ID   YEDZ1_AZOOP             Reviewed;         198 AA.
AC   G8QM62;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Putative protein-methionine-sulfoxide reductase subunit YedZ1 {ECO:0000303|PubMed:25968643};
GN   Name=yedZ1 {ECO:0000303|PubMed:25968643}; OrderedLocusNames=Dsui_0156;
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, INDUCTION, AND DISRUPTION 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: Part of the YedY1-YedZ1 system that may repair oxidized
CC       proteins containing methionine sulfoxide residues (Met-O).
CC       {ECO:0000305|PubMed:25968643}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255}; Multi-pass
CC       membrane protein {ECO:0000255}.
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       {ECO:0000269|PubMed:25968643}.
CC   -!- DISRUPTION PHENOTYPE: Growth somewhat inhibited by chlorite.
CC       {ECO:0000269|PubMed:25968643}.
CC   -!- SIMILARITY: Belongs to the HupC/HyaC/HydC family. {ECO:0000305}.
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DR   EMBL; CP003153; AEV24578.1; -; Genomic_DNA.
DR   RefSeq; WP_014235280.1; NC_016616.1.
DR   AlphaFoldDB; G8QM62; -.
DR   SMR; G8QM62; -.
DR   STRING; 640081.Dsui_0156; -.
DR   EnsemblBacteria; AEV24578; AEV24578; Dsui_0156.
DR   KEGG; dsu:Dsui_0156; -.
DR   eggNOG; COG4117; Bacteria.
DR   HOGENOM; CLU_075520_1_0_4; -.
DR   OMA; WHFFFAW; -.
DR   OrthoDB; 923657at2; -.
DR   Proteomes; UP000005633; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR   InterPro; IPR011577; Cyt_b561_bac/Ni-Hgenase.
DR   InterPro; IPR016174; Di-haem_cyt_TM.
DR   Pfam; PF01292; Ni_hydr_CYTB; 1.
DR   SUPFAM; SSF81342; SSF81342; 1.
PE   2: Evidence at transcript level;
KW   Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW   Stress response; Transmembrane; Transmembrane helix.
FT   CHAIN           1..198
FT                   /note="Putative protein-methionine-sulfoxide reductase
FT                   subunit YedZ1"
FT                   /id="PRO_0000440887"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        63..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        124..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   198 AA;  22355 MW;  9217A1CEB9C2DF72 CRC64;
     MSKEIYAIHP PWLRVTHWLY VVAVVILVMS GWRIYDASPF FPFFIPKEIT LGGWLGGALQ
     WHFAAMWLLA VNGLIYLFFN IFSGRLWHKF FPLSLRAIVA DLLDALKGKL SHADLSHYNA
     LQRAAYLFAI ADIIVIVLSG LVLWKSVQFP ILRELLGGYE AARRVHFIGM SALVAFVGVH
     VAMVALVPRT LIAMIRGH