DNAK_CERS5
ID DNAK_CERS5 Reviewed; 636 AA.
AC A4WW89;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=Rsph17025_2766;
OS Cereibacter sphaeroides (strain ATCC 17025 / ATH 2.4.3) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=349102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17025 / ATH 2.4.3;
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 Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Richardson P., Mackenzie C., Choudhary M.,
RA Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome of Rhodobacter sphaeroides ATCC 17025.";
RL Submitted (APR-2007) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000661; ABP71653.1; -; Genomic_DNA.
DR AlphaFoldDB; A4WW89; -.
DR SMR; A4WW89; -.
DR STRING; 349102.Rsph17025_2766; -.
DR EnsemblBacteria; ABP71653; ABP71653; Rsph17025_2766.
DR KEGG; rsq:Rsph17025_2766; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_5; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR BioCyc; RSPH349102:G1G8M-2847-MON; -.
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..636
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059649"
FT REGION 601..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 636 AA; 68698 MW; 2BF57267097DE9F1 CRC64;
MAKVIGIDLG TTNSCVAIMD GAQPRVIENS EGARTTPSIV GFTDSERLVG QPAKRQAVTN
PSNTVFAVKR LIGRRVGDAE VEKDKKLVPY AIVNGGNGDA WVEVRGEKYS PSQISAFILQ
KMKETAEAYL GESVTQAVIT VPAYFNDAQR QATKDAGKIA GLEVLRIINE PTAAALAYGL
DKKDTKTIAV YDLGGGTFDI TILEIDDGLF EVKSTNGDTF LGGEDFDMRI VNYLADEFKK
EHGVDLTLDK MALQRLKEAA EKAKIELSSS QQTEINQPFI SMDRNTGQPL HMVMKLTRAK
LESLVADLIK KSLKPCEAAL KDAGVSKSDI DEVVLVGGMT RMPRVVEEVT KFFGKEPHKG
VNPDEVVALG AAIQAGVLQG DVKDVVLLDV TPLSLGIETL GGVFTRLIDR NTTIPTKKSQ
VFSTAEDNQN AVTIRVFQGE REMAADNKML GQFNLEDIPP APRGMPQIEV TFDIDANGIV
SVSAKDKGTG KSQNITIQAS GGLSDEDIEK MVRDAEANAE ADKKRRELVE TKNQGESLLH
STRKSIEEHG DKVDPSTVEA IELAMGALEE SLKTEDAGKI KGGIQNLTEA AMRLGEAIYK
ASQSETGAAP DEDGPRSVDD DIVDADFEDL GENKRK