IRAP_SALPA
ID IRAP_SALPA Reviewed; 86 AA.
AC Q5PFV0;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Anti-adapter protein IraP {ECO:0000255|HAMAP-Rule:MF_01198};
GN Name=iraP {ECO:0000255|HAMAP-Rule:MF_01198}; OrderedLocusNames=SPA2340;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(2004).
CC -!- FUNCTION: Inhibits RpoS proteolysis by regulating RssB activity,
CC thereby increasing the stability of the sigma stress factor RpoS
CC especially during phosphate and magnesium starvation, but also in
CC stationary phase and during nitrogen starvation. Its effect on RpoS
CC stability is due to its interaction with RssB, which probably blocks
CC the interaction of RssB with RpoS, and the consequent delivery of the
CC RssB-RpoS complex to the ClpXP protein degradation pathway.
CC {ECO:0000255|HAMAP-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; CP000026; AAV78225.1; -; Genomic_DNA.
DR RefSeq; WP_001518423.1; NC_006511.1.
DR AlphaFoldDB; Q5PFV0; -.
DR SMR; Q5PFV0; -.
DR EnsemblBacteria; AAV78225; AAV78225; SPA2340.
DR KEGG; spt:SPA2340; -.
DR HOGENOM; CLU_169517_0_0_6; -.
DR OMA; IDTAMIH; -.
DR Proteomes; UP000008185; 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_0000337860"
FT COILED 1..36
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01198"
SQ SEQUENCE 86 AA; 9883 MW; 1F904287C95EB24C CRC64;
MKNLIAELLL KLAQKEEESK ELVAQVEALE IIVTAMLRNM AQNEQEMLIR QVEGALEGVK
PDASVPDHDT ELLRQYVKKL LRHPRH