ID A6GNF0_9BURK Unreviewed; 650 AA.
AC A6GNF0;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 73.
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:EDM84238.1};
GN ORFNames=LMED105_01708 {ECO:0000313|EMBL:EDM84238.1};
OS Limnobacter sp. MED105.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Limnobacter.
OX NCBI_TaxID=391597 {ECO:0000313|EMBL:EDM84238.1, ECO:0000313|Proteomes:UP000010322};
RN [1] {ECO:0000313|EMBL:EDM84238.1, ECO:0000313|Proteomes:UP000010322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED105 {ECO:0000313|EMBL:EDM84238.1,
RC ECO:0000313|Proteomes:UP000010322};
RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2007) 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:EDM84238.1}.
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DR EMBL; ABCT01000003; EDM84238.1; -; Genomic_DNA.
DR RefSeq; WP_008248598.1; NZ_ABCT01000003.1.
DR AlphaFoldDB; A6GNF0; -.
DR STRING; 391597.LMED105_01708; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000010322; 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}; Chaperone {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}; Reference proteome {ECO:0000313|Proteomes:UP000010322};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 603..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..650
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 200
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 650 AA; 70001 MW; 7DC540A489D64689 CRC64;
MGKIIGIDLG TTNSCVAVFE GGGYKVIENS EGARTTPSII AYMEDGEILV GAPAKRQAVT
NPKNTLYAVK RLIGRKFEDA EVQKDIDMMP FTIMKADNGD AWVGVRDQKL APPQVSAEVL
RKMKKTAEDY LGEEVTEAVI TVPAYFNDSQ RQATKDAGRI AGLDVKRIIN EPTAAALAFG
MDKAEKGDRK IAVYDLGGGT FDVSIIEIAD IDGEKQFEVL STNGDTFLGG EDFDQRIIDH
IIDEFKKNNG VDLSKDPIAL QRIKAAAERA KIELSSSQQT EINEPYIAMA NGAPVHLTTK
LSRSKLEALV EDLISRTVEP MKMALKDAGV STSQIDDIIL VGGMTRMPKV QEAVKNFFGK
EPRKDVNPDE AVAAGAAIQG SVLSGDRKDV LLLDVSPLSL GIETMGGVMT KMIEKNTTIP
TKFSQVFSTA DDNQPAVTIK VYQGERQMAN DNKSLGEFNL EGIPPAPRGV PQIEVTFDID
ANGILHVSAK DKGTGKENKI VIKANSGLSE DEIQKMVKDA EANAADDAKR RELAEAKNQA
DALVHSTRKS LGEYGDKLEA GEKEKIEAAC KALEEAAKGE DKDAIDARTK ELAESAQKLG
EKMYADMQAQ QAAEGAAAGA NPGGAEQQSS SKKDDADDVV DADFKEVKDK
//
