DHAR_ECOLI
ID DHAR_ECOLI Reviewed; 639 AA.
AC P76016;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=PTS-dependent dihydroxyacetone kinase operon regulatory protein {ECO:0000303|PubMed:15616579};
GN Name=dhaR {ECO:0000303|PubMed:15616579}; Synonyms=ycgU;
GN OrderedLocusNames=b1201, JW5188;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION.
RX PubMed=15616579; DOI=10.1038/sj.emboj.7600517;
RA Baechler C., Schneider P., Baehler P., Lustig A., Erni B.;
RT "Escherichia coli dihydroxyacetone kinase controls gene expression by
RT binding to transcription factor DhaR.";
RL EMBO J. 24:283-293(2005).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) OF 1-318 IN COMPLEXES WITH DHAL AND
RP DHAK, FUNCTION, INDUCTION, AND SUBUNIT.
RX PubMed=24440518; DOI=10.1016/j.str.2013.11.012;
RA Shi R., McDonald L., Cygler M., Ekiel I.;
RT "Coiled-coil helix rotation selects repressing or activating state of
RT transcriptional regulator DhaR.";
RL Structure 22:478-487(2014).
CC -!- FUNCTION: Positively regulates the dhaKLM operon from a sigma-70
CC promoter. Represses its own expression. {ECO:0000269|PubMed:15616579,
CC ECO:0000269|PubMed:24440518}.
CC -!- SUBUNIT: Homodimer. DhaR forms complexes with DhaK and DhaL-ADP.
CC {ECO:0000269|PubMed:24440518}.
CC -!- INTERACTION:
CC P76016; P76015: dhaK; NbExp=4; IntAct=EBI-9153808, EBI-544485;
CC P76016; P76014: dhaL; NbExp=3; IntAct=EBI-9153808, EBI-9021529;
CC -!- INDUCTION: Represses its own expression. DhaL and DhaK act
CC antagonistically as coactivator and corepressor of the transcription
CC activator by mutually exclusive binding to the sensing domain of DhaR.
CC In the presence of dihydroxyacetone, DhaK that binds dihydroxyacetone
CC has less affinity for DhaR and is displaced by DhaL-ADP, which
CC stimulates DhaR activity. In the absence of dihydroxyacetone, DhaL-ADP
CC is converted by the PTS to DhaL-ATP, which does not bind to DhaR.
CC {ECO:0000269|PubMed:24440518}.
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; U00096; AAC74285.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA36058.2; -; Genomic_DNA.
DR PIR; F64866; F64866.
DR RefSeq; NP_415719.2; NC_000913.3.
DR RefSeq; WP_001350505.1; NZ_LN832404.1.
DR PDB; 4LRX; X-ray; 3.25 A; C/D=1-318.
DR PDB; 4LRY; X-ray; 2.83 A; C/D=1-318.
DR PDB; 4LRZ; X-ray; 2.32 A; E/F/G/H=1-318.
DR PDBsum; 4LRX; -.
DR PDBsum; 4LRY; -.
DR PDBsum; 4LRZ; -.
DR AlphaFoldDB; P76016; -.
DR SMR; P76016; -.
DR BioGRID; 4261628; 15.
DR BioGRID; 850110; 1.
DR DIP; DIP-9438N; -.
DR IntAct; P76016; 2.
DR STRING; 511145.b1201; -.
DR PaxDb; P76016; -.
DR PRIDE; P76016; -.
DR EnsemblBacteria; AAC74285; AAC74285; b1201.
DR EnsemblBacteria; BAA36058; BAA36058; BAA36058.
DR GeneID; 945743; -.
DR KEGG; ecj:JW5188; -.
DR KEGG; eco:b1201; -.
DR PATRIC; fig|1411691.4.peg.1084; -.
DR EchoBASE; EB3661; -.
DR eggNOG; COG3284; Bacteria.
DR HOGENOM; CLU_000445_8_12_6; -.
DR InParanoid; P76016; -.
DR OMA; HVEVTFE; -.
DR PhylomeDB; P76016; -.
DR BioCyc; EcoCyc:G6628-MON; -.
DR PRO; PR:P76016; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:EcoCyc.
DR GO; GO:0006351; P:transcription, DNA-templated; IMP:EcoCyc.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR002197; HTH_Fis.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR002078; Sigma_54_int.
DR InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
DR Pfam; PF02954; HTH_8; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF00158; Sigma54_activat; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
DR PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; ATP-binding; DNA-binding; Glycerol metabolism;
KW Nucleotide-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..639
FT /note="PTS-dependent dihydroxyacetone kinase operon
FT regulatory protein"
FT /id="PRO_0000081320"
FT DOMAIN 52..189
FT /note="GAF"
FT /evidence="ECO:0000305|PubMed:24440518"
FT DOMAIN 203..265
FT /note="PAS"
FT /evidence="ECO:0000305|PubMed:24440518"
FT DOMAIN 327..552
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT REGION 1..318
FT /note="Sensor domain"
FT /evidence="ECO:0000305|PubMed:24440518"
FT BINDING 355..362
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT BINDING 415..424
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT HELIX 14..26
FT /evidence="ECO:0007829|PDB:4LRZ"
FT HELIX 40..49
FT /evidence="ECO:0007829|PDB:4LRZ"
FT HELIX 51..66
FT /evidence="ECO:0007829|PDB:4LRZ"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:4LRZ"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:4LRZ"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:4LRZ"
FT HELIX 91..99
FT /evidence="ECO:0007829|PDB:4LRZ"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:4LRZ"
FT HELIX 117..124
FT /evidence="ECO:0007829|PDB:4LRZ"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:4LRZ"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:4LRZ"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:4LRZ"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:4LRZ"
FT STRAND 143..151
FT /evidence="ECO:0007829|PDB:4LRZ"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:4LRY"
FT STRAND 157..166
FT /evidence="ECO:0007829|PDB:4LRZ"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:4LRZ"
FT HELIX 174..211
FT /evidence="ECO:0007829|PDB:4LRZ"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:4LRZ"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:4LRZ"
FT HELIX 230..235
FT /evidence="ECO:0007829|PDB:4LRZ"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:4LRZ"
FT HELIX 248..251
FT /evidence="ECO:0007829|PDB:4LRZ"
FT HELIX 256..263
FT /evidence="ECO:0007829|PDB:4LRZ"
FT STRAND 268..276
FT /evidence="ECO:0007829|PDB:4LRZ"
FT STRAND 281..293
FT /evidence="ECO:0007829|PDB:4LRZ"
FT STRAND 296..304
FT /evidence="ECO:0007829|PDB:4LRZ"
SQ SEQUENCE 639 AA; 70562 MW; 2DD327F3710E1CA7 CRC64;
MSGAFNNDGR GISPLIATSW ERCNKLMKRE TWNVPHQAQG VTFASIYRRK KAMLTLGQAA
LEDAWEYMAP RECALFILDE TACILSRNGD PQTLQQLSAL GFNDGTYCAE GIIGTCALSL
AAISGQAVKT MADQHFKQVL WNWAFCATPL FDSKGRLTGT IALACPVEQT TAADLPLTLA
IAREVGNLLL TDSLLAETNR HLNQLNALLE SMDDGVISWD EQGNLQFINA QAARVLRLDA
TASQGRAITE LLTLPAVLQQ AIKQAHPLKH VEATFESQHQ FIDAVITLKP IIETQGTSFI
LLLHPVEQMR QLMTSQLGKV SHTFAHMPQD DPQTRRLIHF GRQAARSSFP VLLCGEEGVG
KALLSQAIHN ESERAAGPYI AVNCELYGDA ALAEEFIGGD RTDNENGRLS RLELAHGGTL
FLEKIEYLAV ELQSALLQVI KQGVITRLDA RRLIPIDVKV IATTTADLAM LVEQNRFSRQ
LYYALHAFEI TIPPLRMRRG SIPALVNNKL RSLEKRFSTR LKIDDDALAR LVSCAWPGND
FELYSVIENL ALSSDNGRIR VSDLPEHLFT EQATDDVSAT RLSTSLSFAE VEKEAIINAA
QVTGGRIQEM SALLGIGRTT LWRKMKQHGI DAGQFKRRV
