DNAK_GLAP5
ID DNAK_GLAP5 Reviewed; 633 AA.
AC B8F7S6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=HAPS_1889;
OS Glaesserella parasuis serovar 5 (strain SH0165) (Haemophilus parasuis).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Glaesserella.
OX NCBI_TaxID=557723;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH0165;
RX PubMed=19074396; DOI=10.1128/jb.01682-08;
RA Yue M., Yang F., Yang J., Bei W., Cai X., Chen L., Dong J., Zhou R.,
RA Jin M., Jin Q., Chen H.;
RT "Complete genome sequence of Haemophilus parasuis SH0165.";
RL J. Bacteriol. 191:1359-1360(2009).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001321; ACL33378.1; -; Genomic_DNA.
DR RefSeq; WP_010787164.1; NC_011852.1.
DR AlphaFoldDB; B8F7S6; -.
DR SMR; B8F7S6; -.
DR STRING; 557723.HAPS_1889; -.
DR EnsemblBacteria; ACL33378; ACL33378; HAPS_1889.
DR KEGG; hap:HAPS_1889; -.
DR PATRIC; fig|557723.8.peg.1873; -.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000006743; 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..633
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000133146"
FT REGION 600..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..618
FT /note="Polar residues"
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 633 AA; 68241 MW; CCA2FBF0A08048BA CRC64;
MGKIIGIDLG TTNSCVAVMD GDKPRVIENA EGARTTPSII AYTDKETLVG QPAKRQAITN
PKNTLFAIKR LIGRRFTDSE VQRDIEIMPF EITKADNGDA WVSVKGEKMA PPQISAEVLK
KMKKTAEDFL GEPVTEAVIT VPAYFSDAQR QATKDAGRIA GLEVKRIINE PTAAALAYGL
DSKKENQIVA VYDLGGGTFD LSIIEIDNLD GEQTFEVRAT NGDTHLGGED FDNRLINYLV
EEFQKEQGVD LRNDSMAMQR VKEAAEKAKI ELSSAQSTEV NLPYITADAT GPKHLVLTVT
RAKLEALVED LVNRSLEPVK VALADAGLSV SEINDVILVG GQTRMPLVQK KVADFFGKEP
RKDVNPDEAV AIGAAVQGGV LAGDVTDVLL LDVTPLSLGI ETMGGVMTTL IEKNTTIPTK
KSQVFSTAED NQSAVTIHVL QGERKRASDN KSLGQFNLEG INPAPRGMPQ IEVTFDIDAN
GIINVSAKDK NTGKEQQIKI QASSGLSDAE IEQMVRDAEA NAEADRKFEE LVQTRNQADA
IAHSTRKQIA EAGSNLADAD KAKIEEAVAA LEKAAKGEDK ADIEAKIEAL VKASEPLIQA
GQAQAQQGQQ QAQQSQKDDG VVDAEFEEVK DNK