ID   IRAD_ECOHS              Reviewed;         130 AA.
AC   A8A853;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Anti-adapter protein IraD {ECO:0000255|HAMAP-Rule:MF_02010};
GN   Name=iraD {ECO:0000255|HAMAP-Rule:MF_02010}; OrderedLocusNames=EcHS_A4554;
OS   Escherichia coli O9:H4 (strain HS).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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=ABV08707.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000802; ABV08707.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000986204.1; NC_009800.1.
DR   AlphaFoldDB; A8A853; -.
DR   SMR; A8A853; -.
DR   GeneID; 66671790; -.
DR   KEGG; ecx:EcHS_A4554; -.
DR   HOGENOM; CLU_1977621_0_0_6; -.
DR   Proteomes; UP000001123; 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..130
FT                   /note="Anti-adapter protein IraD"
FT                   /id="PRO_0000337896"
SQ   SEQUENCE   130 AA;  14757 MW;  3DAB4DB6D9906291 CRC64;
     MMRQSLQAVL PEISGNKTSL LRKSVCSDIL TLFNSPHSAL PSLLVSGMPE WQVHNQSDKH
     LQSWYCRQLR SALLFHEPRI AALQVNFKEA YCHTLAISLE IMLYHDGEPL TFDLVWDNGG
     WCSAMLENVS