ID A0A124FQU0_9BACT Unreviewed; 630 AA.
AC A0A124FQU0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 13-SEP-2023, entry version 41.
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=XD80_1612 {ECO:0000313|EMBL:KUK57037.1};
OS Synergistales bacterium 53_16.
OC Bacteria; Synergistota; Synergistia; Synergistales.
OX NCBI_TaxID=1635273 {ECO:0000313|EMBL:KUK57037.1, ECO:0000313|Proteomes:UP000053116};
RN [1] {ECO:0000313|Proteomes:UP000053116}
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|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:KUK57037.1}.
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DR EMBL; LGGB01000198; KUK57037.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A124FQU0; -.
DR PATRIC; fig|1635273.3.peg.1888; -.
DR Proteomes; UP000053116; Unassembled WGS sequence.
DR GO; GO:0009579; C:thylakoid; IEA:UniProtKB-KW.
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 InterPro; IPR023222; PsbQ-like_dom_sf.
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 SUPFAM; SSF101112; Oxygen-evolving enhancer protein 3; 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 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}; Thylakoid {ECO:0000256|ARBA:ARBA00023078}.
FT REGION 594..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 196
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 630 AA; 68707 MW; 1147DEC8BBA4D30D CRC64;
MGRTVGIDLG TTNSVVAFME GGRPTVIPNA EGGRTTPSVV AFAKNGERLV GTLAKRQAVL
NPEGTIYSIK RFMGRNYNEV AEEMKIVPYK VVEGPNNSVR VVVGDKQYAP EEISAMILRK
LVQDAEAYLG EKVTDAVITV PAYFNDAQRQ ATKNAGKIAG LNVLRVVNEP TAAALAYGMD
KKENEIVMVF DLGGGTFDVS ILEVGEGLCE VRATSGDTHL GGDNFDKCVV DWLAEEFRKE
QGIDLRNDRQ ALQRLYEAAE KAKCELSSRT STEISLPFIT ADANGPKHLN MTLTRAKFDQ
LTEHLVKRCE GPVKQALKDA KLEAKDISEV ILVGGATRMP SIHELVKSIT GGKQLNMSVN
PDEVVAVGAA VQAGIIKGEV KDVLLLDVTP LSLGIETLGG VMTKIIERNT TIPTRKSQIF
TTAEDNQSAV DVVVLQGERE MARDNRKLGN FRLEGIRPAP RGVPQIEVTF DIDANGILNV
SAKDLDTGKE QKIEITNSTN LDEQEIERMV KEAEQHAEED RRKREWVETR NALETASYQL
EREIGELGDT LPVEEKGRAQ QLVDEAKEAI KNEAEKPRLE ELARQVGEML QKIAQYKQQQ
SAGQETTSGG STGSSGGSDG DVIDADFNEG
//
