GenomeNet

Database: UniProt
Entry: A0A0Q3WNY3_BRECH
LinkDB: A0A0Q3WNY3_BRECH
Original site: A0A0Q3WNY3_BRECH 
ID   A0A0Q3WNY3_BRECH        Unreviewed;       610 AA.
AC   A0A0Q3WNY3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
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:KQL48949.1};
GN   ORFNames=AN963_03935 {ECO:0000313|EMBL:KQL48949.1};
OS   Brevibacillus choshinensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=54911 {ECO:0000313|EMBL:KQL48949.1, ECO:0000313|Proteomes:UP000051063};
RN   [1] {ECO:0000313|EMBL:KQL48949.1, ECO:0000313|Proteomes:UP000051063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8552 {ECO:0000313|EMBL:KQL48949.1,
RC   ECO:0000313|Proteomes:UP000051063};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Genome sequencing project for genomic taxonomy and phylogenomics of
RT   Bacillus-like bacteria.";
RL   Submitted (SEP-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}.
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:KQL48949.1}.
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DR   EMBL; LJJB01000007; KQL48949.1; -; Genomic_DNA.
DR   RefSeq; WP_055743246.1; NZ_LJJB01000007.1.
DR   AlphaFoldDB; A0A0Q3WNY3; -.
DR   PATRIC; fig|54911.3.peg.4903; -.
DR   OrthoDB; 9766019at2; -.
DR   Proteomes; UP000051063; 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; 3.30.30.30; -; 1.
DR   Gene3D; 3.30.420.40; -; 3.
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          576..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          486..540
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        593..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;  65579 MW;  CC8B689D2508C26F CRC64;
     MSRVIGIDLG TTNSCVAVME GGEPVVIANP EGNRTTPSVV AFKNGEKIVG EAAKRQAITN
     PDNTVISIKR HMGTAHKETL EGNEYTPQQI SAMILQKLKS DAEAYLGEAV TQAVITVPAY
     FNDSQRQATK DAGKIAGLEV LRIVNEPTAA ALAYGMEKSE DQTVLVFDLG GGTFDVSILE
     LSEGFFEVKA TSGDNKLGGD DFDQVVMDYL VSEFKKEHGI DLSKDRMAQQ RLKDAAEKAK
     KDLSGVLTTT ISLPFITADA TGPKHLEMNM TRAKFEELSA TLVERTMGPT RQALNDAGLT
     PNELDKVILV GGSTRIPAVQ EAIKKFTGKE PHKGVNPDEV VALGAAVQAG VLTGDVKDVV
     LLDVTPLSLG IETLGGVFTK LIDRNTTIPT SKSQVFSTAA DNQPGVEIHV LQGERQMAAD
     NKTLGRFNLN DIPPAPRGVP QIEVSFDIDA NGIVNVRAKD LGTGKEQRIT ITSNSGLSDD
     DIERMVKEAE LNAEADKQRK EQVEIRNEAD QLVFTTEKTL KEVEGKVDQA EIDRANAAKD
     KVKKALEGGN IDEIKSAKDE LSEIVQQISV KLYEQAAQAA QGAQGGAEGG QEPKKDNVVD
     ADYEVVDDKK
//
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