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YJIE_ECOLI
ID   YJIE_ECOLI              Reviewed;         303 AA.
AC   P39376; Q2M5Y6;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=HTH-type transcriptional regulator YjiE;
DE   AltName: Full=Hypochlorite-response regulator protein YjiE;
DE   AltName: Full=Quorum-sensing regulator protein D;
GN   Name=yjiE; Synonyms=qseD; OrderedLocusNames=b4327, JW4290;
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 / MG1655 / ATCC 47076;
RX   PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA   Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT   from 92.8 through 100 minutes.";
RL   Nucleic Acids Res. 23:2105-2119(1995).
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-117.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=7876157; DOI=10.1074/jbc.270.8.4076;
RA   Gary J.D., Clarke S.;
RT   "Purification and characterization of an isoaspartyl dipeptidase from
RT   Escherichia coli.";
RL   J. Biol. Chem. 270:4076-4087(1995).
RN   [5]
RP   POSSIBLE ROLE IN REGULATION OF MOTILITY, DNA-BINDING, INDUCTION, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=K12 / BW25113;
RX   PubMed=20494990; DOI=10.1128/jb.00382-10;
RA   Habdas B.J., Smart J., Kaper J.B., Sperandio V.;
RT   "The LysR-type transcriptional regulator QseD alters type three secretion
RT   in enterohemorrhagic Escherichia coli and motility in K-12 Escherichia
RT   coli.";
RL   J. Bacteriol. 192:3699-3712(2010).
RN   [6]
RP   ROLE IN HYPOCHLORITE RESPONSE, SUBUNIT, DNA-BINDING, INDUCTION, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=K12 / C600 / CR34 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222;
RX   PubMed=22223481; DOI=10.1074/jbc.m111.287219;
RA   Gebendorfer K.M., Drazic A., Le Y., Gundlach J., Bepperling A.,
RA   Kastenmuller A., Ganzinger K.A., Braun N., Franzmann T.M., Winter J.;
RT   "Identification of a hypochlorite-specific transcription factor from
RT   Escherichia coli.";
RL   J. Biol. Chem. 287:6892-6903(2012).
CC   -!- FUNCTION: Protects cells from HOCl (hypochlorite) stress but not
CC       peroxide or diamide stress. Decreases the intracellular load of
CC       reactive oxygen species by up-regulating genes involved in methionine
CC       and cysteine biosynthesis and down-regulating Fur-regulated genes
CC       involved in iron acquisition. Has also been suggested to down-regulate
CC       expression of the flagellar regulon, decreasing motility, but this
CC       activity was not confirmed in a second study (PubMed:22223481).
CC       {ECO:0000269|PubMed:22223481}.
CC   -!- SUBUNIT: Forms dimers, tetramers and possibly dodecameric complexes;
CC       oligomerization may be governed by cellular concentrations. DNA-binding
CC       seems to decrease oligomerization. {ECO:0000269|PubMed:22223481}.
CC   -!- INDUCTION: Transcription increases throughout growth and is maximal
CC       during stationary phase. Is not up-regulated upon exposure to HOCl.
CC       {ECO:0000269|PubMed:20494990, ECO:0000269|PubMed:22223481}.
CC   -!- DISRUPTION PHENOTYPE: Controversial. Hypermotility, up-regulation of
CC       flagellar genes and up-regulation of flagellar protein FliC
CC       (PubMed:20494990). Decreased viability following HOCl stress; no effect
CC       on motility was seen in this study (PubMed:22223481).
CC       {ECO:0000269|PubMed:20494990, ECO:0000269|PubMed:22223481}.
CC   -!- SIMILARITY: Belongs to the LysR transcriptional regulatory family.
CC       {ECO:0000305}.
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DR   EMBL; U14003; AAA97223.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC77283.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE78320.1; -; Genomic_DNA.
DR   EMBL; U15029; AAC43300.1; -; Genomic_DNA.
DR   PIR; S56552; S56552.
DR   RefSeq; NP_418747.1; NC_000913.3.
DR   RefSeq; WP_000340740.1; NZ_STEB01000025.1.
DR   AlphaFoldDB; P39376; -.
DR   SMR; P39376; -.
DR   BioGRID; 4261004; 6.
DR   DIP; DIP-12633N; -.
DR   IntAct; P39376; 3.
DR   STRING; 511145.b4327; -.
DR   jPOST; P39376; -.
DR   PaxDb; P39376; -.
DR   PRIDE; P39376; -.
DR   DNASU; 948852; -.
DR   EnsemblBacteria; AAC77283; AAC77283; b4327.
DR   EnsemblBacteria; BAE78320; BAE78320; BAE78320.
DR   GeneID; 66671789; -.
DR   GeneID; 948852; -.
DR   KEGG; ecj:JW4290; -.
DR   KEGG; eco:b4327; -.
DR   PATRIC; fig|511145.12.peg.4471; -.
DR   EchoBASE; EB2454; -.
DR   eggNOG; COG0583; Bacteria.
DR   HOGENOM; CLU_039613_4_1_6; -.
DR   InParanoid; P39376; -.
DR   OMA; WHVPLEI; -.
DR   PhylomeDB; P39376; -.
DR   BioCyc; EcoCyc:G7924-MON; -.
DR   PRO; PR:P39376; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:EcoCyc.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:EcoCyc.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR005119; LysR_subst-bd.
DR   InterPro; IPR000847; Tscrpt_reg_HTH_LysR.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00126; HTH_1; 1.
DR   Pfam; PF03466; LysR_substrate; 1.
DR   PRINTS; PR00039; HTHLYSR.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS50931; HTH_LYSR; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..303
FT                   /note="HTH-type transcriptional regulator YjiE"
FT                   /id="PRO_0000105807"
FT   DOMAIN          11..68
FT                   /note="HTH lysR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT   DNA_BIND        28..47
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
SQ   SEQUENCE   303 AA;  34711 MW;  C6E6926128C694B0 CRC64;
     MDDCGAILHN IETKWLYDFL TLEKCRNFSQ AAVSRNVSQP AFSRRIRALE QAIGVELFNR
     QVTPLQLSEQ GKIFHSQIRH LLQQLESNLA ELRGGSDYAQ RKIKIAAAHS LSLGLLPSII
     SQMPPLFTWA IEAIDVDEAV DKLREGQSDC IFSFHDEDLL EAPFDHIRLF ESQLFPVCAS
     DEHGEALFNL AQPHFPLLNY SRNSYMGRLI NRTLTRHSEL SFSTFFVSSM SELLKQVALD
     GCGIAWLPEY AIQQEIRSGK LVVLNRDELV IPIQAYAYRM NTRMNPVAER FWRELRELEI
     VLS
 
 
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