ID   DNAK_ACIBT              Reviewed;         646 AA.
AC   A3M8W9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
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}; OrderedLocusNames=A1S_2960;
OS   Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC
OS   KC755 / 5377).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=400667;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX   PubMed=17344419; DOI=10.1101/gad.1510307;
RA   Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA   Gerstein M., Snyder M.;
RT   "New insights into Acinetobacter baumannii pathogenesis revealed by high-
RT   density pyrosequencing and transposon mutagenesis.";
RL   Genes Dev. 21:601-614(2007).
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; CP000521; ABO13363.2; -; Genomic_DNA.
DR   RefSeq; WP_001062605.1; NZ_CP053098.1.
DR   AlphaFoldDB; A3M8W9; -.
DR   SMR; A3M8W9; -.
DR   GeneID; 66398997; -.
DR   KEGG; acb:A1S_2960; -.
DR   HOGENOM; CLU_005965_2_1_6; -.
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..646
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119654"
FT   REGION          603..646
FT                   /note="Disordered"
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   646 AA;  69404 MW;  7E759211769E8E4B CRC64;
     MAKIIGIDLG TTNSCVAVLE GDKVKVIENA EGARTTPSII AYKDGEILVG QSAKRQAVTN
     PKNTLFAIKR LIGRRYEDQA VQKDIGLVPY KIIKADNGDA WVEVNDKKLA PQQISAEILK
     KMKKTAEDYL GETVTEAVIT VPAYFNDAQR QATKDAGKIA GLDVKRIINE PTAAALAFGM
     DKKEGDRKVA VYDLGGGTFD VSIIEIADLD GDQQIEVLST NGDTFLGGED FDNALIEYLV
     EEFKKEQNVN LKNDPLALQR LKEAAEKAKI ELSSSNATEI NLPYITADAT GPKHLVINVT
     RAKLEGLVAD LVARTIEPCK IALKDAGLST SDISDVILVG GQSRMPLVQQ KVQEFFGREP
     RKDVNPDEAV AIGAAIQGAV LSGDKNDVLL LDVTPLTLGI ETMGGVLTPI IEKNTTIPAK
     KSQVFSTAAD NQPAVDISVY QGERKMAQQN KLLGNFQLGD IPPAPRGVPQ IEVSFDINAD
     GILKVSAKDK STGKEQSIQI KANSGLSDAE IEAMIKDAEA NAEEDRKFEE LAKARNEADA
     LISSSNKAVK DLGDKVTEDE KTAVNTAVSE LEAATKENDV EAIKAKTEAL QNILMPITQR
     AYEQAQQAGG AEGFDPNAFQ GGDAGQQKAD DGVVDAEFTE VKDDKK