ID   IRAP_ESCF3              Reviewed;          86 AA.
AC   P28243; B7LMK3;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Anti-adapter protein IraP {ECO:0000255|HAMAP-Rule:MF_01198};
GN   Name=iraP {ECO:0000255|HAMAP-Rule:MF_01198}; OrderedLocusNames=EFER_2641;
OS   Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS   14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2129542; DOI=10.1093/oxfordjournals.molbev.a040623;
RA   Dubose R.F., Hartl D.L.;
RT   "The molecular evolution of bacterial alkaline phosphatase: correlating
RT   variation among enteric bacteria to experimental manipulations of the
RT   protein.";
RL   Mol. Biol. Evol. 7:547-577(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / JCM
RC   21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
CC   -!- FUNCTION: Inhibits RpoS proteolysis by regulating RssB activity,
CC       thereby increasing the stability of the sigma stress factor RpoS
CC       especially during phosphate starvation, but also in stationary phase
CC       and during nitrogen starvation. Its effect on RpoS stability is due to
CC       its interaction with RssB, which probably blocks the interaction of
CC       RssB with RpoS, and the consequent delivery of the RssB-RpoS complex to
CC       the ClpXP protein degradation pathway. {ECO:0000255|HAMAP-
CC       Rule:MF_01198}.
CC   -!- SUBUNIT: Interacts with RssB. {ECO:0000255|HAMAP-Rule:MF_01198}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01198}.
CC   -!- SIMILARITY: Belongs to the IraP family. {ECO:0000255|HAMAP-
CC       Rule:MF_01198}.
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DR   EMBL; M33966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CU928158; CAQ90136.1; -; Genomic_DNA.
DR   RefSeq; WP_000793043.1; NC_011740.1.
DR   AlphaFoldDB; P28243; -.
DR   SMR; P28243; -.
DR   EnsemblBacteria; CAQ90136; CAQ90136; EFER_2641.
DR   GeneID; 60901429; -.
DR   KEGG; efe:EFER_2641; -.
DR   HOGENOM; CLU_169517_0_0_6; -.
DR   OMA; IDTAMIH; -.
DR   OrthoDB; 2029093at2; -.
DR   BioCyc; EFER585054:EFER_RS13300-MON; -.
DR   Proteomes; UP000000745; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009267; P:cellular response to starvation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01198; Anti_adapt_IraP; 1.
DR   InterPro; IPR019732; SigmaS_Anti-adapt_IraP.
DR   Pfam; PF10796; Anti-adapt_IraP; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; Stress response.
FT   CHAIN           1..86
FT                   /note="Anti-adapter protein IraP"
FT                   /id="PRO_0000168587"
FT   COILED          1..36
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01198"
SQ   SEQUENCE   86 AA;  9664 MW;  B9842EC00FD5C3DB CRC64;
     MKNLISELLI KLAQKEEESK ELVAQVEALE IIVTAMLRNM GQPEQKRVID QIEGALAGVK
     PDASVPDGDT EMLRAYVKKL LRHPRQ