DNAK_ACIB3
ID DNAK_ACIB3 Reviewed; 646 AA.
AC B7H317;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=ABBFA_003505;
OS Acinetobacter baumannii (strain AB307-0294).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=557600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AB307-0294;
RX PubMed=18931120; DOI=10.1128/jb.00834-08;
RA Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J.,
RA MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M.,
RA Bonomo R.A., Gill S.R.;
RT "Comparative genome sequence analysis of multidrug-resistant Acinetobacter
RT baumannii.";
RL J. Bacteriol. 190:8053-8064(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; CP001172; ACJ58774.1; -; Genomic_DNA.
DR RefSeq; WP_001062607.1; NZ_CP001172.1.
DR AlphaFoldDB; B7H317; -.
DR SMR; B7H317; -.
DR HOGENOM; CLU_005965_2_4_6; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000006924; 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 Stress response.
FT CHAIN 1..646
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000119651"
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; 69432 MW; 617A820E798E8E4B 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 EVIKAKTEAL QNILMPITQR
AYEQAQQAGG AEGFDPNAFQ GGDAGQQKAD DGVVDAEFTE VKDDKK