
     LESLVDDLIK ASLKPCAAAL KDAGVSKDEI DEVVLVGGMT RMPRVVEEVT KFFGKEPHKG
     VNPDEVVALG AAIQAGVLQG DVKDVVLLDV TPLSLGIETL GGVFTRLIDR NTTIPTKKSQ
     IFSTAEDNQN AVTIRVFQGE REMAADNKML GMFNLENIPP APRGVPQIEV TFDIDANGIV
     SVKAKDKGTG KEQQITIQAS GGLSDDDIEK MIKDAEANAE ADKKRKELVE AKNTGESLLH
     STRKSLEEHG DKVDGSTVEM IELACNALEE SLKSEDPGKI KGAVQNLTDA AMKLGEAIYK
     AQASEAGPAS DDEDGPRSVD DDIVDADFED MGENKRK