DNAK_PORGI
ID DNAK_PORGI Reviewed; 640 AA.
AC P0C937; Q9ZAD3;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Chaperone protein DnaK;
DE AltName: Full=HSP70;
DE AltName: Full=Heat shock 70 kDa protein;
DE AltName: Full=Heat shock protein 70;
GN Name=dnaK; OrderedLocusNames=PG_1208;
OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=242619;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83;
RX PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA Fraser C.M.;
RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT gingivalis strain W83.";
RL J. Bacteriol. 185:5591-5601(2003).
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; AE015924; AAQ66298.1; -; Genomic_DNA.
DR RefSeq; WP_004583505.1; NC_002950.2.
DR AlphaFoldDB; P0C937; -.
DR SMR; P0C937; -.
DR STRING; 242619.PG_1208; -.
DR EnsemblBacteria; AAQ66298; AAQ66298; PG_1208.
DR KEGG; pgi:PG_1208; -.
DR PATRIC; fig|242619.8.peg.1119; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_10; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR BioCyc; PGIN242619:G1G02-1122-MON; -.
DR Proteomes; UP000000588; 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; 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..640
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000078509"
FT REGION 600..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 640 AA; 68974 MW; 07CB789EFFFE1EBC CRC64;
MGKIIGIDLG TTNSCVSVLE GNEPIVITNS EGKRTTPSVV AFVDGGERKV GDPAKRQAIT
NPTKTIYSIK RFMGETYDQV SREVERVPFK VVRGDNNTPR VDIDGRLYTP QEISAMILQK
MKKTAEDYLG QEVTEAVITV PAYFNDAQRQ ATKEAGEIAG LKVRRIVNEP TAASLAYGLD
KSNKDMKIAV FDLGGGTFDI SILELGDGVF EVKSTNGDTH LGGDDFDHVI IDWLAEEFKS
QEGVDLRQDP MAMQRLKEAA EKAKIELSST SSTEINLPYI MPVNGIPKHL VMTLTRAKFE
QLADRLIQAC VAPCETALKD AGMSRGDIDE VILVGGSTRI PAIQEIVEKI FGKAPSKGVN
PDEVVAVGAA IQGGVLTGEV KDVLLLDVTP LSLGIETMGG VMTRLIDANT TIPTKKSEIF
TTAVDNQPSV EIHVLQGERS LAKDNKSIGR FNLDGIAPAP RQTPQIEVTF DIDANGILNV
TAHDKATGKK QNIRIEASSG LSDDEIKRMK EEAQANAEAD KKEKERIDKI NQADSMIFQT
EKQLKELGDK FPADKKAPID TALDKLKEAH KAQDVAAIDT AMAELQTALS AAGEELYKNA
GAAQGGAQPG PDFGGAQGPS AGDQPSDDKN VTDVDFEEVK