IRAD_SALPA
ID IRAD_SALPA Reviewed; 126 AA.
AC Q5PMN6;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Anti-adapter protein IraD {ECO:0000255|HAMAP-Rule:MF_02010};
GN Name=iraD {ECO:0000255|HAMAP-Rule:MF_02010}; OrderedLocusNames=SPA2998;
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 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=AAV78835.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000026; AAV78835.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_016504930.1; NC_006511.1.
DR AlphaFoldDB; Q5PMN6; -.
DR SMR; Q5PMN6; -.
DR EnsemblBacteria; AAV78835; AAV78835; SPA2998.
DR KEGG; spt:SPA2998; -.
DR HOGENOM; CLU_1977621_0_0_6; -.
DR OMA; FKEAYCH; -.
DR Proteomes; UP000008185; 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..126
FT /note="Anti-adapter protein IraD"
FT /id="PRO_0000337899"
SQ SEQUENCE 126 AA; 14475 MW; 93B0D0F21BC92CB5 CRC64;
MMTPTIPVAL FDRLLVEGIS PHELVRRKLM CLFNSCVVPG GETLPPLLTR GMPEWHEVNV
GDKRVLNWFC RELRAAILRY EPSINMLEVS VKDAHHQTLA LSLEAMLQDE PEPLRLEIAY
SNGRWR