ID A0A196NIL7_9SPHN Unreviewed; 640 AA.
AC A0A196NIL7;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=A7X12_10050 {ECO:0000313|EMBL:OAN66951.1};
OS Sphingomonas sp. TDK1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=453247 {ECO:0000313|EMBL:OAN66951.1, ECO:0000313|Proteomes:UP000078445};
RN [1] {ECO:0000313|EMBL:OAN66951.1, ECO:0000313|Proteomes:UP000078445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TDK1 {ECO:0000313|EMBL:OAN66951.1,
RC ECO:0000313|Proteomes:UP000078445};
RA Takahashi S.;
RT "Draft Genome Sequences of Sphingobium sp. strain TCM1 and Sphingomonas sp.
RT strain TDK1, Haloalkyl Organophosphorus Flame Retardant-Degrading
RT Bacteria.";
RL Submitted (MAY-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:OAN66951.1}.
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DR EMBL; LXVY01000002; OAN66951.1; -; Genomic_DNA.
DR RefSeq; WP_064309979.1; NZ_LXVY01000002.1.
DR AlphaFoldDB; A0A196NIL7; -.
DR STRING; 453247.A7X12_10050; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000078445; 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; 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};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 529..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 247..274
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 198
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 640 AA; 68368 MW; 294167939D12D611 CRC64;
MAKVIGIDLG TTNSCVAVME GGKPKVIENV EGARTTPSIV AFAKDGERLI GQPAKRQAVT
NPDNTIFAVK RLIGRRFDDP VTKKDTELVP YTIARGSNGD AWVKAGGEEY SPSQISAFIL
QKMKETAESY LGESVTQAVI TVPAYFNDAQ RQATKDAGKI AGLEVLRIIN EPTAAALAYG
LDKDNNKTIV VYDLGGGTFD ISVLEIGDGV FEVKATNGDT FLGGEDFDNK IVDYLADQFK
KKEGLDLRTD KLALQRLKES AEKAKIELSS AATTEINLPF ITARMEGGAT TPLHLVETIT
RADLERLVDD LIKRTLEPCR KALADAGVKA EAIDEVVLVG GMTRMPKVRQ VVKDFFGKEP
HTGVNPDEVV AIGAAIQAGV LQGDVKDVLL LDVTPLSLGI ETLGGVFTRM IDRNTTIPTK
KSQVYSTADD NQQAVTIRVF QGEREMAADN KMLGQFDLVG IPPAPRGVPQ IEVTFDIDAN
GIVNVSAKDK GTGKEQQIRI QASGGLSDGD IEQMVRDAEK FADEDKKRRA AAEAKNNAES
LVHTTERQLA ENGDKVDASL KGEIEAAIAE TKSAIESGDA DAMTAKAQNL AQVAMKLGQA
IYEKQAAENA SPNAGAAAGS EAGGEEVVDA EFSEVDDNKA
//
