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DECR_ECOLI
ID   DECR_ECOLI              Reviewed;         152 AA.
AC   P0ACJ5; P54986; P71209; P77575; Q2MBX9;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=DNA-binding transcriptional activator DecR {ECO:0000303|PubMed:27435271};
GN   Name=decR {ECO:0000303|PubMed:27435271}; Synonyms=ybaO;
GN   OrderedLocusNames=b0447, JW0437;
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 / W3110 / ATCC 27325 / DSM 5911;
RA   Hatada E., Ohmori H., Qiao Y., Tsuji M., Fukuda R.;
RL   Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-55.
RC   STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RA   Patzer S.I., Hantke K.;
RL   Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 126-152.
RC   STRAIN=TAP90 / ATCC 47037;
RX   PubMed=7904973; DOI=10.1016/0378-1119(93)90470-n;
RA   Allikmets R., Gerrard B.C., Court D., Dean M.C.;
RT   "Cloning and organization of the abc and mdl genes of Escherichia coli:
RT   relationship to eukaryotic multidrug resistance.";
RL   Gene 136:231-236(1993).
RN   [7]
RP   IDENTIFICATION.
RA   Robison K., Rudd K.E.;
RL   Unpublished observations (JAN-1996).
RN   [8]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND DNA-BINDING.
RC   STRAIN=K12 / BW25113;
RX   PubMed=27435271; DOI=10.1099/mic.0.000337;
RA   Shimada T., Tanaka K., Ishihama A.;
RT   "Transcription factor DecR (YbaO) controls detoxification of L-cysteine in
RT   Escherichia coli.";
RL   Microbiology 162:1698-1707(2016).
CC   -!- FUNCTION: Plays a role in L-cysteine detoxification. Binds to the
CC       dlsT(yhaO)-yhaM operon promoter in the presence but not absence of L-
CC       cysteine; activates transcription from the dlsT(yhaO)-yhaM operon. No
CC       other DNA target was identified in strain K12 / BW25113. Thiosulfate
CC       does not activate its transcription function. Overexpression doubles
CC       hydrogen sulfide production in the presence of cysteine.
CC       {ECO:0000269|Ref.1}.
CC   -!- DISRUPTION PHENOTYPE: Slightly increased sensitivity to excess L-
CC       cysteine, the effect is more pronounced in M9 minimal medium. Loss of
CC       expression of dlsT(yhaO)-yhaM operon. Cells no longer produce hydrogen
CC       sulfide in the presence of excess cysteine.
CC       {ECO:0000269|PubMed:27435271}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB40203.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; D82943; BAA11651.1; -; Genomic_DNA.
DR   EMBL; U82664; AAB40203.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC73550.2; -; Genomic_DNA.
DR   EMBL; Z54355; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; L08627; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR   EMBL; AP009048; BAE76227.1; -; Genomic_DNA.
DR   RefSeq; NP_414981.4; NC_000913.3.
DR   RefSeq; WP_000884589.1; NZ_STEB01000007.1.
DR   AlphaFoldDB; P0ACJ5; -.
DR   SMR; P0ACJ5; -.
DR   BioGRID; 4260653; 14.
DR   DIP; DIP-11303N; -.
DR   IntAct; P0ACJ5; 3.
DR   STRING; 511145.b0447; -.
DR   jPOST; P0ACJ5; -.
DR   PaxDb; P0ACJ5; -.
DR   PRIDE; P0ACJ5; -.
DR   EnsemblBacteria; AAC73550; AAC73550; b0447.
DR   EnsemblBacteria; BAE76227; BAE76227; BAE76227.
DR   GeneID; 67416478; -.
DR   GeneID; 945091; -.
DR   KEGG; ecj:JW0437; -.
DR   KEGG; eco:b0447; -.
DR   PATRIC; fig|1411691.4.peg.1829; -.
DR   EchoBASE; EB3009; -.
DR   eggNOG; COG1522; Bacteria.
DR   HOGENOM; CLU_091233_0_2_6; -.
DR   InParanoid; P0ACJ5; -.
DR   OMA; HVSGDYD; -.
DR   PhylomeDB; P0ACJ5; -.
DR   BioCyc; EcoCyc:G6247-MON; -.
DR   PRO; PR:P0ACJ5; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0009093; P:cysteine catabolic process; IMP:UniProtKB.
DR   GO; GO:2000144; P:positive regulation of DNA-templated transcription, initiation; IDA:EcoCyc.
DR   GO; GO:0043200; P:response to amino acid; IBA:GO_Central.
DR   CDD; cd00090; HTH_ARSR; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR011991; ArsR-like_HTH.
DR   InterPro; IPR000485; AsnC-type_HTH_dom.
DR   InterPro; IPR011008; Dimeric_a/b-barrel.
DR   InterPro; IPR019888; Tscrpt_reg_AsnC-like.
DR   InterPro; IPR019887; Tscrpt_reg_AsnC/Lrp_C.
DR   InterPro; IPR019885; Tscrpt_reg_HTH_AsnC-type_CS.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF01037; AsnC_trans_reg; 1.
DR   PRINTS; PR00033; HTHASNC.
DR   SMART; SM00344; HTH_ASNC; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF54909; SSF54909; 1.
DR   PROSITE; PS00519; HTH_ASNC_1; 1.
DR   PROSITE; PS50956; HTH_ASNC_2; 1.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..152
FT                   /note="DNA-binding transcriptional activator DecR"
FT                   /id="PRO_0000111747"
FT   DOMAIN          2..63
FT                   /note="HTH asnC-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00319"
FT   DNA_BIND        21..40
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00319"
SQ   SEQUENCE   152 AA;  17437 MW;  8409CEDC4CA3D012 CRC64;
     MLDKIDRKLL ALLQQDCTLS LQALAEAVNL TTTPCWKRLK RLEDDGILIG KVALLDPEKI
     GLGLTAFVLI KTQHHSSEWY CRFVTVVTEM PEVLGFWRMA GEYDYLMRVQ VADMKRYDEF
     YKRLVNSVPG LSDVTSSFAM EQIKYTTSLP IE
 
 
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