ID A0A290XEP3_9GAMM Unreviewed; 640 AA.
AC A0A290XEP3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=CNR27_09265 {ECO:0000313|EMBL:ATD67600.1};
OS Luteimonas chenhongjianii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Luteimonas.
OX NCBI_TaxID=2006110 {ECO:0000313|EMBL:ATD67600.1, ECO:0000313|Proteomes:UP000218968};
RN [1] {ECO:0000313|Proteomes:UP000218968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=100111 {ECO:0000313|Proteomes:UP000218968};
RA Gui Z.;
RT "Luteimonas liuhanmingii sp.nov., isolated from the intestinal contents of
RT Tibetan Plateau Pika in Yushu, Qinghai Province, China.";
RL Submitted (SEP-2017) 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; CP023406; ATD67600.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A290XEP3; -.
DR KEGG; lum:CNR27_09265; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000218968; Chromosome.
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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000218968};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 604..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..640
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 640 AA; 68531 MW; C2B1FC459337E2E7 CRC64;
MAKIIGIDLG TTNSCVAIMD GGKAKVIENS EGDRTTPSIV AYTKDGEVLV GASAKRQAVT
NPNNTFFAVK RLIGRRFKDA EVQKDIGLVP YKILEHDNGD AWVSTNDGKR LSPQEVSARI
LEKMKKTAED YLGEKVTEAV ITVPAYFNDS QRQATKDAGR IAGLDVKRII NEPTAAALAY
GLDKSGGDRK VAVYDLGGGT FDVSIIEIAE VDGEKQFEVL ATNGDTFLGG EDFDARVIDY
LVEEFNKDQG IDLRKDPLAL QRLKDAAERA KIELSSSQQT EVNLPYVTAD ASGPKHLNIK
LTRAKLEALV EELVRKTIEP CRTALNDAGL RASDINEVIL VGGQTRMPKV QAAVAEFFGK
EPRKDVNPDE AVAIGAAVQG GVLAGDVKDV LLLDVTPLSL GIETLGGVFT KIIEKNTTIP
TKASQTFSTA DDNQSAVTVH VLQGEREQAR YNKSLARFDL TGIEPAPRGM PQVEVSFDID
ANGILHVSAK DKKTGKEQKV EIKAGSGLSE EEIAQMVADA EAHREDDKRF HELVAARNQA
DALVHSTRSA IKDNGEKLPG DLIGNAEAAI ADVETAMKGE DKAQIEAKSK ALEEVAQRLF
AAAGAAGQPG AGGSAGGDAP RSDDVVDAEF TEVKDDEKKS
//
