DNAK_PARL1
ID DNAK_PARL1 Reviewed; 639 AA.
AC A7HZ39;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=Plav_3574;
OS Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Parvibaculaceae; Parvibaculum.
OX NCBI_TaxID=402881;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-1 / DSM 13023 / NCIMB 13966;
RX PubMed=22675581; DOI=10.4056/sigs.2215005;
RA Schleheck D., Weiss M., Pitluck S., Bruce D., Land M.L., Han S.,
RA Saunders E., Tapia R., Detter C., Brettin T., Han J., Woyke T., Goodwin L.,
RA Pennacchio L., Nolan M., Cook A.M., Kjelleberg S., Thomas T.;
RT "Complete genome sequence of Parvibaculum lavamentivorans type strain (DS-
RT 1(T)).";
RL Stand. Genomic Sci. 5:298-310(2011).
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; CP000774; ABS65172.1; -; Genomic_DNA.
DR RefSeq; WP_012112432.1; NC_009719.1.
DR AlphaFoldDB; A7HZ39; -.
DR SMR; A7HZ39; -.
DR STRING; 402881.Plav_3574; -.
DR PRIDE; A7HZ39; -.
DR EnsemblBacteria; ABS65172; ABS65172; Plav_3574.
DR KEGG; pla:Plav_3574; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_5; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000006377; 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 Reference proteome; Stress response.
FT CHAIN 1..639
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000072039"
FT REGION 597..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 198
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 639 AA; 68583 MW; B60E00B26519CB68 CRC64;
MAKVIGIDLG TTNSCVAVME GSSAKVIENS EGMRTTPSMV AFTQDGERLV GQSAKRQAVT
NPTNTLFAIK RLIGRSYDDP TTQKDKGMVP YDIVKAPNGD AWVEAHGEKY SPSQISAFIL
QKMKETAESY LGEKVEKAVI TVPAYFNDAQ RQATKDAGKI AGLEVLRIIN EPTAAALAYG
LDKKEGELIA VYDLGGGTFD VSILEIGDGV FEVKSTNGDT FLGGEDFDMR LVNYLADEFK
KENGIDLRGD KLALQRLKEA AEKAKIELSS ASQTEVNLPF ITADASGPKH LTMKITRSKL
EALVADLIQR TIDPCKAALK DAGVTAGQIN EIVLVGGQSR MPKIREAVKQ FFGKEPNMSV
NPDEVVAMGA AIQAGVLQGD VKDVLLLDVT PLSLGIETLG GVFTRLIERN TTIPTKKAQT
FSTAEDNQSA VTIRVFQGER EMAADNKLLG QFDLVGIPAA PRGVPQIEVA FDIDANGIVN
VSAKDKATNK EQTIRIEASG GLSEADIEQM VKDAEAHAEE DKKRREEVET RNHAEALANA
TEKTLQENAD KIGGDVKADV EAALEALRTA LKEGSSEDIK AKMEALTQTS MKMGEALYKS
AQAEAESEAA GGTDASGDDV VDADFEEVDD DKKDQDKSA