DNAK_HALOH
ID DNAK_HALOH Reviewed; 617 AA.
AC B8CXL1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Chaperone protein DnaK {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=HSP70 {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock 70 kDa protein {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock protein 70 {ECO:0000255|HAMAP-Rule:MF_00332};
GN Name=dnaK {ECO:0000255|HAMAP-Rule:MF_00332}; OrderedLocusNames=Hore_12800;
OS Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562).
OC Bacteria; Firmicutes; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC Halothermothrix.
OX NCBI_TaxID=373903;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H 168 / OCM 544 / DSM 9562;
RX PubMed=19145256; DOI=10.1371/journal.pone.0004192;
RA Mavromatis K., Ivanova N., Anderson I., Lykidis A., Hooper S.D., Sun H.,
RA Kunin V., Lapidus A., Hugenholtz P., Patel B., Kyrpides N.C.;
RT "Genome analysis of the anaerobic thermohalophilic bacterium
RT Halothermothrix orenii.";
RL PLoS ONE 4:E4192-E4192(2009).
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000255|HAMAP-Rule:MF_00332}.
CC -!- INDUCTION: By stress conditions e.g. heat shock. {ECO:0000255|HAMAP-
CC Rule:MF_00332}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000255|HAMAP-Rule:MF_00332}.
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DR EMBL; CP001098; ACL70030.1; -; Genomic_DNA.
DR RefSeq; WP_012636214.1; NC_011899.1.
DR AlphaFoldDB; B8CXL1; -.
DR SMR; B8CXL1; -.
DR STRING; 373903.Hore_12800; -.
DR EnsemblBacteria; ACL70030; ACL70030; Hore_12800.
DR KEGG; hor:Hore_12800; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_9; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000000719; Chromosome.
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 Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
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 PANTHER; PTHR19375; PTHR19375; 2.
DR Pfam; PF00012; HSP70; 2.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR02350; prok_dnaK; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1..617
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000133148"
FT REGION 575..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 174
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 617 AA; 67324 MW; 5BCD644592D8D2AA CRC64;
MGKIIGIDLG TTNSCVAVLE GGEPTVIPNA EGNRTTPSVV AYTKKGERIV GEPAKRQAIT
NPDQTIRSIK RHMGTDHKVT LNDKEYTPQE ISAMILQKLK RDAEEYLGEE VNEAVITVPA
YFTDSQRQAT KDAGRIAGLE VKRIINEPTA AALAYGLDKE GDKTILVFDL GGGTFDVSLL
EIGDGVFEVV ATSGNNHLGG DDFDKRIIDY LAENFKKEYG VDLRDDRMAL QRLKDAAEKA
KKELSSVKTT NINLPFITQT EDGPKHLDID LTRAKFNELT EDLVEKTMGP TRQALKDAGL
EPGDIDEVIL VGGSTRIPAV QEAVKDFIGK APHKGINPDE VVAMGAAIQA GVLAGDVDDI
VLLDVTPLSL GIETLGGVFT KLIERNTTIP TSKKKVFTTA ADNQTSVDIH VLQGERKLAK
DNVTLGRFQL TGIPPAPRGV PQIEVKFDID ANGIVHVSAK DLGTGKKQQI TIKSSSGLSE
DEIEKMVNDA RKHEEEDKKR LEEIEARNEA DSLVYQTEKT LKESGDKVSK DVKDKVEKAK
DELKKALEGD DVDQIKEKTE ALKNELTELS SQLYAQAQQQ AQQQAQGQQG AQTDNQTGQN
DGKTIDVDYE EVDDDDK