ID A0A1J4N0M4_9ACTN Unreviewed; 619 AA.
AC A0A1J4N0M4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Chaperone protein DnaK {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=UG56_022665 {ECO:0000313|EMBL:OIJ24487.1};
OS Nocardioides luteus.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1844 {ECO:0000313|EMBL:OIJ24487.1, ECO:0000313|Proteomes:UP000033772};
RN [1] {ECO:0000313|EMBL:OIJ24487.1, ECO:0000313|Proteomes:UP000033772}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAFB {ECO:0000313|EMBL:OIJ24487.1,
RC ECO:0000313|Proteomes:UP000033772};
RA Murphy D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OIJ24487.1, ECO:0000313|Proteomes:UP000033772}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAFB {ECO:0000313|EMBL:OIJ24487.1,
RC ECO:0000313|Proteomes:UP000033772};
RA Brown L., Ruiz O.N., Gunasekera T.;
RT "Draft Genome Sequence of Nocardioides luteus Strain BAFB, an Alkane-
RT Degrading Bacterium Isolated from JP-7 Polluted Soil.";
RL Submitted (OCT-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}.
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:OIJ24487.1}.
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DR EMBL; JZDQ02000038; OIJ24487.1; -; Genomic_DNA.
DR RefSeq; WP_045549436.1; NZ_JZDQ02000038.1.
DR AlphaFoldDB; A0A1J4N0M4; -.
DR STRING; 1844.UG56_022665; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000033772; 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}; 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:UP000033772};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 580..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 223..250
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 534..561
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 174
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 619 AA; 65958 MW; 9A495408CC051C04 CRC64;
MARAVGIDLG TTNSVVSVLE GGEPTVIANA EGARTTPSVV AFSKSGEVLV GEVAKRQAVT
NVDRTIKSVK RHMGTDWKVT IDDKDFTPQQ ISAFVLQKLK RDAEAYLGET VTDAVITVPA
YFSDAQRQAT KEAGEIAGLN VSRIVNEPTA AALAYGLDKG DDQTILVFDL GGGTFDVSLL
EIGEGVVEVK ATSGDNHLGG DDWDNAIVKW MVDKFKAANG VDLSKDKIAA QRLQEAAEKA
KIELSSSQNT SIHLPYITHG ESGPLHFEET LTRAEFQKIT ADLLDRTKKP FESVLKDAGV
ALKDIDHVVL VGGSTRMPAV TDLVKSLLGG KEPNKGVNPD EVVAVGAALQ AGVLKGEVKD
VLLLDVTPLS LGIETKGGVF TTLIERNTTI PTKRSEIFTT ADDNQPSVEI KVAQGERPMW
SENQPLGNFE LTGLPPAPRG VPKIEVTFDI DANGIVHVSA KDQASGREQS MTISGGSALS
KEDIDRMVKE AEQYAEEDAK RRESIEIRNQ GDSLVYTTEK FITDSGDKVP DDVKTEVQAD
LDALKKILED TEADKDAIQT AITKLGESSQ KMGAAMYAAA EAEQSAAGGA TGATGEADDD
VVDAEIVDEP VEGEEGDKK
//
