ID   IPRA_SALTY              Reviewed;         207 AA.
AC   Q8ZRF7;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Inhibitor of hydrogen peroxide resistance {ECO:0000255|HAMAP-Rule:MF_02072, ECO:0000303|PubMed:27246569};
GN   Name=iprA {ECO:0000255|HAMAP-Rule:MF_02072, ECO:0000303|PubMed:27246569};
GN   Synonyms=yaiV {ECO:0000312|EMBL:AAL19328.1};
GN   OrderedLocusNames=STM0374 {ECO:0000312|EMBL:AAL19328.1};
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   FUNCTION, DOMAIN, AND DISRUPTION PHENOTYPE.
RX   PubMed=27246569; DOI=10.1128/jb.00144-16;
RA   Herman A., Serfecz J., Kinnally A., Crosby K., Youngman M., Wykoff D.,
RA   Wilson J.W.;
RT   "The bacterial iprA gene is conserved across Enterobacteriaceae, is
RT   involved in oxidative stress resistance, and influences gene expression in
RT   Salmonella enterica serovar typhimurium.";
RL   J. Bacteriol. 198:2166-2179(2016).
CC   -!- FUNCTION: Involved in oxidative stress resistance. {ECO:0000255|HAMAP-
CC       Rule:MF_02072, ECO:0000269|PubMed:27246569}.
CC   -!- DOMAIN: Deletion of the N- or the C-terminal 10 amino acids abolishes
CC       activity, while a region that includes amino acids 56 to 80 is
CC       dispensable for activity. Contains a predicted HTH motif, which may
CC       bind DNA. {ECO:0000269|PubMed:27246569}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutants display increased resistance to
CC       oxidative stress, increased catalase activity and increased survival in
CC       macrophage cells. Deletion results in the altered expression of 82 and
CC       56 genes in log and stationary phase, respectively.
CC       {ECO:0000269|PubMed:27246569}.
CC   -!- SIMILARITY: Belongs to the IprA family. {ECO:0000255|HAMAP-
CC       Rule:MF_02072, ECO:0000305}.
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DR   EMBL; AE006468; AAL19328.1; -; Genomic_DNA.
DR   RefSeq; NP_459369.1; NC_003197.2.
DR   RefSeq; WP_000950242.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZRF7; -.
DR   SMR; Q8ZRF7; -.
DR   STRING; 99287.STM0374; -.
DR   PaxDb; Q8ZRF7; -.
DR   DNASU; 1251893; -.
DR   EnsemblBacteria; AAL19328; AAL19328; STM0374.
DR   GeneID; 1251893; -.
DR   KEGG; stm:STM0374; -.
DR   PATRIC; fig|99287.12.peg.397; -.
DR   HOGENOM; CLU_080453_0_0_6; -.
DR   OMA; MAEWDET; -.
DR   PhylomeDB; Q8ZRF7; -.
DR   BioCyc; SENT99287:STM0374-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:UniProtKB-UniRule.
DR   CDD; cd00038; CAP_ED; 1.
DR   Gene3D; 2.60.120.10; -; 1.
DR   HAMAP; MF_02072; IprA; 1.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR041687; HTH_46.
DR   InterPro; IPR034719; IprA.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Pfam; PF15977; HTH_46; 1.
DR   SUPFAM; SSF51206; SSF51206; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Stress response.
FT   CHAIN           1..207
FT                   /note="Inhibitor of hydrogen peroxide resistance"
FT                   /id="PRO_0000437676"
FT   DNA_BIND        163..182
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02072, ECO:0000305"
SQ   SEQUENCE   207 AA;  23733 MW;  2878541F5E8C9F1D CRC64;
     MLSLSKPLQE FYRLDKCLSK HGTRFEFVND KEIICSPDES NTHTFVILEG VVSLVRGDKV
     LIGIVQAPFI FGLADGVAKK EAQYKLIAES GCIGYRLSSS QTLAIIEQNQ LWREAFCWIV
     WKSQVLELRD KQLIGNNSYD QIRATLMTMI EWDEELRSRI GVMNYIHQRT RVSRSVVAEV
     LAALRKGNYI EMNKGKLISI NRLPSEY