DNAK_RICRO
ID DNAK_RICRO Reviewed; 627 AA.
AC B0BWH1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=RrIowa_0288;
OS Rickettsia rickettsii (strain Iowa).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=452659;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Iowa;
RX PubMed=18025092; DOI=10.1128/iai.00952-07;
RA Ellison D.W., Clark T.R., Sturdevant D.E., Virtaneva K., Porcella S.F.,
RA Hackstadt T.;
RT "Genomic comparison of virulent Rickettsia rickettsii Sheila Smith and
RT avirulent Rickettsia rickettsii Iowa.";
RL Infect. Immun. 76:542-550(2008).
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; CP000766; ABY72197.1; -; Genomic_DNA.
DR AlphaFoldDB; B0BWH1; -.
DR SMR; B0BWH1; -.
DR STRING; 452659.RrIowa_0288; -.
DR EnsemblBacteria; ABY72197; ABY72197; RrIowa_0288.
DR KEGG; rrj:RrIowa_0288; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_5; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000000796; 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_1000079239"
FT REGION 598..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; 67922 MW; 6E597586FACE3AE7 CRC64;
MGKVIGIDLG TTNSCVAVME GKEPKVIENA EGERTTPSII AFANGEKLVG QSAKRQAVTN
PRNTIYAVKR LIGRNFIDPM VRKDQGIVPY NIVKADNGDA WVEADNNKYS PSQISAFILQ
KMKETAENYL GDKVTQAVIT VPAYFNDAQR QATKDAGKIA GLEVLRIINE PTAAALAYGF
EKSASKTIAV YDLGGGTFDV SILEISDGVF EVKSTNGDTF LGGEDFDTRI LNHLIDVFKK
ENGIDLSKDP LALQRLKEAA EKAKKELSSA VTTDINLPYI TADSSGPKHL NIKFTRAELE
KLVDDLIEKT IEPCRKALQD AGFKASDIQE VVLVGGMTRM PKVQEAVKKF FGREPHKGVN
PDEVVALGAA IQGGVLNKEV TDILLLDVTP LSLGIETLGG VFTRLIDRNT TIPTKKSQVF
STADDNQHAV TIRVFQGERE MAKDNKLLGQ FNLEGIPPAP RGLPQIEVTF DIDANGIVHV
SAKDKASGKE QKVTIQASGG LSDAEIEQMV KDAEQNADED KKRKELIEAK NAADSLVYST
EKTLTEYGDK LSSDDKGAVE EALAALKAVL ESEDTALIKE KTASLTAASM KIGEAMYKAQ
SESQPAAENA TNDEKIVDAD FQDVEKK