DNAK_RHOBA
ID DNAK_RHOBA Reviewed; 645 AA.
AC Q7UM31;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 2.
DT 03-AUG-2022, entry version 102.
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=RB9105;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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 -!- SEQUENCE CAUTION:
CC Sequence=CAD76086.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX294148; CAD76086.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_868709.1; NC_005027.1.
DR RefSeq; WP_007326035.1; NC_005027.1.
DR AlphaFoldDB; Q7UM31; -.
DR SMR; Q7UM31; -.
DR STRING; 243090.RB9105; -.
DR EnsemblBacteria; CAD76086; CAD76086; RB9105.
DR KEGG; rba:RB9105; -.
DR PATRIC; fig|243090.15.peg.4363; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_0; -.
DR InParanoid; Q7UM31; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000001025; 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..645
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000078526"
FT REGION 509..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..645
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 645 AA; 69423 MW; FBCDF71F3C3A645B CRC64;
MAQGEKIIGI DLGTTNSVVA IMEGSEPKVI PNPEGNRLTP SVVAFTDKQE TIVGEPARRQ
AVTNPKRTVY SAKRFMGRRH NEVQSEEKMV PYGITGGPGD YVKIQVGDSE YTPQEISAKV
LRKLKESAES YLGHKVNKAV ITVPAYFNDA QRQATKDAGQ IAGLEVARII NEPTAAALAY
GLDKKKDESI IVFDLGGGTF DVSVLEVADS GDEEQESRVF QVVSTSGDTH LGGDDFDEAL
INYVASEFQK DNGIDLRNDA MALQRLQEAC EKAKKELSTL PETDINLPFI TMDASGPKHL
TMKITRSKFE ELIDALVERC RGPVLQALKD AGMDPKDIDE VVLVGGSTRV PKVREVVKSI
FGKDPHQGVN PDEVVAVGAA IQGSVLAGDR NDVLLLDVTP LTLGIETEGG VMTALVERNT
TIPAEKKNVF STAADNQTAV TVRVFQGERK MANANRLLAE FNLEDIPAAP RGVPQIEVKF
DIDQNGILSV SAKELKTGKE ANVEIKDSGA LSDSDIEQMQ KDAEANAEED KRQFELVEAR
NKVNQQVYQL EKLMGENDDK LSDDDKAPMN AAIEKVKKAA EGDDLAEIKA ASDELEAASQ
AFSKVLYEKT DAAGEAGADA AGAAGATAGG GDDDDAIDAE FEVKE