ID A0A0Q9N8Y2_9BACL Unreviewed; 612 AA.
AC A0A0Q9N8Y2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-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:KRE74992.1};
GN ORFNames=ASL11_03630 {ECO:0000313|EMBL:KRE74992.1};
OS Paenibacillus sp. Soil750.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736398 {ECO:0000313|EMBL:KRE74992.1, ECO:0000313|Proteomes:UP000051252};
RN [1] {ECO:0000313|EMBL:KRE74992.1, ECO:0000313|Proteomes:UP000051252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil750 {ECO:0000313|EMBL:KRE74992.1,
RC ECO:0000313|Proteomes:UP000051252};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE74992.1, ECO:0000313|Proteomes:UP000051252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil750 {ECO:0000313|EMBL:KRE74992.1,
RC ECO:0000313|Proteomes:UP000051252};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
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}.
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:KRE74992.1}.
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DR EMBL; LMSD01000002; KRE74992.1; -; Genomic_DNA.
DR RefSeq; WP_056609785.1; NZ_LMSD01000002.1.
DR AlphaFoldDB; A0A0Q9N8Y2; -.
DR STRING; 1736398.ASL11_03630; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000051252; 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 576..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 223..250
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 596..612
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 174
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 612 AA; 65198 MW; CC47A5D87B66A4DF CRC64;
MSKVIGIDLG TTNSCVAVME GGEAVVIPNP EGNRTTPSVV GFKKDGERVV GETAKRQAIT
NPDKTISSIK RHIGTNHKEH IDGKDYTPQE ISAIILQKLK ADAEAYLGQT VTQAVITVPA
YFNDSQRQAT KDAGKIAGLE VLRIVNEPTA AALAYGLEKT EDQTILVYDL GGGTFDVSIL
ELGDGFFEVK ATSGDNKLGG DDFDQVVMDY LVAEFKKEQG IDLSKDKAAV QRLKDAAEKA
KKELSGVLTT TVSLPFITVA DGVPQHLELN LTRAKFEELS AGLVERTLGP TRQALQDSGL
STSQIDKVVL VGGSTRIPAV VEAIKKLIGK EPHKGVNPDE VVALGAAVQA GVLTGEVKDV
VLLDVTPLSL GIETAGGVFT KMIDRNTTIP TTKSQVYSTY ADNQTSVEIH VLQGERSMAS
GNKTLGRFML GDIPPAPRGV PQIEVSFDID ANGIVNVSAL DKGTGKSQKI TITSSSGLSD
AEVEQMVKDA EAHAEEDRAR KELVEARNEA DQLVYSVDKT IKDLGDKVDQ GEIDKANAAK
EKVTAALAGN DLETIKKATE ELTEVIQQLS VKLYEQASQD QGPGPDAGAG EAPKGRENVV
DADYEVVDEP KK
//
