DNAK_CHLPB
ID DNAK_CHLPB Reviewed; 642 AA.
AC B3EKT9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=Cphamn1_1707;
OS Chlorobium phaeobacteroides (strain BS1).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=331678;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BS1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Li T., Liu Z., Zhao F.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium phaeobacteroides BS1.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001101; ACE04625.1; -; Genomic_DNA.
DR RefSeq; WP_012475102.1; NC_010831.1.
DR AlphaFoldDB; B3EKT9; -.
DR SMR; B3EKT9; -.
DR STRING; 331678.Cphamn1_1707; -.
DR KEGG; cpb:Cphamn1_1707; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_10; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
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..642
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000119686"
FT REGION 593..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 196
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 642 AA; 69655 MW; 7C25904A5666FFE8 CRC64;
MGKIIGIDLG TTNSCVAVMQ GTKPTVIENS EGYRTTPSMV AFTKNGERLV GHAAKRQAIT
NAENTIFSIK RFMGRKFDEI SNEKKIAPYK VTNVNGEARV EIGDKTYSPQ EISAMILQKM
KQTAEDFLGE KVTEAVITVP AYFNDAQRQA TKDAGKIAGL EVKRIINEPT AASLSYGLDT
KNENEKVAVF DLGGGTFDIS ILELGDGVFE VKSTDGDTHL GGDDFDQKII DFLADEFKKQ
EGIDLRNDMM ALQRLKEAAE KAKVELSSRT DTEINLPFIT ATQEGPKHLV VNLTRSKFEA
LCSDLFDSLI APCKRAIKNS KLKTSEINEV VLVGGSTRIP KVQALVEELF GREPNRSVNP
DEVVAVGAAI QGGVLSGDVS DVLLLDVTPL SLGIETLGGV MTKLIEANTT IPSKKQEVFS
TAADNQTSVE VHVLQGERPM ASDNKTLGRF HLGDIPPAPR GVPQIEVAFD IDSNGILHVS
AKDKATGKEQ SIRIEASGKL NDAEIEKMKE DAKTHAAEDE KRKEAIDLKN SADALIFSTE
KQLGELGDKV PADKKTQLEE ALEKLKEAHK SENVETIKPA MDELNTIWND VASTMYQTPS
GDTPPSEPET GASEESKGGD KTQGDGEVDA EYEVIDGNDK DK