ID A0A0F2P9D2_9GAMM Unreviewed; 641 AA.
AC A0A0F2P9D2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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:KJS09961.1};
GN ORFNames=VR73_00385 {ECO:0000313|EMBL:KJS09961.1};
OS Gammaproteobacteria bacterium BRH_c0.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1629722 {ECO:0000313|EMBL:KJS09961.1, ECO:0000313|Proteomes:UP000033581};
RN [1] {ECO:0000313|EMBL:KJS09961.1, ECO:0000313|Proteomes:UP000033581}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c0 {ECO:0000313|EMBL:KJS09961.1};
RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (MAR-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:KJS09961.1}.
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DR EMBL; LADM01000004; KJS09961.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2P9D2; -.
DR STRING; 1629722.VR73_00385; -.
DR PATRIC; fig|1629722.3.peg.2489; -.
DR Proteomes; UP000033581; 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 604..627
FT /note="Disordered"
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 641 AA; 68493 MW; A5CA047D29CED79B CRC64;
MGKIIGIDLG TTNSCVAVLE GGKARVIENA EGTRTTPSIV AFTEDGEILV GQAAKRQSVT
NPHNTLYAIK RLIGRRFDDS VVQKDIGMVP YKIIKADNGD AWVDVKGDKK APPQISAEVL
KKMKKTAEDY LGEAVTEAVI TVPAYFNDSQ RQATKDAGRI AGLDVKRIIN EPTAAALAYG
MDKAGGDRVI AVYDLGGGTF DISIIEIADV DGEKQFEVLS TNGDTFLGGE DFDMTLINYL
ADEFKKENTI DLKGDALAMQ RLKEAAEKAK IELSSSQQTE VNLPYITADA TGPKHLVVKL
TRSKLESLVE SLVNRSLEPL KLALQDAGKT TAQIDEIILV GGQTRMPLVQ QKVTDFFGKE
PRKDVNPDEA VAVGAALQAA VLSGDVKDVL LLDVTPLSLG IETMGGIATP LIEKNTTIPT
KKSQVFSTAD DNQTAVTIHV VQGERKQASQ NKSLGRFDLA DIPPAPRGLP QIEVTFNIDA
NGILHVSAKD KATGKEQSIV IKASSGLSDE EIEQMVRDAE ANAAEDKKFE DLVHARNAAD
SLVHAVSKTL ADAGDKASEE EKTAIEAAIK DVEEALKSDD KDAIEAATGK LSEASANLAQ
KLYAEQAQAE NPGAGDAGEN AQTAEDVVDA EFEEVKDADK K
//
