ID   BSAA_BACSU              Reviewed;         160 AA.
AC   P52035;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Glutathione peroxidase homolog BsaA;
DE            EC=1.-.-.-;
GN   Name=bsaA; OrderedLocusNames=BSU21900;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=8969496; DOI=10.1099/13500872-142-11-3005;
RA   Capuano V., Galleron N., Pujic P., Sorokin A., Ehrlich S.D.;
RT   "Organization of the Bacillus subtilis 168 chromosome between kdg and the
RT   attachment site of the SP beta prophage: use of long accurate PCR and yeast
RT   artificial chromosomes for sequencing.";
RL   Microbiology 142:3005-3015(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000305}.
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DR   EMBL; L77246; AAA96626.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14108.1; -; Genomic_DNA.
DR   PIR; E69596; E69596.
DR   RefSeq; NP_390073.1; NC_000964.3.
DR   RefSeq; WP_003230784.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P52035; -.
DR   SMR; P52035; -.
DR   STRING; 224308.BSU21900; -.
DR   PeroxiBase; 3984; BsGPx01_Marburg.
DR   PaxDb; P52035; -.
DR   PRIDE; P52035; -.
DR   EnsemblBacteria; CAB14108; CAB14108; BSU_21900.
DR   GeneID; 939086; -.
DR   KEGG; bsu:BSU21900; -.
DR   PATRIC; fig|224308.179.peg.2392; -.
DR   eggNOG; COG0386; Bacteria.
DR   InParanoid; P52035; -.
DR   OMA; FPMMSKI; -.
DR   PhylomeDB; P52035; -.
DR   BioCyc; BSUB:BSU21900-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd00340; GSH_Peroxidase; 1.
DR   InterPro; IPR000889; Glutathione_peroxidase.
DR   InterPro; IPR029759; GPX_AS.
DR   InterPro; IPR029760; GPX_CS.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11592; PTHR11592; 1.
DR   Pfam; PF00255; GSHPx; 1.
DR   PIRSF; PIRSF000303; Glutathion_perox; 1.
DR   PRINTS; PR01011; GLUTPROXDASE.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
DR   PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR   PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Peroxidase; Reference proteome.
FT   CHAIN           1..160
FT                   /note="Glutathione peroxidase homolog BsaA"
FT                   /id="PRO_0000066649"
FT   ACT_SITE        35
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   160 AA;  18256 MW;  59B21F065634E404 CRC64;
     MSIYHMKVRT ITGKDMTLQP FAGKVLMIVN TASKCGFTSQ LKQLQELYDT YQQEGLEILG
     FPCNQFMNQE PGEEADIQEF CETNYGVTFP MFSKVDVNGK NAHPLFVYLT EHAKGMLGTK
     AIKWNFTKFI VDRNGEIVGR YSPNTNPKEL EDDIVKLLEQ