DNAK_BLOPB
ID DNAK_BLOPB Reviewed; 637 AA.
AC Q493S7;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=BPEN_118;
OS Blochmannia pennsylvanicus (strain BPEN).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX NCBI_TaxID=291272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BPEN;
RX PubMed=16077009; DOI=10.1101/gr.3771305;
RA Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT evolutionary trends among bacterial mutualists of insects.";
RL Genome Res. 15:1023-1033(2005).
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; CP000016; AAZ40758.1; -; Genomic_DNA.
DR RefSeq; WP_011282665.1; NC_007292.1.
DR AlphaFoldDB; Q493S7; -.
DR SMR; Q493S7; -.
DR STRING; 291272.BPEN_118; -.
DR EnsemblBacteria; AAZ40758; AAZ40758; BPEN_118.
DR KEGG; bpn:BPEN_118; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; ISIKRHM; -.
DR BioCyc; CBLO291272:BPEN_RS00575-MON; -.
DR Proteomes; UP000007794; 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..637
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000225941"
FT REGION 600..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 200
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 637 AA; 69839 MW; 33F68AF55302B3C9 CRC64;
MGKIIGIDLG TTNSCVAIIE GNKPRVLENS EGDRTTPSII AYTQDGEILV GQPAKRQSVT
NPKNTLFAIK RLIGRRFQDT EVQRDVNIMP YKIISADNGD AWLDVKGQKM APPQVSAEIL
KKMKKTAEDY LGEQISEAVI TVPAYFNDAQ RQATKDSGRI AGLEVKRIIN EPTAAALAYG
LDKETRGNRT IAVYDLGGGT FDISIIEIDD VDGEKTFEVL STNGDTHLGG EDFDSLLINY
LADEFKKDQR INLYNDPLAM QRLKEAAEKA KIELSASHQT DVNLPYITAD NTGPKHMNIR
VTRAKLESLV EDLVNRTMEP LKVALKDANL SVSNINDVIL VGGQTRMPLV QKKVSEFFRK
EPRRDVNPDE AVAIGAAVQG GVLSGDVKDV LLLDVTPLSL GIETMGGVMT SLIAKNTTIP
TKHSQIFSTA EDNQSAVTIH VLQGERKRAS DNKSLGQFNL DGIAAAMRGI PQIEVTFDID
ADGILHVSAK DKNSGREQKI TIKASSGLNE EEINKMVQEA EANAESDRKF EELVQIRNQA
DHLLHSTKKQ LTEVGDNISL DDKSAIEGAL KELESVIKKE DKNEIESKIQ SLIKVSGKLL
EASQKHQEQS KSQSSNSTSD PNGEVVDAEF EEIKNKK