DNAK_PSEA6
ID DNAK_PSEA6 Reviewed; 639 AA.
AC Q15UD3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=Patl_1987;
OS Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=342610;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T6c / ATCC BAA-1087;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Karls A.C.,
RA Bartlett D., Higgins B.P., Richardson P.;
RT "Complete sequence of Pseudoalteromonas atlantica T6c.";
RL Submitted (JUN-2006) 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; CP000388; ABG40505.1; -; Genomic_DNA.
DR RefSeq; WP_011574800.1; NC_008228.1.
DR AlphaFoldDB; Q15UD3; -.
DR SMR; Q15UD3; -.
DR STRING; 342610.Patl_1987; -.
DR PRIDE; Q15UD3; -.
DR EnsemblBacteria; ABG40505; ABG40505; Patl_1987.
DR KEGG; pat:Patl_1987; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000001981; 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..639
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059630"
FT REGION 602..639
FT /note="Disordered"
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; 68971 MW; CED96CD637A2F067 CRC64;
MGRIIGIDLG TTNSCVAVLD GEKAKVIENA EGDRTTPSII AYSQDGETLV GQPAKRQAIT
NPKNTLFAIK RLIGRRFEDK EVQRDIDIMP FDIIKADNGD AWVQAKDEKL APPQISAEVL
KKMKKTAEDY LGEEVTAAVI TVPAYFNDSQ RQATKDAGRI AGLEVKRIIN EPTAAALAYG
MDKKKGDSVV AVYDLGGGTF DISIIEIDEA DGEHTFEVLA TNGDTHLGGE DFDNQVINYL
VEEFKKDSGM DLRKDPLAMQ RLKEAGEKAK IELSSAQQTE VNLPYITADA SGPKHLTIKL
TRAKLESLVE KMVKATLEPL KQALADADLS VGDINDIILV GGQTRMPLVQ KYVTEFFGKE
PRKDVNPDEA VAVGAAIQGG VLSGDVKDVL LLDVTPLSLG IETMGGVMTA LIEKNTTVPT
KKSQTFSTAE DNQSAVTVHV LQGERKQAAG NKSLGQFNLE GIRPAQRGAP QIEVTFDIDA
DGILHVSAKD KDTNKEQKIT IKASSGLSDD EVEKMVQDAE ANKEADKQFE EMVQARNQAD
GLIHGTRKQV EEAGDALSDE DKAEIEAAVV ALEEAVKAGE KEAIESKTQE LIQASAKLME
VAQAQQAAAG AEGQPEDASA KQDDDVVDAE FEEVKDDKK