ID DNAK_STRA1 Reviewed; 609 AA.
AC Q3K3T2;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 100.
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=SAK_0147;
OS Streptococcus agalactiae serotype Ia (strain ATCC 27591 / A909 / CDC
OS SS700).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=205921;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27591 / A909 / CDC SS700;
RX PubMed=16172379; DOI=10.1073/pnas.0506758102;
RA Tettelin H., Masignani V., Cieslewicz M.J., Donati C., Medini D.,
RA Ward N.L., Angiuoli S.V., Crabtree J., Jones A.L., Durkin A.S., DeBoy R.T.,
RA Davidsen T.M., Mora M., Scarselli M., Margarit y Ros I., Peterson J.D.,
RA Hauser C.R., Sundaram J.P., Nelson W.C., Madupu R., Brinkac L.M.,
RA Dodson R.J., Rosovitz M.J., Sullivan S.A., Daugherty S.C., Haft D.H.,
RA Selengut J., Gwinn M.L., Zhou L., Zafar N., Khouri H., Radune D.,
RA Dimitrov G., Watkins K., O'Connor K.J., Smith S., Utterback T.R., White O.,
RA Rubens C.E., Grandi G., Madoff L.C., Kasper D.L., Telford J.L.,
RA Wessels M.R., Rappuoli R., Fraser C.M.;
RT "Genome analysis of multiple pathogenic isolates of Streptococcus
RT agalactiae: implications for the microbial 'pan-genome'.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13950-13955(2005).
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; CP000114; ABA45634.1; -; Genomic_DNA.
DR RefSeq; WP_000034648.1; NC_007432.1.
DR AlphaFoldDB; Q3K3T2; -.
DR SMR; Q3K3T2; -.
DR GeneID; 66885073; -.
DR KEGG; sak:SAK_0147; -.
DR HOGENOM; CLU_005965_2_4_9; -.
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 CDD; cd10234; HSPA9-Ssq1-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
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 NCBIfam; TIGR02350; prok_dnaK; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 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..609
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000226014"
FT REGION 578..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 173
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 609 AA; 64980 MW; 298D8ADCC9D31E0C CRC64;
MSKIIGIDLG TTNSAVAVLE GTESKIIANP EGNRTTPSVV SFKNGEIIVG DAAKRQAVTN
PDTVISIKSK MGTSEKVSAN GKEYTPQEIS AMILQYLKGY AEDYLGEKVE KAVITVPAYF
NDAQRQATKD AGKIAGLEVE RIVNEPTAAA LAYGMDKTDK DEKILVFDLG GGTFDVSILE
LGDGVFDVLA TAGDNKLGGD DFDQKIIDFL VEEFKKENGI DLSQDKMALQ RLKDAAEKAK
KDLSGVTQTQ ISLPFITAGS AGPLHLEMSL SRAKFDDLTR DLVERTKTPV RQALSDAGLS
LSEIDEVILV GGSTRIPAVV EAVKAETGKE PNKSVNPDEV VAMGAAIQGG VITGDVKDVV
LLDVTPLSLG IETMGGVFTK LIDRNTTIPT SKSQVFSTAA DNQPAVDIHV LQGERPMAAD
NKTLGRFQLT DIPAAPRGIP QIEVTFDIDK NGIVSVKAKD LGTQKEQHIV IQSNSGLTDE
EIDKMMKDAE ANAEADAKRK EEVDLKNEVD QAIFATEKTI KETEGKGFDT ERDAAQSALD
ELKKAQESGN LDDMKAKLEA LNEKAQALAV KLYEQAAAAQ QAAQGAEGAQ SADSSSKGDD
VVDGEFTEK
//
