DNAK_RICAH
ID DNAK_RICAH Reviewed; 627 AA.
AC A8GMF9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=A1C_01330;
OS Rickettsia akari (strain Hartford).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=293614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hartford;
RA Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Dasch G., Eremeeva M.;
RT "Complete genome sequence of Rickettsia akari.";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000847; ABV74584.1; -; Genomic_DNA.
DR RefSeq; WP_012013454.1; NC_009881.1.
DR AlphaFoldDB; A8GMF9; -.
DR SMR; A8GMF9; -.
DR STRING; 293614.A1C_01330; -.
DR EnsemblBacteria; ABV74584; ABV74584; A1C_01330.
DR KEGG; rak:A1C_01330; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_5; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000006830; 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_1000059650"
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; 67745 MW; E525A7324F98429D CRC64;
MGKVIGIDLG TTNSCVAVME GKEPKVIENA EGERTTPSII AFANGEKLVG QSAKRQAVTN
PSNTIYAVKR LIGRNFTDPM VKKDQDIVPY NIVKADNGDA WVEADSNKYS PSQISAFILQ
KMKETAENYL GEKVTQAVIT VPAYFNDAQR QATKDAGKIA GLEVLRIINE PTAAALAYGF
DKAASKTIAV YDLGGGTFDV SILEIGDGVF EVKSTNGDTF LGGEDFDTRI LNHLIDVFKK
ESGIDLRNDP LALQRLKEAA EKAKKELSSA VTTDINLPYI TADSTGPKHL NIKFTRAEFE
KLVDDLIEKT VEPCITALKD AGLKASDIQE VVLVGGMTRM PKVQEAVKKF FGREPHKGVN
PDEVVALGAA IQGGVLNKEV TDILLLDVTP LSLGIETLGG VFTRLIDRNT TIPTKKSQVF
STADDNQHAV TIRVFQGERE MAASNKLLGQ FNLEGIPPAP RGVPQIEVTF DIDVNGIVHV
SAKDKASGKE QKVTIQASGG LSDAEIEQMV KDAEQNAYED KKRKELIEAK NAADSLVYST
EKSLTEYGDK LSSEDKGAAE EALSALKAVL ESEDAALIKE KTERLTAASM KIGEAMYKAQ
SENQPAGENT ANDDKVVDAD FQDVAKK