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   16-MAY-2012, entry version 74.
DE   RecName: Full=Anti-adapter protein iraD;
GN   Name=iraD; Synonyms=yjiD; OrderedLocusNames=b4326, JW5782;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=95334362; PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA   Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.,
RA   Blattner F.R.;
RT   "Analysis of the Escherichia coli genome VI: DNA sequence of the
RT   region 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   MEDLINE=97426617; 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.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(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
RT   MG1655 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.,
RA   Storz G.;
RT   "DNA microarray-mediated transcriptional profiling of the Escherichia
RT   coli 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
RT   Escherichia 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
RT   Escherichia coli via the action of multiple anti-adaptors.";
RL   Mol. Microbiol. 68:298-313(2008).
CC   -!- FUNCTION: Inhibits RpoS proteolysis by regulating RssB activity,
CC       thereby increasing the stability of the sigma stress factor RpoS
CC       during oxidative stress. Its effect on RpoS stability is due to
CC       its interaction with RssB, which probably blocks the interaction
CC       of RssB with RpoS, and the consequent delivery of the RssB-RpoS
CC       complex to the ClpXP protein degradation pathway.
CC   -!- SUBUNIT: Interacts with rssB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- INDUCTION: By oxidative stress.
CC   -!- SIMILARITY: Belongs to the GpW/Gp25 family. IraD subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA97222.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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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_000913.2.
DR   ProteinModelPortal; P39375; -.
DR   EnsemblBacteria; EBESCT00000000288; EBESCP00000000288; EBESCG00000000238.
DR   EnsemblBacteria; EBESCT00000015034; EBESCP00000014325; EBESCG00000014094.
DR   GeneID; 948851; -.
DR   GenomeReviews; AP009048_GR; JW5782.
DR   GenomeReviews; U00096_GR; b4326.
DR   KEGG; eco:b4326; -.
DR   PATRIC; 32124254; VBIEscCol129921_4470.
DR   EchoBASE; EB2453; -.
DR   EcoGene; EG12565; yjiD.
DR   eggNOG; NOG15434; -.
DR   HOGENOM; HOG000050876; -.
DR   OMA; WHRTMPQ; -.
DR   ProtClustDB; PRK14128; -.
DR   BioCyc; EcoCyc:G7923-MONOMER; -.
DR   Genevestigator; P39375; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043856; F:anti-sigma factor antagonist activity; IDA:EcoCyc.
DR   GO; GO:0005515; F:protein binding; IPI:EcoCyc.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; IDA:EcoCyc.
DR   GO; GO:0006974; P:response to DNA damage stimulus; IEP:EcoCyc.
DR   HAMAP; MF_02010; IraD; 1; -.
DR   InterPro; IPR023776; Anti-adapt_IraD.
DR   InterPro; IPR007048; Anti-sigma_antagonist_IraD.
DR   Pfam; PF04965; GPW_gp25; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; Reference proteome; Stress response.
FT   CHAIN         1    130       Anti-adapter protein iraD.
FT                                /FTId=PRO_0000169787.
SQ   SEQUENCE   130 AA;  14747 MW;  AA07645C39525D90 CRC64;
     MMRQSLQAVL PEISGNKTSS LRKSVCSDLL TLFNSPHSAL PSLLVSGMPE WQVHNPSDKH
     LQSWYCRQLR SALLFHEPRI AALQVNLKEA YCHTLAISLE IMLYHDDEPL TFDLVWDNGG
     WRSATLENVS
//