ID   DNAK2_PHOPR             Reviewed;         641 AA.
AC   Q6LS31;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Chaperone protein DnaK 2 {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=HSP70 2 {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=Heat shock 70 kDa protein 2 {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=Heat shock protein 70 2 {ECO:0000255|HAMAP-Rule:MF_00332};
GN   Name=dnaK2 {ECO:0000255|HAMAP-Rule:MF_00332}; OrderedLocusNames=PBPRA1484;
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=298386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9;
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(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; CR378667; CAG19895.1; -; Genomic_DNA.
DR   RefSeq; WP_011218217.1; NC_006370.1.
DR   AlphaFoldDB; Q6LS31; -.
DR   SMR; Q6LS31; -.
DR   STRING; 298386.PBPRA1484; -.
DR   EnsemblBacteria; CAG19895; CAG19895; PBPRA1484.
DR   KEGG; ppr:PBPRA1484; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; DKMVLQR; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000593; Chromosome 1.
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..641
FT                   /note="Chaperone protein DnaK 2"
FT                   /id="PRO_0000225993"
FT   REGION          601..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        601..628
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         199
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   641 AA;  69251 MW;  BAB9D518A131BD03 CRC64;
     MSKIIGIDLG TTNSCIALLD GDKPRVIENA EGERTTASVI AYTQDGEILV GQPAKRQAVT
     NPKNTLFAIK RLLGRRFEDE EVQRDIEIMP FNIVKADNGD AWVEAKGKKM AAPQVSAEVL
     KKMKKTAEDY LGEEVTGAVI TVPAYFNDAQ RQATKDAGRI AGLDVKRIIN EPTAAALAYG
     LDKQGGERTI AVYDLGGGTF DISIIEIDEV DGEKTFEVLS TNGDTHLGGE DFDNRMINYL
     VGEFKKEQGI DLKSDPLAMQ RVKEAAEKAK IELSSAQQTD VNLPYVTADA AGPKHMNVKV
     TRAKLESLVE DLVQRTLEPL KIALTDANLS ITDITDVILV GGQTRMPMVQ AKVTEFFGKE
     PRKDVNPDEA VAVGAAIQAG VLAGEVKDVL LLDVTPLSLG IETMGGVMTK LIEKNTTIPT
     KANQVFSTAE DNQSAVTIHV LQGERKQSSY NKSLGQFNLE GIQAGSRGTA QIDVTFDLDA
     DGILHVSATD KATNKEQKIT IQASGGLSND DIEKMVQEAE ANKEADKMFE ELVTARNQAD
     QLVHSTRKQV EELGDALPAD EKAKIDTAIA DVETALKGED KAAIDNATQA LMTASQALVQ
     MAQQQAQAQH AQSSQQTNDT TGQSSTDDDV FEAEFEEVKD K