ID   MRPX_AZOOP              Reviewed;          79 AA.
AC   G8QM64;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Methionine-rich peptide X {ECO:0000303|PubMed:25968643};
DE   Flags: Precursor;
GN   Name=mrpX {ECO:0000303|PubMed:25968643}; OrderedLocusNames=Dsui_0158;
OS   Azospira oryzae (strain ATCC BAA-33 / DSM 13638 / PS) (Dechlorosoma
OS   suillum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Azospira.
OX   NCBI_TaxID=640081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-33 / DSM 13638 / PS;
RX   PubMed=22535943; DOI=10.1128/jb.00124-12;
RA   Byrne-Bailey K.G., Coates J.D.;
RT   "Complete genome sequence of the anaerobic perchlorate-reducing bacterium
RT   Azospira suillum strain PS.";
RL   J. Bacteriol. 194:2767-2768(2012).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, INDUCTION, OXIDATION, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=ATCC BAA-33 / DSM 13638 / PS;
RX   PubMed=25968643; DOI=10.1128/mbio.00233-15;
RA   Melnyk R.A., Youngblut M.D., Clark I.C., Carlson H.K., Wetmore K.M.,
RA   Price M.N., Iavarone A.T., Deutschbauer A.M., Arkin A.P., Coates J.D.;
RT   "Novel mechanism for scavenging of hypochlorite involving a periplasmic
RT   methionine-rich peptide and methionine sulfoxide reductase.";
RL   MBio 6:E00233-E00233(2015).
CC   -!- FUNCTION: Serves as an oxidative stress sink, specifically for chlorite
CC       and hypochlorite. {ECO:0000269|PubMed:25968643}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:25968643}.
CC   -!- INDUCTION: Part of the SigF regulon, induced by chlorite under positive
CC       control of SigF. Part of the probable yedZ1-yedY1-mrpX operon.
CC       Transcript levels are 20- to 60-fold increased when induced by chlorite
CC       or hypochlorite or in the absence of anti-sigma factor NrsF. Not
CC       induced by hydrogen peroxide. {ECO:0000269|PubMed:25968643}.
CC   -!- PTM: Protein is oxidized (possibly on Met residues) when cells are
CC       exposed to chlorite or hypochlorite; initially the protein is highly
CC       oxidized, by 50 minutes all protein is in the reduced form.
CC       {ECO:0000269|PubMed:25968643}.
CC   -!- DISRUPTION PHENOTYPE: Growth somewhat inhibited by chlorite.
CC       {ECO:0000269|PubMed:25968643}.
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DR   EMBL; CP003153; AEV24580.1; -; Genomic_DNA.
DR   RefSeq; WP_014235282.1; NC_016616.1.
DR   AlphaFoldDB; G8QM64; -.
DR   STRING; 640081.Dsui_0158; -.
DR   EnsemblBacteria; AEV24580; AEV24580; Dsui_0158.
DR   KEGG; dsu:Dsui_0158; -.
DR   eggNOG; ENOG5030IAG; Bacteria.
DR   HOGENOM; CLU_148386_1_0_4; -.
DR   OMA; DKMDHMG; -.
DR   Proteomes; UP000005633; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   InterPro; IPR014299; Penta_MxKDx.
DR   TIGRFAMs; TIGR02953; penta_MxKDx; 1.
PE   1: Evidence at protein level;
KW   Oxidation; Periplasm; Reference proteome; Signal; Stress response.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..79
FT                   /note="Methionine-rich peptide X"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5003514902"
FT   REGION          37..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   79 AA;  8953 MW;  304A2BA467E88D1F CRC64;
     MKKLAAVMLT SCLMVAVGAS FADEMKKDDM KKDVMMKKDD MAKDEMKKDS MAKDGMKKDA
     MKKDAMMKKD GMTKDEMKK