ID   DNAK_PELPB              Reviewed;         640 AA.
AC   B4SDA0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=Ppha_2156;
OS   Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Pelodictyon.
OX   NCBI_TaxID=324925;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5477 / BU-1;
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., Mikhailova N., Liu Z., Li T., Zhao F., Overmann J.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of Pelodictyon phaeoclathratiforme BU-1.";
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; CP001110; ACF44359.1; -; Genomic_DNA.
DR   RefSeq; WP_012508836.1; NC_011060.1.
DR   AlphaFoldDB; B4SDA0; -.
DR   SMR; B4SDA0; -.
DR   STRING; 324925.Ppha_2156; -.
DR   PRIDE; B4SDA0; -.
DR   EnsemblBacteria; ACF44359; ACF44359; Ppha_2156.
DR   KEGG; pph:Ppha_2156; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_10; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000002724; 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..640
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119737"
FT   REGION          487..526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          593..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..526
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        593..612
FT                   /note="Polar 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   640 AA;  69918 MW;  A38E2D26F0050D19 CRC64;
     MGKIIGIDLG TTNSCVSVMQ GSQPTVIENS EGNRTTPSII ALTKTGDRLV GQAAKRQAIT
     NPKNTIFSIK RFMGRKYDEI NDEKKLAPYE IINEGGEARV KINDKIYSPQ EVSAMILQKM
     KQTAEDFLGE KVTEAVITVP AYFNDAQRQA TKDAGRIAGL DVKRIINEPT AAALAYGLDR
     KQTSEKVAVF DLGGGTFDIS VLELGDGVFE VKSTDGDTHL GGDNFDQKII DYIADEFKKQ
     EGIDLRKDAI TLQRLKEAAE KAKIELSSRT DTEINLPFIT ATQEGPKHLV INLTRAKFEA
     LCADLFDKIL DPCRRAIKNS KLEMKEIDEV VLVGGSTRIP KVQALVKDFF GKEPNKSVNP
     DEVVAIGAAI QGGVLKGDVT DVLLLDVTPL SLGIETLGGV MTKLIDANTT IPTRKQEVFS
     TAGDNQTSVE VHVLQGERPM ATDNKTLGRF HLGDIPPSPR GIPQIEVTFD IDSNGILHVS
     AKDKATGKEQ SIKIESSSKL TDAEISKMKE DAKEHAAEDQ KRKEEIDTRN IADSLIFSTE
     KQLKELGDKI PADKRPVLEG SLEKLKEAYK NGTVESLKSA MEELNKEWSE IASHLYQSQG
     PESSQPETAA QSDSGEKSKK NSGDGNVENA EYEVIDGNDK