DNAK_MARSD
ID DNAK_MARSD Reviewed; 638 AA.
AC C6BSF2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 60.
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=Desal_1566;
OS Maridesulfovibrio salexigens (strain ATCC 14822 / DSM 2638 / NCIMB 8403 /
OS VKM B-1763) (Desulfovibrio salexigens).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Maridesulfovibrio.
OX NCBI_TaxID=526222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14822 / DSM 2638 / NCIMB 8403 / VKM B-1763;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA Wall J.D., Arkin A.P., Dehal P., Chivian D., Giles B., Hazen T.C.;
RT "Complete sequence of Desulfovibrio salexigens DSM 2638.";
RL Submitted (JUN-2009) 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; CP001649; ACS79628.1; -; Genomic_DNA.
DR RefSeq; WP_015851446.1; NC_012881.1.
DR AlphaFoldDB; C6BSF2; -.
DR SMR; C6BSF2; -.
DR STRING; 526222.Desal_1566; -.
DR PRIDE; C6BSF2; -.
DR EnsemblBacteria; ACS79628; ACS79628; Desal_1566.
DR KEGG; dsa:Desal_1566; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_7; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000002601; 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..638
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000205183"
FT REGION 596..638
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 638 AA; 68729 MW; 3BA7141DEF553960 CRC64;
MSKIIGIDLG TTNSCVYVME GKDPKCVTNA EGGRTTPSIV GFTDKERLVG EIAKRQAVTN
PEKTVFAIKR LMGRQASSPE VKKWADHCPY PIVDGKGGDA WVEIEGKKYS PSEVSAIILQ
QLKKDAETYL GETVSEAVIT VPAYFNDSQR QATKDAGRIA GLEVKRIINE PTAASLAYGF
DKKANEKIAV FDLGGGTFDI SILEVGDNVV EVRATNGDTF LGGEDFDNAV IQYLVEEFKR
ENGIDLSADR MALQRLKEAG EKAKKELSTA METEVNLPFI TADQNGPKHL MVKISRAKLE
KLVEDLVERT KVPCQKALKD AGLTAADIDE VILVGGMTRM PLVQQKVQEF FGKEPNRSVN
PDEVVAMGAS IQGGILAGDV KDVLLLDVTP LSLGIETMGG VFTNLIERNT TIPTRKSQVF
TTAADNQPSV SIHVLQGERP MAADNMTLGR FELTGLPAAP RGVPQIEVTF DIDANGIVNV
SAKDMGTGKE QSIQITASSG LSEEDIEKMV KDAESHAEDD KKKQALIEAR NQADSLIYTT
EKSLREVGEN VDAALKSDIE AKIEDLKKVQ DSDDPETIKQ ATDALAQASH KLAEQLYAQQ
NAGAEGAEGP EGAANAGAAG ADDDVVDADF TEVKDEKK