ID   DNAK_BARBK              Reviewed;         631 AA.
AC   A1UUC3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=BARBAKC583_1328;
OS   Bartonella bacilliformis (strain ATCC 35685 / NCTC 12138 / KC583).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=360095;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35685 / NCTC 12138 / KC583;
RA   Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S.,
RA   Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R.,
RA   Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J.,
RA   Fraser-Ligget C., Seshadri R.;
RL   Submitted (DEC-2006) 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; CP000524; ABM45470.1; -; Genomic_DNA.
DR   RefSeq; WP_005768116.1; NC_008783.1.
DR   AlphaFoldDB; A1UUC3; -.
DR   SMR; A1UUC3; -.
DR   STRING; 360095.BARBAKC583_1328; -.
DR   PRIDE; A1UUC3; -.
DR   EnsemblBacteria; ABM45470; ABM45470; BARBAKC583_1328.
DR   KEGG; bbk:BARBAKC583_1328; -.
DR   PATRIC; fig|360095.6.peg.1300; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_5; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000643; 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_1000059512"
FT   MOD_RES         198
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   631 AA;  68104 MW;  731B9E9BAE3D178F CRC64;
     MAKVIGIDLG TTNSCVAVMD GKNAKVIENS EGARTTPSVV AFTDSGERLV GQPAKRQAVT
     NPEGTVFAVK RLIGRRFDDP MVEKDKALVP YKIVKGDNGD AWVEENSKKY SPSQISAMIL
     QKMKETAESY LGEKVEQAVI TVPAYFNDAQ RQATKDAGKI AGLEVLRIIN EPTAAALAYG
     LDKKDGKTIA VYDLGGGTFD ISVLEIGDGV FEVKSTNGDT FLGGEDFDMC LVSYFADEFK
     KEQGIDLKND KLALQRLKEA AEKAKIELSS SQQTEVNLPF ITADQSGPKH LTMKLTRAKF
     ESLVDDLVQR TIEPCKAALK DAGLRAGEID EVVLVGGMTR MPKIQEVVQN FFGKDPHKGV
     NPDEVVAMGA AIQGGVLQGD VKDVLLLDVT PLSLGIETLG GVFTRLIERN TTIPTKKSQT
     FSTADDNQNA VTIRVFQGER EMANDNKLLA QFDLVGIPPA PRGVPQIEVT FDIDANGIVN
     VSAKDKGTGK EHQIRIQASG GLSDADIENM VKDAESHAAE DKKRRENVEA KNQAEALIHS
     TEKSLTEYGD KVSAEDKGQI EAAIADLKAV LDGDNSEEVK AKMQKLAEVS MKLGQAMYEA
     SNASAEADAV ADSANDDVVD ADFEEINDKK K