ID A0A117LSE3_9FIRM Unreviewed; 632 AA.
AC A0A117LSE3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=XD84_1040 {ECO:0000313|EMBL:KUK64872.1};
OS Desulfotomaculum sp. 46_80.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Desulfotomaculum.
OX NCBI_TaxID=1641375 {ECO:0000313|EMBL:KUK64872.1, ECO:0000313|Proteomes:UP000053828};
RN [1] {ECO:0000313|Proteomes:UP000053828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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:KUK64872.1}.
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DR EMBL; LGGF01000016; KUK64872.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117LSE3; -.
DR PATRIC; fig|1641375.3.peg.642; -.
DR Proteomes; UP000053828; 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; 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};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 595..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 245..272
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 196
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 632 AA; 69032 MW; 74E52BBDE6D35DD1 CRC64;
MAKAVGIDLG TTNSVVAVME GGKPTVIVNA EGSRTTPSVV AFKDDGERLV GQIARRQAAL
NPEKTLFSIK RFIGRRYSEV SEERNLVTYK AVSGPNDAVR FQVGDKNYAP EEISAMILKK
LVDDASKYLG EKVVDAVITV PAYFNDAQRQ STKDAGKIAG LNVLRIINEP TAASLAYGMD
KKNNEMVMVF DLGGGTFDVS ILEVGDGVFE VKSTNGDTHL GGDNFDKEIV NWMADEFKKN
YGIDLRSDKQ ALQRLIEAAE KAKTELSTTL ETNISLPFIT ADASGPKHLD MKLARAKFDD
LTHYLVERCR GPVKTALADA KLSEKDIDEV ILVGGSTRIP AVQKLVREMT GGREPNQGVN
PDEVVAVGAA IQAGVLVGEV KDVVLLDVTP LSLGVETLGG IMSKIIERNT TIPTKRSQIF
TTAEDSQPAV DIHVLQGERE MARDNRSLGQ FKLDGIPLAP RGMPQIEVTF DIDANGILKV
NARDKATAKE QTITITGSTS LVKEEIDRMV RDAEMNTEED KKRKQEVEVR NEADGLAYRV
ERQLKDFQDS IPVHEKARIE QILNDLKTAL KENAPIERVR SLHDDLQQAA YSLSEAVYQK
THGENAAPGP GGPPPGRPKP DDVVDAEFEE KS
//
