ID A0A0Q8AI58_9PSED Unreviewed; 638 AA.
AC A0A0Q8AI58;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
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:KQZ82425.1};
GN ORFNames=ASD60_08065 {ECO:0000313|EMBL:KQZ82425.1};
OS Pseudomonas sp. Root562.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1736561 {ECO:0000313|EMBL:KQZ82425.1, ECO:0000313|Proteomes:UP000051426};
RN [1] {ECO:0000313|EMBL:KQZ82425.1, ECO:0000313|Proteomes:UP000051426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root562 {ECO:0000313|EMBL:KQZ82425.1,
RC ECO:0000313|Proteomes:UP000051426};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQZ82425.1, ECO:0000313|Proteomes:UP000051426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root562 {ECO:0000313|EMBL:KQZ82425.1,
RC ECO:0000313|Proteomes:UP000051426};
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|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:KQZ82425.1}.
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DR EMBL; LMGK01000021; KQZ82425.1; -; Genomic_DNA.
DR RefSeq; WP_056854958.1; NZ_LMGK01000021.1.
DR AlphaFoldDB; A0A0Q8AI58; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000051426; 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 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:SF541; CHAPERONE PROTEIN DNAK; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 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 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 605..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 199
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 638 AA; 68244 MW; 7A4319A9F3F0E5DB CRC64;
MGKIIGIDLG TTNSCVSVLE NGVAKVIENA EGARTTPSII AYANDGEILV GQSAKRQAVT
NPHNTLYAVK RLIGRKFDEE VVQKDIKMVP YKIAKADNGD AWVEVNGQKM APPQISAEIL
KKMKKTAEDY LGEPVTEAVI TVPAYFNDSQ RQATKDAGRI AGLDVKRIIN EPTAAALAYG
MDKAKGDHTV IVYDLGGGTF DVSVIEIAEV DGEHQFEVLA TNGDTFLGGE DFDIRLIDYL
VDEFKKESGM NLKGDPLAMQ RLKEAAEKAK IELSSAQSTD VNLPYITADA TGPKHLNVKI
SRAKLEALVE DLVQRTIEPC RIALKDSGID VGAINDVILV GGQTRMPLVQ KLVTEFFGKE
ARKDVNPDEA VAMGAAIQGA VLAGDVKDVL LLDVSPLTLG IETMGGVMTA LIEKNTTIPT
KKSQVFSTAD DNQGAVTIHV LQGERKQAAQ NKSLGKFDLA EIPPAPRGVP QIEVTFDIDA
NGILHVGAKD KATGKTQSIV IKANSGLSDE EIERMVRDAE ANAEEDRKFE ELAAARNQGD
ALVHSTRKMV ADAGDKVSAE EKTAIEAAVV ALEAAVKGDD KAAIEAKVEE LSKVSAPVAQ
KMYAEQAQPA EGAAPQGESA EKADDVVDAE FEEVKDHK
//
