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IRAD_ECOLI
ID   IRAD_ECOLI              Reviewed;         130 AA.
AC   P39375; Q2M5Y7;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Anti-adapter protein IraD;
GN   Name=iraD; Synonyms=yjiD; OrderedLocusNames=b4326, JW5782;
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   INDUCTION BY HYDROGEN PEROXIDE.
RX   PubMed=11443091; DOI=10.1128/jb.183.15.4562-4570.2001;
RA   Zheng M., Wang X., Templeton L.J., Smulski D.R., LaRossa R.A., Storz G.;
RT   "DNA microarray-mediated transcriptional profiling of the Escherichia coli
RT   response to hydrogen peroxide.";
RL   J. Bacteriol. 183:4562-4570(2001).
RN   [5]
RP   MUTATOR PHENOTYPE.
RX   PubMed=15225322; DOI=10.1111/j.1365-2958.2004.04125.x;
RA   Yang H., Wolff E., Kim M., Diep A., Miller J.H.;
RT   "Identification of mutator genes and mutational pathways in Escherichia
RT   coli using a multicopy cloning approach.";
RL   Mol. Microbiol. 53:283-295(2004).
RN   [6]
RP   FUNCTION IN THE STABILIZATION OF RPOS, AND INTERACTION WITH RSSB.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=18383615; DOI=10.1111/j.1365-2958.2008.06146.x;
RA   Bougdour A., Cunning C., Baptiste P.J., Elliott T., Gottesman S.;
RT   "Multiple pathways for regulation of sigmaS (RpoS) stability in Escherichia
RT   coli via the action of multiple anti-adaptors.";
RL   Mol. Microbiol. 68:298-313(2008).
RN   [7]
RP   MECHANISM OF TRANSLATION REGULATION.
RC   STRAIN=K12 / CF7789;
RX   PubMed=28851853; DOI=10.1128/mbio.01355-17;
RA   Park H., McGibbon L.C., Potts A.H., Yakhnin H., Romeo T., Babitzke P.;
RT   "Translational repression of the RpoS antiadapter IraD by CsrA is mediated
RT   via translational coupling to a short upstream open reading frame.";
RL   MBio 8:0-0(2017).
CC   -!- FUNCTION: Inhibits RpoS proteolysis by regulating RssB activity,
CC       thereby increasing the stability of the sigma stress factor RpoS during
CC       oxidative stress. Its effect on RpoS stability is due to its
CC       interaction with RssB, which probably blocks the interaction of RssB
CC       with RpoS, and the consequent delivery of the RssB-RpoS complex to the
CC       ClpXP protein degradation pathway. {ECO:0000269|PubMed:18383615}.
CC   -!- SUBUNIT: Interacts with RssB. {ECO:0000269|PubMed:18383615}.
CC   -!- INTERACTION:
CC       P39375; P0AEV1: rssB; NbExp=4; IntAct=EBI-6479779, EBI-1122979;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: By oxidative stress (PubMed:11443091). Low expression in
CC       exponential phase, rises in stationary phase, translation is repressed
CC       by CsrA via translational coupling to the upstream open reading frame
CC       IdlP (at protein level) (PubMed:28851853).
CC       {ECO:0000269|PubMed:11443091, ECO:0000269|PubMed:28851853}.
CC   -!- SIMILARITY: Belongs to the GpW/Gp25 family. IraD subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA97222.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U14003; AAA97222.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC77282.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAE78319.1; -; Genomic_DNA.
DR   PIR; S56551; S56551.
DR   RefSeq; NP_418746.4; NC_000913.3.
DR   RefSeq; WP_001309187.1; NZ_SSUV01000012.1.
DR   PDB; 6OD1; X-ray; 2.00 A; B=17-130.
DR   PDBsum; 6OD1; -.
DR   AlphaFoldDB; P39375; -.
DR   SMR; P39375; -.
DR   BioGRID; 4261002; 127.
DR   IntAct; P39375; 1.
DR   STRING; 511145.b4326; -.
DR   PaxDb; P39375; -.
DR   PRIDE; P39375; -.
DR   EnsemblBacteria; AAC77282; AAC77282; b4326.
DR   EnsemblBacteria; BAE78319; BAE78319; BAE78319.
DR   GeneID; 948851; -.
DR   KEGG; ecj:JW5782; -.
DR   KEGG; eco:b4326; -.
DR   PATRIC; fig|1411691.4.peg.2363; -.
DR   EchoBASE; EB2453; -.
DR   eggNOG; COG3518; Bacteria.
DR   HOGENOM; CLU_1977621_0_0_6; -.
DR   OMA; FKEAYCH; -.
DR   PhylomeDB; P39375; -.
DR   BioCyc; EcoCyc:G7923-MON; -.
DR   PRO; PR:P39375; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043856; F:anti-sigma factor antagonist activity; IDA:EcoCyc.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoCyc.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:UniProtKB-UniRule.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; IDA:EcoCyc.
DR   HAMAP; MF_02010; IraD; 1.
DR   InterPro; IPR023776; Anti-adapt_IraD.
DR   InterPro; IPR007048; IraD/Gp25-like.
DR   Pfam; PF04965; GPW_gp25; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Reference proteome; Stress response.
FT   CHAIN           1..130
FT                   /note="Anti-adapter protein IraD"
FT                   /id="PRO_0000169787"
FT   HELIX           20..34
FT                   /evidence="ECO:0007829|PDB:6OD1"
FT   HELIX           42..45
FT                   /evidence="ECO:0007829|PDB:6OD1"
FT   HELIX           47..54
FT                   /evidence="ECO:0007829|PDB:6OD1"
FT   HELIX           59..76
FT                   /evidence="ECO:0007829|PDB:6OD1"
FT   STRAND          80..87
FT                   /evidence="ECO:0007829|PDB:6OD1"
FT   STRAND          96..103
FT                   /evidence="ECO:0007829|PDB:6OD1"
FT   STRAND          110..116
FT                   /evidence="ECO:0007829|PDB:6OD1"
FT   STRAND          118..123
FT                   /evidence="ECO:0007829|PDB:6OD1"
SQ   SEQUENCE   130 AA;  14747 MW;  AA07645C39525D90 CRC64;
     MMRQSLQAVL PEISGNKTSS LRKSVCSDLL TLFNSPHSAL PSLLVSGMPE WQVHNPSDKH
     LQSWYCRQLR SALLFHEPRI AALQVNLKEA YCHTLAISLE IMLYHDDEPL TFDLVWDNGG
     WRSATLENVS
 
 
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