ID A0A1F8CPH3_9BACT Unreviewed; 636 AA.
AC A0A1F8CPH3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 24.
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=A2188_03440 {ECO:0000313|EMBL:OGM77465.1};
OS Candidatus Woesebacteria bacterium RIFOXYA1_FULL_43_9.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1802534 {ECO:0000313|EMBL:OGM77465.1, ECO:0000313|Proteomes:UP000179241};
RN [1] {ECO:0000313|EMBL:OGM77465.1, ECO:0000313|Proteomes:UP000179241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGM77465.1}.
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DR EMBL; MGHU01000018; OGM77465.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8CPH3; -.
DR Proteomes; UP000179241; 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}; 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};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 590..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 498..527
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 604..636
FT /note="Basic and acidic 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 636 AA; 68951 MW; 2A468580C69A200A CRC64;
MSKIVGIDLG TTNSVVAVME AGRPVVIAAS DTGKNTTPSV VEPVKNLVGD VAKRQMILNS
KNTIYSIKRL MGRRADDKEV ERSKKMVPYD IAAGKDDGAG VNVDGKHYTP QEISARILMK
LKKDAEAYLG GKVDQAVITV PAYFDDSQRQ ATKQAGEIAG FKVERIINEP TAAALAYGMD
KKQAHKIAVY DLGGGTFDIS ILELGEGVFE VKSTNGDTHL GGDDFDEVIV QWIIGEFKKE
NSMDLSADRQ ALQRVRDAAE KAKIELSAAS EVEINQPYIT QKDGNPLHLT MKLTRAKLES
LVDELIQKTI KPVEAALKDA KLDAHDIDEV IMVGGMTRMP KVVEVVKNFF GKTPNQSVNP
DEVVAVGAAI QAGVLGGEVK DILLLDVTPL TLGIETLGGV ATPMITRNTT VPTSKTEVFS
TAADNQTQVE IHVSQGERPM SADNKDLGRF VLDGIPPSPR GVPQIEVTFD IDASGILKVA
AKDKASGKTQ NITISGAVGL SDDEVKRMQE EAEKHKEEDK VKQEKIESKN RADAIIGTAE
KALKDGGDKV PAEVKTKVED KIKALKEVLE TGTKEDLDAK TKDLSEVLSS IGEAMYGNQN
AKNENDKKQN EEQPEKSQEK RDDKKEEKVE EGEVVN
//
