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DCTR_ECOLI
ID   DCTR_ECOLI              Reviewed;         176 AA.
AC   P37195; Q2M7G9;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=HTH-type transcriptional regulator DctR;
GN   Name=dctR; Synonyms=yhiF; OrderedLocusNames=b3507, JW3475;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=8022277; DOI=10.1111/j.1365-2958.1994.tb00383.x;
RA   Alexander D.M., St John A.C.;
RT   "Characterization of the carbon starvation-inducible and stationary phase-
RT   inducible gene slp encoding an outer membrane lipoprotein in Escherichia
RT   coli.";
RL   Mol. Microbiol. 11:1059-1071(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA   Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT   "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT   from 76.0 to 81.5 minutes.";
RL   Nucleic Acids Res. 22:2576-2586(1994).
RN   [3]
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   [4]
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   [5]
RP   FUNCTION, AND GENE NAME.
RC   STRAIN=K12;
RX   PubMed=9811641; DOI=10.1128/jb.180.22.5855-5859.1998;
RA   Boogerd F.C., Boe L., Michelsen O., Jensen P.R.;
RT   "atp mutants of Escherichia coli fail to grow on succinate due to a
RT   transport deficiency.";
RL   J. Bacteriol. 180:5855-5859(1998).
RN   [6]
RP   INDUCTION.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=12399493; DOI=10.1128/jb.184.22.6225-6234.2002;
RA   Masuda N., Church G.M.;
RT   "Escherichia coli gene expression responsive to levels of the response
RT   regulator EvgA.";
RL   J. Bacteriol. 184:6225-6234(2002).
RN   [7]
RP   INVOLVEMENT IN BIOFILM FORMATION.
RX   PubMed=12900028; DOI=10.1016/s0378-1097(03)00507-x;
RA   Tenorio E., Saeki T., Fujita K., Kitakawa M., Baba T., Mori H., Isono K.;
RT   "Systematic characterization of Escherichia coli genes/ORFs affecting
RT   biofilm formation.";
RL   FEMS Microbiol. Lett. 225:107-114(2003).
RN   [8]
RP   INDUCTION.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=12694615; DOI=10.1046/j.1365-2958.2003.03477.x;
RA   Masuda N., Church G.M.;
RT   "Regulatory network of acid resistance genes in Escherichia coli.";
RL   Mol. Microbiol. 48:699-712(2003).
CC   -!- FUNCTION: May act as a transcriptional regulator of dctA.
CC       {ECO:0000269|PubMed:9811641}.
CC   -!- INTERACTION:
CC       P37195; P0DMC7: rcsB; NbExp=3; IntAct=EBI-562540, EBI-369670;
CC   -!- INDUCTION: By acidic conditions. Could be induced by EvgA via the
CC       induction of YdeO. {ECO:0000269|PubMed:12399493,
CC       ECO:0000269|PubMed:12694615}.
CC   -!- MISCELLANEOUS: Overexpression causes filamentous biofilm formation.
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DR   EMBL; L23635; AAA60371.1; -; Genomic_DNA.
DR   EMBL; U00039; AAB18483.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76532.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77787.1; -; Genomic_DNA.
DR   PIR; S47727; S47727.
DR   RefSeq; NP_417964.1; NC_000913.3.
DR   RefSeq; WP_000478619.1; NZ_SSZK01000042.1.
DR   AlphaFoldDB; P37195; -.
DR   SMR; P37195; -.
DR   BioGRID; 4261143; 13.
DR   BioGRID; 852329; 1.
DR   DIP; DIP-12362N; -.
DR   IntAct; P37195; 10.
DR   STRING; 511145.b3507; -.
DR   jPOST; P37195; -.
DR   PaxDb; P37195; -.
DR   PRIDE; P37195; -.
DR   EnsemblBacteria; AAC76532; AAC76532; b3507.
DR   EnsemblBacteria; BAE77787; BAE77787; BAE77787.
DR   GeneID; 948021; -.
DR   KEGG; ecj:JW3475; -.
DR   KEGG; eco:b3507; -.
DR   PATRIC; fig|1411691.4.peg.3212; -.
DR   EchoBASE; EB1835; -.
DR   eggNOG; COG2197; Bacteria.
DR   HOGENOM; CLU_1522929_0_0_6; -.
DR   OMA; QMQTEDI; -.
DR   BioCyc; EcoCyc:EG11889-MON; -.
DR   PRO; PR:P37195; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:1990451; P:cellular stress response to acidic pH; IMP:EcoCyc.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd06170; LuxR_C_like; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR   InterPro; IPR000792; Tscrpt_reg_LuxR_C.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF00196; GerE; 1.
DR   SMART; SM00421; HTH_LUXR; 1.
DR   SUPFAM; SSF46894; SSF46894; 1.
DR   PROSITE; PS50043; HTH_LUXR_2; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..176
FT                   /note="HTH-type transcriptional regulator DctR"
FT                   /id="PRO_0000184145"
FT   DOMAIN          109..174
FT                   /note="HTH luxR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT   DNA_BIND        133..152
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT   CONFLICT        163..176
FT                   /note="INELVRHQHIDYLV -> DQ (in Ref. 1; AAA60371)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   176 AA;  20408 MW;  F87354C3AB82BB83 CRC64;
     MFLIITRDTM FFTAMKNILS KGNVVHIQNE EEIDVMLHQN AFVIIDTLMN NVFHSNFLTQ
     IERLKPVHVI IFSPFNIKRC LGKVPVTFVP RTITIIDFVA LINGSYCSVP EAAVSLSRKQ
     HQVLSCIANQ MTTEDILEKL KISLKTFYCH KHNIMMILNL KRINELVRHQ HIDYLV
 
 
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