DNAK1_PHOPR
ID DNAK1_PHOPR Reviewed; 639 AA.
AC Q6LUA7;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Chaperone protein DnaK 1 {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=HSP70 1 {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock 70 kDa protein 1 {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock protein 70 1 {ECO:0000255|HAMAP-Rule:MF_00332};
GN Name=dnaK1 {ECO:0000255|HAMAP-Rule:MF_00332}; OrderedLocusNames=PBPRA0697;
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; CR378665; CAG19118.1; -; Genomic_DNA.
DR RefSeq; WP_011217464.1; NC_006370.1.
DR AlphaFoldDB; Q6LUA7; -.
DR SMR; Q6LUA7; -.
DR STRING; 298386.PBPRA0697; -.
DR PRIDE; Q6LUA7; -.
DR EnsemblBacteria; CAG19118; CAG19118; PBPRA0697.
DR KEGG; ppr:PBPRA0697; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; ISIKRHM; -.
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; 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..639
FT /note="Chaperone protein DnaK 1"
FT /id="PRO_0000225992"
FT REGION 603..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..639
FT /note="Basic and acidic 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 639 AA; 69359 MW; AB5AE4D04A7600DC CRC64;
MGRIIGIDLG TTNSCVAVLD GDKPRVIENA EGERTTASVV AYTQDGETLV GQPAKRQAVT
NPENTLYAIK RLIGRRFEDE EVQRDLKIMP FKIVKADNGD AWVEAKGQKM AAPQVSAEIL
KKMKKTAEDF LGEEVTAAVI TVPAYFNDAQ RQATKDAGRI AGLEVKRIIN EPTAAALAYG
LDKKGGDRTI AVYDLGGGTF DISIIEIDEV EGEKTFEVLS TNGDTHLGGE DFDNRLINYL
VEEFKKEQGM DLRNDPLAMQ RLKEAAEKAK IELSSAQQTD VNLPYITADA TGPKHMNIKV
TRAKLESLVE DLVQRSLEPL KVALSDAGLS VSEITDIIVV GGQTRMPMVQ AKVAEFFGKE
PRKDVNPDEA VAVGAAVQAG VLAGDVKDVL LLDVTPLSLG IETMGGVMTK LIEKNTTIPT
KANQVFSTAE DNQSAVTIHV LQGERKQSSY NKSLGQFNLE GIQAAARGMP QIEVTFDLDA
DGILHVSAKD KSTGKEQKIT IQSSSGLSEE DIEKMVQEAE ANKESDKKFE ELVTARNQAD
QLIHGTRKQV EEAGEALPAE DKEKIEAAVS ELEEARKAED KEAIDAKVQA LVAASQKLME
IAQQQAQAQQ APGGEGEQEA KQDDNVVDAE FEEVKDEKK