ID A0A0X1S0J5_9BACL Unreviewed; 609 AA.
AC A0A0X1S0J5;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Chaperone protein DnaK {ECO:0000256|ARBA:ARBA00014415, ECO:0000256|HAMAP-Rule:MF_00332};
DE AltName: Full=HSP70 {ECO:0000256|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock 70 kDa protein {ECO:0000256|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock protein 70 {ECO:0000256|HAMAP-Rule:MF_00332};
GN Name=dnaK {ECO:0000256|HAMAP-Rule:MF_00332,
GN ECO:0000313|EMBL:AMA64319.1};
GN ORFNames=ASO14_1108 {ECO:0000313|EMBL:AMA64319.1};
OS Kurthia sp. 11kri321.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Kurthia.
OX NCBI_TaxID=1750719 {ECO:0000313|EMBL:AMA64319.1, ECO:0000313|Proteomes:UP000058129};
RN [1] {ECO:0000313|EMBL:AMA64319.1, ECO:0000313|Proteomes:UP000058129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11kri321 {ECO:0000313|EMBL:AMA64319.1,
RC ECO:0000313|Proteomes:UP000058129};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000256|ARBA:ARBA00002290,
CC ECO:0000256|HAMAP-Rule:MF_00332}.
CC -!- INDUCTION: By stress conditions e.g. heat shock. {ECO:0000256|HAMAP-
CC Rule:MF_00332}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|HAMAP-Rule:MF_00332,
CC ECO:0000256|RuleBase:RU003322}.
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DR EMBL; CP013217; AMA64319.1; -; Genomic_DNA.
DR RefSeq; WP_068452563.1; NZ_CP013217.1.
DR AlphaFoldDB; A0A0X1S0J5; -.
DR STRING; 1750719.ASO14_1108; -.
DR KEGG; kur:ASO14_1108; -.
DR PATRIC; fig|1750719.3.peg.1048; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000058129; 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 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 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00332};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00332};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00332};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW Rule:MF_00332}; Reference proteome {ECO:0000313|Proteomes:UP000058129};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 580..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 222..249
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 479..515
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 593..609
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 173
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 609 AA; 65248 MW; C6D19929A86F5F15 CRC64;
MSKIIGIDLG TTNSCVSVLE GGEPVVIANK EGARTTPSVV AFKNGERQVG EVAKRQSITN
PNTIISIKRH MGEDYKVTVE DKTYTPQEIS AMILTHLKEY AEDYLGEKVT KAVITVPAYF
NDAQRQATKD AGKIAGLEVE RIINEPTAAA LAYGLEKMDV DQKVLVFDLG GGTFDVSILE
LGDGVFEVLA TAGDNKLGGD DFDEAIIDYL VAEFKKENGI DLSKDKMAMQ RLKDAAEKAK
KELSGVTTAQ VSLPFITAGE AGPLHLEMSI SRAKFNEITA DLVERTMIPT RQALKDAGLS
ASEIDQVILV GGSTRIPAVQ EAVQKATGKE PHKGVNPDEV VAMGAAVQGG VLTGDVEDVV
LLDVTPLSLG IETMGGVFTK LIERNTTIPT SKSQTFSTAA DNQPAVDIHV LQGERPMAAD
NKTLGRFQLT DIPAAPRGIP QIEVTFDIDK NGIVTVKAKD LGTNKEQNIV IQSDSGLSEA
DIERMVKEAE ENAEADKARK EEADLRNEAD QLVFQTDKTL ADLGEQVTED EKKPVEEAKE
ELAKAIEAGE IEGIKAAKEK LEGLLQPLVM KVYEQAAAAQ QAAQGGEAGG AKDDGVVDAD
FTEVDDDKK
//
