ID   DNAK_RHIME              Reviewed;         641 AA.
AC   P42374;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2001, sequence version 2.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Chaperone protein DnaK;
DE   AltName: Full=HSP70;
DE   AltName: Full=Heat shock 70 kDa protein;
DE   AltName: Full=Heat shock protein 70;
GN   Name=dnaK; OrderedLocusNames=R00182; ORFNames=SMc02857;
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 25416;
RX   PubMed=7528198; DOI=10.1128/jb.176.24.7748-7753.1994;
RA   Falah M., Gupta R.S.;
RT   "Cloning of the hsp70 (dnaK) genes from Rhizobium meliloti and Pseudomonas
RT   cepacia: phylogenetic analyses of mitochondrial origin based on a highly
RT   conserved protein sequence.";
RL   J. Bacteriol. 176:7748-7753(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11481430; DOI=10.1073/pnas.161294398;
RA   Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA   Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA   Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA   Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA   Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT   "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT   meliloti strain 1021.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-101.
RC   STRAIN=104A14;
RX   PubMed=9805396; DOI=10.1094/mpmi.1998.11.11.1094;
RA   Summers M.L., Elkins J.G., Elliott B.A., McDermott T.R.;
RT   "Expression and regulation of phosphate stress inducible genes in
RT   Sinorhizobium meliloti.";
RL   Mol. Plant Microbe Interact. 11:1094-1101(1998).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; L36602; AAA64925.1; -; Genomic_DNA.
DR   EMBL; AL591688; CAC41569.1; -; Genomic_DNA.
DR   EMBL; AF074451; AAD42995.1; -; Genomic_DNA.
DR   RefSeq; NP_384288.1; NC_003047.1.
DR   RefSeq; WP_003531910.1; NC_003047.1.
DR   AlphaFoldDB; P42374; -.
DR   SMR; P42374; -.
DR   STRING; 266834.SMc02857; -.
DR   PRIDE; P42374; -.
DR   EnsemblBacteria; CAC41569; CAC41569; SMc02857.
DR   GeneID; 61601661; -.
DR   KEGG; sme:SMc02857; -.
DR   PATRIC; fig|266834.11.peg.1544; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_5; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000001976; 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..641
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078525"
FT   REGION          514..554
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          604..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        514..532
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        611..641
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         198
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        405
FT                   /note="R -> V (in Ref. 1; AAA64925)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        570
FT                   /note="A -> R (in Ref. 1; AAA64925)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        611..614
FT                   /note="DAAA -> MPPP (in Ref. 1; AAA64925)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   641 AA;  68950 MW;  B711D9BD9CC2360C CRC64;
     MAKVIGIDLG TTNSCVSVMD GKDAKVIENA EGARTTPSMV AFTEDGERLV GQPAKRQAVT
     NPENTLFAIK RLIGRTFEDP TTQKDKGMVP YKIVKADNGD AWVEAHGTSY SPSQISAMIL
     QKMKETAESY LGEKVEKAVI TVPAYFNDAQ RQATKDAGKI AGLDVLRIIN EPTAAALAYG
     LDKKEGKTIA VYDLGGGTFD ISVLEIGDGV FEVKSTNGDT FLGGEDFDMR LVEYLASEFK
     KEQGIDLKND KLALQRLKEA AEKAKIELSS SQQTEINLPF ITADASGPKH LTMKLSRAKF
     ESLVEDLIQK TIAPCKAALK DAGVSAAEID EVVLVGGMTR MPKVQETVKQ LFGKEPHKGV
     NPDEVVAMGA AIQAGVLQGD VKDVLLLDVT PLSLGIETLG GVFTRLIERN TTIPTKKSQV
     FSTADDNQSA VTIRVSQGER EMAADNKLLG QFDLVGIPPA PRGVPQIEVT FDIDANGIVQ
     VSAKDKGTGK EHQIRIQASG GLSDAEIEKM VKDAEANAEA DKKRREGVEA KNQAESLVHS
     SEKSLQEHGD KVSETDRKAI EDAIAALKSA VEVSEPDAED IKAKTNTLME VSMKLGQAIY
     EAQQTDAAHA DAAADAKRSG DDVVDADYEE VKDEDDRKRS A