ID D4FYY8_BACNB Unreviewed; 611 AA.
AC D4FYY8;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 67.
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:BAI86069.1};
GN ORFNames=BSNT_08991 {ECO:0000313|EMBL:BAI86069.1};
OS Bacillus subtilis subsp. natto (strain BEST195).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=645657 {ECO:0000313|EMBL:BAI86069.1, ECO:0000313|Proteomes:UP000006805};
RN [1] {ECO:0000313|EMBL:BAI86069.1, ECO:0000313|Proteomes:UP000006805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BEST195 {ECO:0000313|EMBL:BAI86069.1,
RC ECO:0000313|Proteomes:UP000006805};
RX PubMed=20398357; DOI=10.1186/1471-2164-11-243;
RA Nishito Y., Osana Y., Hachiya T., Popendorf K., Toyoda A., Fujiyama A.,
RA Itaya M., Sakakibara Y.;
RT "Whole genome assembly of a natto production strain Bacillus subtilis natto
RT from very short read data.";
RL BMC Genomics 11:243-243(2010).
RN [2] {ECO:0000313|EMBL:BAI86069.1, ECO:0000313|Proteomes:UP000006805}
RP GENOME REANNOTATION.
RC STRAIN=BEST195 {ECO:0000313|EMBL:BAI86069.1,
RC ECO:0000313|Proteomes:UP000006805};
RX PubMed=25329997; DOI=10.1371/journal.pone.0109999;
RA Kamada M., Hase S., Sato K., Toyoda A., Fujiyama A., Sakakibara Y.;
RT "Whole genome complete resequencing of Bacillus subtilis natto by combining
RT long reads with high-quality short reads.";
RL PLoS ONE 9:E109999-E109999(2014).
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; AP011541; BAI86069.1; -; Genomic_DNA.
DR RefSeq; WP_004398786.1; NC_017196.2.
DR AlphaFoldDB; D4FYY8; -.
DR SMR; D4FYY8; -.
DR STRING; 86029.AWV81_13235; -.
DR KEGG; bso:BSNT_08991; -.
DR PATRIC; fig|645657.3.peg.3488; -.
DR HOGENOM; CLU_005965_2_4_9; -.
DR Proteomes; UP000006805; 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};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 579..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 222..249
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 532..571
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 593..611
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 611 AA; 66002 MW; E83CEA6E16A31593 CRC64;
MSKVIGIDLG TTNSCVAVLE GGEPKVIANA EGNRTTPSVV AFKNGERQVG EVAKRQSITN
PNTIMSIKRH MGTDYKVEIE GKDYTPQEVS AIILQHLKSY AESYLGETVS KAVITVPAYF
NDAERQATKD AGKIAGLEVE RIINEPTAAA LAYGLDKTDE DQTILVYDLG GGTFDVSILE
LGDGVFEVRS TAGDNRLGGD DFDQVIIDHL VSEFKKENGI DLSKDKMALQ RLKDAAEKAK
KDLSGVSSTQ ISLPFITAGE AGPLHLELTL TRAKFEELSS HLVERTMGPV RQALQDAGLS
ASEIDKVILV GGSTRIPAVQ EAIKKETGKE AHKGVNPDEV VALGAAIQGG VITGDVKDVV
LLDVTPLSLG IETMGGVFTK LIDRNTTIPT SKSQVFSTAA DNQTAVDIHV LQGERPMSAD
NKTLGRFQLT DIPPAPRGVP QIEVSFDIDK NGIVNVRAKD LGTGKEQNIT IKSSSGLSDE
EIERMVKEAE ENADADAKKK EEIEVRNEAD QLVFQTEKTL KDLEGKVDEE QVKKANDAKD
ALKAAIEKNE FEEIKAKKDE LQTIVQELSM KLYEEAAKAQ QAQGGANAEG KADDNVVDAE
YEEVNDDQNK K
//
