ID B1C0Y4_9FIRM Unreviewed; 602 AA.
AC B1C0Y4;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
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 ECO:0000313|EMBL:EDS75469.1};
GN ORFNames=CLOSPI_00865 {ECO:0000313|EMBL:EDS75469.1};
OS Thomasclavelia spiroformis DSM 1552.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Thomasclavelia.
OX NCBI_TaxID=428126 {ECO:0000313|EMBL:EDS75469.1, ECO:0000313|Proteomes:UP000004910};
RN [1] {ECO:0000313|EMBL:EDS75469.1, ECO:0000313|Proteomes:UP000004910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1552 {ECO:0000313|EMBL:EDS75469.1,
RC ECO:0000313|Proteomes:UP000004910};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Clostridium spiroforme (DSM 1552).";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDS75469.1, ECO:0000313|Proteomes:UP000004910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1552 {ECO:0000313|EMBL:EDS75469.1,
RC ECO:0000313|Proteomes:UP000004910};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000256|ARBA:ARBA00002290,
CC 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:EDS75469.1}.
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DR EMBL; ABIK02000006; EDS75469.1; -; Genomic_DNA.
DR RefSeq; WP_004609338.1; NZ_DS562846.1.
DR AlphaFoldDB; B1C0Y4; -.
DR STRING; 428126.CLOSPI_00865; -.
DR GeneID; 67387174; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_9; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000004910; 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; 2.
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};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, 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:UP000004910};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 575..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 477..571
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 575..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 173
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 602 AA; 65302 MW; F75B2176C3FB343D CRC64;
MSKIIGIDLG TTNSCVSVME NGEVKVIANP EGNRTTPSVV SFKNGEIIVG EAAKRQAVTN
PDTVMSVKRH MGTSHKEHVN GKDYTPQEIS AMILQNLKAT AEAYLGETVT KAVITVPAYF
NDAQRQATKD AGKIAGLEVE RIINEPTAAA LAFGLDKLDQ EQKVLVYDLG GGTFDVSILD
LADGTFEVLA TAGDNQLGGD DFDQKIMNWV IDEFKKEQGI DLSADKMAMQ RIKEAAEKAK
KDLSGTMQTQ ISLPFISAGA SGPLHLELTL TRAKFDELTR DLVERTEVPV RQALKDAGMD
PTEIHQVLLV GGSTRIPAVQ ESVKRLLGKE PNKSVNPDEV VSMGAAIQGG VIAGDVKDVL
LLDVTPLSLG IETMGGVMTV LIERNTTIPT TKSQIFSTAA DNQPAVDINV LQGERSMAKD
NKQLGLFKLD GIEPAPRGVP QIEVTFSIDV NGIVNVKAKD LKTQKEQSIV IQNSTGLSDE
EIDRMVKEAE ANKAEDEKKR KDIETRNKAE QMINEIDKAL AEQGDKIDAT QKESAQKLRD
ELKTALDNND MATLEAKMSE LEQMAQQMAS YAYQQQGANT NANSTNTAQD DNVVDADFEE
KN
//
