DNAK_RICCN
ID DNAK_RICCN Reviewed; 627 AA.
AC Q92J36;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=RC0233;
OS Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=272944;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-613 / Malish 7;
RX PubMed=11557893; DOI=10.1126/science.1061471;
RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL Science 293:2093-2098(2001).
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; AE006914; AAL02771.1; -; Genomic_DNA.
DR PIR; A97729; A97729.
DR RefSeq; WP_010976896.1; NC_003103.1.
DR AlphaFoldDB; Q92J36; -.
DR SMR; Q92J36; -.
DR EnsemblBacteria; AAL02771; AAL02771; RC0233.
DR KEGG; rco:RC0233; -.
DR PATRIC; fig|272944.4.peg.269; -.
DR HOGENOM; CLU_005965_2_4_5; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000000816; 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; 1.
DR Pfam; PF00012; HSP70; 1.
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 Stress response.
FT CHAIN 1..627
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000078529"
FT REGION 597..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..627
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 627 AA; 67909 MW; FE6612C831D5B916 CRC64;
MGKVIGIDLG TTNSCVAVME GKEPKVIENA EGERTTPSII AFANGEKLVG QSAKRQAVTN
PRNTIYAVKR LIGRNFIDPM VRKDQGIVPY NIVKADNGDA WVEADNNKYS PSQISAFILQ
KMKETAENYL GDKVTQAVIT VPAYFNDAQR QATKDAGKIA GLEVLRIINE PTAAALAYGF
EKSASKTIAV YDLGGGTFDV SILEIADGVF EVKSTNGDTF LGGEDFDTRI LNHLIDVFKK
ENGIDLSKDP LALQRLKEAA EKAKKELSSA VTTDINLPYI TADSSGPKHL NIKFTRAELE
KLVDDLIEKT IEPCRKALQD AGFKASDIQE VVLVGGMTRM PKVQEAVKKF FGREPHKGVN
PDEVVALGAA IQGGVLNKEV TDILLLDVTP LSLGIETLGG VFTRLIDRNT TIPTKKSQIF
STADDNQHAV TIRVFQGERE MAKDNKLLGQ FNLEGIPLAP RGLPQIEVTF DIDANGIVHV
SAKDKASGKE QKVTIQASGG LSDAEIEQMV KDAEQNADED KKRKELIEAK NAADSLVYST
EKTLTEYGDK LSSDDKGAVE AALAALKAVL ESEDTALIKE KTESLTAASM KIGEAMYKAQ
SESQPAAESA TNDEKIVDAD FQDVEKK