ID   IRAD_ECOL6              Reviewed;         127 AA.
AC   Q8FAA2;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Anti-adapter protein IraD {ECO:0000255|HAMAP-Rule:MF_02010};
GN   Name=iraD {ECO:0000255|HAMAP-Rule:MF_02010}; OrderedLocusNames=c5405;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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:0000255|HAMAP-Rule:MF_02010}.
CC   -!- SUBUNIT: Interacts with RssB. {ECO:0000255|HAMAP-Rule:MF_02010}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02010}.
CC   -!- SIMILARITY: Belongs to the GpW/Gp25 family. IraD subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_02010}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN83827.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN83827.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001304530.1; NC_004431.1.
DR   AlphaFoldDB; Q8FAA2; -.
DR   SMR; Q8FAA2; -.
DR   STRING; 199310.c5405; -.
DR   DNASU; 1037225; -.
DR   EnsemblBacteria; AAN83827; AAN83827; c5405.
DR   KEGG; ecc:c5405; -.
DR   eggNOG; COG3518; Bacteria.
DR   HOGENOM; CLU_1977621_0_0_6; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043856; F:anti-sigma factor antagonist activity; IEA:InterPro.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:InterPro.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Cytoplasm; Stress response.
FT   CHAIN           1..127
FT                   /note="Anti-adapter protein IraD"
FT                   /id="PRO_0000337894"
SQ   SEQUENCE   127 AA;  14766 MW;  8AEF897151E4E20C CRC64;
     MMRQSVQTVL PESTGNNTLS LRDSVCRDLF QLFSSPHSPL PILLVSGMPE WQGHNQSDKL
     LQSWYCRQLR SALLFHEPRI AALQVNLKEA YCHELAISLE MMLYHDDEPL TFDLVWQKGS
     WHRTMPQ