DNAK_EHRRG
ID DNAK_EHRRG Reviewed; 645 AA.
AC Q5FFM4;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
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};
GN OrderedLocusNames=ERGA_CDS_05670;
OS Ehrlichia ruminantium (strain Gardel).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=302409;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gardel;
RX PubMed=16547041; DOI=10.1128/jb.188.7.2533-2542.2006;
RA Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y.,
RA Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.;
RT "Comparative genomic analysis of three strains of Ehrlichia ruminantium
RT reveals an active process of genome size plasticity.";
RL J. Bacteriol. 188:2533-2542(2006).
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; CR925677; CAI28019.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5FFM4; -.
DR SMR; Q5FFM4; -.
DR PRIDE; Q5FFM4; -.
DR EnsemblBacteria; CAI28019; CAI28019; ERGA_CDS_05670.
DR KEGG; erg:ERGA_CDS_05670; -.
DR HOGENOM; CLU_005965_2_1_5; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000000533; 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..645
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000225962"
FT REGION 606..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 201
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 645 AA; 69957 MW; 77C3F1F9668D10E7 CRC64;
MILCRGLFMA VIGIDLGTTN SCVAVMEGGD AKAIENSEGA RTTPSIVAFT DSEVLVGDPA
KRQATTNAKN TIYASKRLIG RRYQDTRDIK TSYDIVSAKN GDAWIKVRDK DYSPSQIGAL
ILEKMKETAE RHLGCKVEKA VITVPAYFDD AQRQATKDAG KIAGLDVIRI INEPTAAALA
YGLNKSDKQK VIAVYDLGGG TFDVSILEIA DGVFEVKSTN GDTMLGGEDF DHAIMEYLMD
DFKKSTGIDL HSDAMAMQRI KEAAEKAKIE LSSRMETDIN LPFLSSDSTG PKHLSLKLTR
ATFENLVSDL VKRTIEPCKK ALKDAGISAD KIDEVVLVGG MTRVPKIIQT VKEFFGKEPH
KGVNPDEVVA IGAAIQGGIL AGDVRDVLLL DVTPLSLGIE TLGGVFTPLI ERNTTIPTKK
SQVFSTAEDG QTAVTIKVFQ GERKMANDNK LLGQFSLEGI PPAPRGMPQI EVTFDIDANG
IVHVSAKDKA SGKEQAIRIQ SSGGLTDDEI QNMIKEAESK AEEDEKRKKF VEVKNNAENL
VHSTEKSLKE HGDKISNADK LDIENAIRDL KDCISKDNIE DTDTMQNKLD HLMKVSMKLG
EALYSNTNNA TAGDNNTTDT GSSSNSDGSK VVDSDYQEID KKDGK