ID A0A1M7PMK3_9SPHI Unreviewed; 635 AA.
AC A0A1M7PMK3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=SAMN05216524_106208 {ECO:0000313|EMBL:SHN18472.1};
OS Mucilaginibacter sp. OK098.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1855297 {ECO:0000313|EMBL:SHN18472.1, ECO:0000313|Proteomes:UP000184158};
RN [1] {ECO:0000313|EMBL:SHN18472.1, ECO:0000313|Proteomes:UP000184158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK098 {ECO:0000313|EMBL:SHN18472.1,
RC ECO:0000313|Proteomes:UP000184158};
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; FRCM01000006; SHN18472.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M7PMK3; -.
DR STRING; 1855297.SAMN05216524_106208; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000184158; 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; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR PROSITE; PS00297; HSP70_1; 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};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 600..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 635 AA; 68096 MW; EAE18D504ED325C4 CRC64;
MSKIIGIDLG TTNSCVAVME GNEPVVIANS EGKRTTPSVV AFVDNGERKV GDPAKRQAIT
NPTRTIYSIK RFMGNQFNEV TKEASRVPYK VVKGDNNTPR VEIGDRMYTP QEISAMILQK
MKKTAEDFLG HEVTEAVITV PAYFNDAQRQ ATKEAGEIAG LKVRRIINEP TAAALAYGLD
KTHKDMKIAV FDCGGGTHDV SILELGDGVF EVKSTDGDTH LGGDDFDQVI IDWMADEFKS
DEGVDLRKDP MALQRLKESA EKAKIELSSS AQTEINLPYV TASDGVPKHL VKTLTRAKFE
QLADSLIKRT IEPCKSALKN AGLSTSDIDE VILVGGSTRI PAIQEAVEKF FGKAPSKGVN
PDEVVAIGAA IQGGVLTGEV KDVLLLDVTP LSLGIETMGG VMTKLIEANT TIPTKKSEVF
STASDSQPSV EIHILQGERP IASGNRTIGR FHLDGIPPAP RGVPQVEVTF DIDANGILHV
SAKDKATGKE QKIRIEASSG LTDAEIKKMK DEAEANADSD KKAKEEVEKL NAADALIFST
EKQLKEYGDK ISADKKGPIE EGLTKLKEAY AAKNFADIDT AQAELSNAWN VASEEMYKAA
GDAGQAQPGA EGGAGAPHAE GNADTVTDVD FEEVK
//
