IRAP_ECOLI
ID IRAP_ECOLI Reviewed; 86 AA.
AC P0AAN9; P21831; P77383; Q2MC43;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Anti-adapter protein IraP;
GN Name=iraP; Synonyms=yaiB; OrderedLocusNames=b0382, JW0373;
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;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-86.
RC STRAIN=294;
RX PubMed=3533724; DOI=10.1016/0378-1119(86)90050-8;
RA Chang C.N., Kuang W.-J., Chen E.Y.;
RT "Nucleotide sequence of the alkaline phosphatase gene of Escherichia
RT coli.";
RL Gene 44:121-125(1986).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-86.
RC STRAIN=K12;
RX PubMed=6273802; DOI=10.1093/nar/9.21.5671;
RA Kikuchi Y., Yoda K., Yamasaki M., Tamura G.;
RT "The nucleotide sequence of the promoter and the amino-terminal region of
RT alkaline phosphatase structural gene (phoA) of Escherichia coli.";
RL Nucleic Acids Res. 9:5671-5678(1981).
RN [6]
RP FUNCTION AS INHIBITOR OF RSSB ACTIVITY, INTERACTION WITH RSSB, INDUCTION,
RP GENE NAME, AND MUTAGENESIS OF LEU-9.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=16600914; DOI=10.1101/gad.1400306;
RA Bougdour A., Wickner S., Gottesman S.;
RT "Modulating RssB activity: IraP, a novel regulator of sigma(S) stability in
RT Escherichia coli.";
RL Genes Dev. 20:884-897(2006).
RN [7]
RP INDUCTION BY PPGPP.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=17640895; DOI=10.1073/pnas.0705561104;
RA Bougdour A., Gottesman S.;
RT "ppGpp regulation of RpoS degradation via anti-adaptor protein IraP.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12896-12901(2007).
RN [8]
RP FUNCTION.
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).
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:0000269|PubMed:16600914,
CC ECO:0000269|PubMed:18383615}.
CC -!- SUBUNIT: Interacts with RssB. {ECO:0000269|PubMed:16600914}.
CC -!- INTERACTION:
CC P0AAN9; P0AEV1: rssB; NbExp=3; IntAct=EBI-1116300, EBI-1122979;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: By phosphate and nitrogen starvation, and in stationary
CC phase, via the alarmone ppGpp. {ECO:0000269|PubMed:16600914,
CC ECO:0000269|PubMed:17640895}.
CC -!- SIMILARITY: Belongs to the IraP family. {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; U73857; AAB18106.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73485.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76163.1; -; Genomic_DNA.
DR EMBL; M13345; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; J01659; AAR23118.1; -; Genomic_DNA.
DR PIR; F64766; F64766.
DR RefSeq; NP_414916.1; NC_000913.3.
DR RefSeq; WP_000792970.1; NZ_STEB01000007.1.
DR AlphaFoldDB; P0AAN9; -.
DR SMR; P0AAN9; -.
DR BioGRID; 4261526; 9.
DR BioGRID; 852022; 1.
DR DIP; DIP-48131N; -.
DR IntAct; P0AAN9; 8.
DR STRING; 511145.b0382; -.
DR jPOST; P0AAN9; -.
DR PaxDb; P0AAN9; -.
DR PRIDE; P0AAN9; -.
DR EnsemblBacteria; AAC73485; AAC73485; b0382.
DR EnsemblBacteria; BAE76163; BAE76163; BAE76163.
DR GeneID; 66671319; -.
DR GeneID; 947709; -.
DR KEGG; ecj:JW0373; -.
DR KEGG; eco:b0382; -.
DR PATRIC; fig|1411691.4.peg.1896; -.
DR EchoBASE; EB1236; -.
DR eggNOG; ENOG5032SF1; Bacteria.
DR HOGENOM; CLU_169517_0_0_6; -.
DR OMA; IDTAMIH; -.
DR PhylomeDB; P0AAN9; -.
DR BioCyc; EcoCyc:EG11256-MON; -.
DR PRO; PR:P0AAN9; -.
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:0016036; P:cellular response to phosphate starvation; IMP:EcoCyc.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IDA:EcoCyc.
DR HAMAP; MF_01198; Anti_adapt_IraP; 1.
DR InterPro; IPR019732; SigmaS_Anti-adapt_IraP.
DR Pfam; PF10796; Anti-adapt_IraP; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Reference proteome; Stress response.
FT CHAIN 1..86
FT /note="Anti-adapter protein IraP"
FT /id="PRO_0000168585"
FT COILED 1..36
FT /evidence="ECO:0000255"
FT MUTAGEN 9
FT /note="L->S: Loss of ability to interact with RssB."
FT /evidence="ECO:0000269|PubMed:16600914"
SQ SEQUENCE 86 AA; 9937 MW; 1C2EE018BFB16BEE CRC64;
MKNLIAELLF KLAQKEEESK ELCAQVEALE IIVTAMLRNM AQNDQQRLID QVEGALYEVK
PDASIPDDDT ELLRDYVKKL LKHPRQ
