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Database: UniProt
Entry: W4EP51_9BACL
LinkDB: W4EP51_9BACL
Original site: W4EP51_9BACL 
ID   W4EP51_9BACL            Unreviewed;       610 AA.
AC   W4EP51;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 41.
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   ORFNames=C176_15282 {ECO:0000313|EMBL:ETT82365.1};
OS   Viridibacillus arenosi FSL R5-213.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Viridibacillus.
OX   NCBI_TaxID=1227360 {ECO:0000313|EMBL:ETT82365.1, ECO:0000313|Proteomes:UP000019062};
RN   [1] {ECO:0000313|EMBL:ETT82365.1, ECO:0000313|Proteomes:UP000019062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL R5-213 {ECO:0000313|EMBL:ETT82365.1,
RC   ECO:0000313|Proteomes:UP000019062};
RX   PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA   Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA   den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT   "Genomic comparison of sporeforming bacilli isolated from milk.";
RL   BMC Genomics 15:26-26(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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ETT82365.1}.
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DR   EMBL; ASQA01000034; ETT82365.1; -; Genomic_DNA.
DR   RefSeq; WP_038187159.1; NZ_ASQA01000034.1.
DR   AlphaFoldDB; W4EP51; -.
DR   PATRIC; fig|1227360.4.peg.3111; -.
DR   eggNOG; COG0443; Bacteria.
DR   Proteomes; UP000019062; Unassembled WGS sequence.
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:UP000019062};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW   Rule:MF_00332}.
FT   REGION          577..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          222..249
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          484..545
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        589..610
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   610 AA;  65840 MW;  028722E28EABE888 CRC64;
     MSKIIGIDLG TTNSCVSVLE GGEPIVIANK EGARTTPSVV AFKNGERQVG EVAKRQSITN
     PNTIMSIKRH MGTDYKVDVE GTEYTPQQVS AMILQHLKDF AEDYLGEKVT QAVITVPAYF
     NDAQRQATKD AGKIAGLEVE RIINEPTAAA LAYGLEKTDV DQTVLVFDLG GGTFDVSILE
     LGDGVFEVKA TAGDNALGGD DFDQKIIDFL VAEFKKENGI DLAKDKMALQ RLKDAAEKAK
     KELSGVTTTQ ISLPFITAGE AGPLHLEVSL SRAKFNEITA DLVERTMIPT RQALKDAGLS
     ASEIDQVILV GGSTRIPAVQ EAVKKETGKE PHKGVNPDEV VAMGAAVQGG VLTGDVKDVV
     LLDVTPLSLG IETMGGVFTK LIDRNTTIPT SKSQTFSTAA DNQPAVDIHV LQGERPMAAD
     NKTLGRFQLS DIPAAPRGIP QIEVTFDIDK NGIVNVKAKD LGTQKEQTIT IQSDSSLSDE
     DIERMVKEAE LHAEEDKKRK EEAELRNEAD QLVFQVDKTI ADLGEQITED EKKSVEDAKE
     ELTKAIELGE IEGIKTSKEK LEGILQPLVM KVYEQAAQQQ QAAQGEQGPT ADKKDDGVVD
     ADFTEVDDNK
//
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