ID A0A3M8B2E7_9BACL Unreviewed; 608 AA.
AC A0A3M8B2E7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
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:RNB57631.1};
GN ORFNames=EDM57_09960 {ECO:0000313|EMBL:RNB57631.1};
OS Brevibacillus gelatini.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=1655277 {ECO:0000313|EMBL:RNB57631.1, ECO:0000313|Proteomes:UP000268829};
RN [1] {ECO:0000313|EMBL:RNB57631.1, ECO:0000313|Proteomes:UP000268829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100115 {ECO:0000313|EMBL:RNB57631.1,
RC ECO:0000313|Proteomes:UP000268829};
RA Dunlap C.;
RT "Phylogenomics of Brevibacillus.";
RL Submitted (OCT-2018) 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:RNB57631.1}.
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DR EMBL; RHHS01000022; RNB57631.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M8B2E7; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000268829; 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};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 578..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 477..511
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 173
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 608 AA; 65614 MW; 6AB28BA891AC1796 CRC64;
MSRVIGIDLG TTNSCVAVME GGEPVVIANA EGNRTTPSVV AFKNGERIVG EAAKRQAITN
PDNTVISIKR HMGTTHKETL EGKQYTPEQI SAMILQKLKA DAEAYLGQPV TQAVITVPAY
FNDSQRQATK DAGKIAGLEV LRIVNEPTAA ALAYGMEKTE DQTVLVFDLG GGTFDVSILE
LSDGFFEVKA TSGDNQLGGD DFDNVIINYL VNEFKKEHGI DLSKDRMAQQ RLKDAAEKAK
KDLSGVLTTT ISLPFITADA TGPKHLEMNL TRAKFEELSA ELVERTMGPT RQALKDAGLT
PSEIDRVILV GGSTRIPAVQ EAIKKFIGKE PHKGVNPDEV VALGAAVQAG VLTGDVKDVV
LLDVTPLSLG IETLGGVFTK LIDRNTTIPT SKSQVFSTAA DNQTSVEIHV LQGERQMAAD
NKSLGRFTLS DIPPAPRGVP QIEVSFDIDA NGIVNVRAKD LGTGKEQRIT ITSNSGLSDE
EIERMVKEAE LNAEEDKKRK EQVEIRNEAD QLVFTTEKTL KDVDGKVDQA EIDRANAAKD
KVKKALEGGN IDEIKAAKDE LSEIIQQITV KLYQQAAQAQ QNAGGAAEGQ EPKKDNVVDA
DYEVVDEK
//
