ID A0A437PWL6_9BACT Unreviewed; 628 AA.
AC A0A437PWL6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 16.
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 ECO:0000313|EMBL:RVU26646.1};
GN ORFNames=EOJ36_01225 {ECO:0000313|EMBL:RVU26646.1};
OS Sandaracinomonas limnophila.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae;
OC Sandaracinomonas.
OX NCBI_TaxID=1862386 {ECO:0000313|EMBL:RVU26646.1, ECO:0000313|Proteomes:UP000282832};
RN [1] {ECO:0000313|EMBL:RVU26646.1, ECO:0000313|Proteomes:UP000282832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSY-15 {ECO:0000313|EMBL:RVU26646.1,
RC ECO:0000313|Proteomes:UP000282832};
RA Chen W.-M.;
RL Submitted (JAN-2019) 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:RVU26646.1}.
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DR EMBL; SACY01000001; RVU26646.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A437PWL6; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000282832; 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; 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:UP000282832};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 599..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 501..528
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 197
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 628 AA; 67590 MW; 7B8A19356EF74936 CRC64;
MGKIIGIDLG TTNSCVAVME GNEAVVIANS EGRRTTPSIV GFLENGERKV GDPAKRQAIT
NPQNTISSVK RFMGKKYSEV GSELKTISYN VEQGNNDTPR VKIGDRLYTP QEISAQILTK
MKQTAEDYLG QTVTEAVITV PAYFNDAERQ ATKEAGQIAG LEVKRIINEP TAAALAYGVD
KQGKDMKIAV FDLGGGTFDV SILELGDGVF EVKSTDGDTH LGGDDFDQVI IDWLAQEFIT
DEGIDLRKDP MALQRLKEAA EKAKIELSAG ASTEINLPYI MPVNGIPKHL VRSLSRAKFE
QLADSLIQRT LEPCRRAMKN ANYTNSDIDE VILVGGSTRI PRIVEEVEKF FGKKPSKGVN
PDEVVAIGAA IQGGVLTGEV KDVLLLDVTP LSLGIETMGG VFTKLIEANT TIPTKKSEVF
STAADNQPSV ELNILQGERP MAKDNRSLGR FHLDGIPSAP RGVPQIEVTF DIDANGILNV
SAKDKGTGKE QKIRIEASSG LTDAEIEKMR NEAKANEASD KIEKEKVEKI NQADSLIFQS
DKQLKEYGEK LSEGNKSAIE AALTELKAAH ASQDLAAIDA GVEKLNNAWQ AASQEMYAAG
DQGGATETAD ANAGGSDAAE DVSFEEVK
//
