ID A0A1M5YWZ7_9BURK Unreviewed; 640 AA.
AC A0A1M5YWZ7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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 ORFNames=SAMN04488135_11112 {ECO:0000313|EMBL:SHI16390.1};
OS Pollutimonas bauzanensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Pollutimonas.
OX NCBI_TaxID=658167 {ECO:0000313|EMBL:SHI16390.1, ECO:0000313|Proteomes:UP000184226};
RN [1] {ECO:0000313|EMBL:SHI16390.1, ECO:0000313|Proteomes:UP000184226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10190 {ECO:0000313|EMBL:SHI16390.1,
RC ECO:0000313|Proteomes:UP000184226};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FQXE01000011; SHI16390.1; -; Genomic_DNA.
DR RefSeq; WP_073105698.1; NZ_FQXE01000011.1.
DR AlphaFoldDB; A0A1M5YWZ7; -.
DR STRING; 658167.SAMN04488135_11112; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000184226; 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000184226};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 611..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 253..280
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 200
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 640 AA; 69131 MW; 8BA6D829BC3B7066 CRC64;
MGKIIGIDLG TTNSCVAVMD GSSVKIIENA EGTRTTPSIV AYLQDGEILV GAPAKRQAVT
NPKNTLYAVK RLIGRKFDEK AVQKDIHLMP YNILKADNGD AWVEAQGKKL APPQVSADVL
RKMKKTAEDY LGEEVTEAVI TVPAYFNDSQ RQATKDAGRI AGLDVKRIIN EPTAAALAFG
MDKTEKGDRK IAVYDLGGGT FDISIIDIAD VDGEKQFEVL STNGDTFLGG EDFDQRIIEY
IISEFKKESS VDLSKDMLAL QRLKEAAEKA KIELSSAQQT EINLPYITAD ATGPKHLSLK
ITRAKLEALV EELIERTIEP CRVAIKDAGV KVSEIDDVIL VGGMTRMPKV QEKVKEFFGK
EPRKDVNPDE AVAAGAAIQG SVLSGDRKDV LLLDVTPLSL GIETLGGVMT KMIQKNTTIP
TRFSQVFSTA DDNQPAVTIK VFQGEREIAA GNKGLGEFNL EGIPPSARGT PQIEVTFDID
ANGILHVSAK DKGTGKENKI TIKANSGLTD QEIERMVKDA EANAEDDHRI AELALARNQA
DALVHSTRKS LEEYGDKLEA SEKETIEAAI KAVEDTLKDG DKAAIDAKVE ALSTASQKLG
EKMYADMQAQ AAASQGAAEA AEPADDNVVD ADFKEVKRDQ
//
