ID   MSRA_BACSU              Reviewed;         177 AA.
AC   P54154;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   04-NOV-2008, entry version 56.
DE   RecName: Full=Peptide methionine sulfoxide reductase msrA;
DE            Short=Protein-methionine-S-oxide reductase;
DE            EC=1.8.4.11;
DE   AltName: Full=Peptide-methionine (S)-S-oxide reductase;
DE            Short=Peptide Met(O) reductase;
GN   Name=msrA; Synonyms=yppP; OrderedLocusNames=BSU21690;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / Marburg;
RX   PubMed=8969496;
RA   Capuano V., Galleron N., Pujic P., Sorokin A., Ehrlich S.D.;
RT   "Organization of the Bacillus subtilis 168 chromosome between kdg and
RT   the attachment site of the SP beta prophage: use of long accurate PCR
RT   and yeast artificial chromosomes for sequencing.";
RL   Microbiology 142:3005-3015(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   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.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   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).
RN   [3]
RP   CHARACTERIZATION.
RX   MEDLINE=98241532; PubMed=9573155;
RA   Hayes C.S., Illades-Aguiar B., Casillas-Martinez L., Setlow P.;
RT   "In vitro and in vivo oxidation of methionine residues in small, acid-
RT   soluble spore proteins from Bacillus species.";
RL   J. Bacteriol. 180:2694-2700(1998).
CC   -!- FUNCTION: Has an important function as a repair enzyme for
CC       proteins that have been inactivated by oxidation. Catalyzes the
CC       reversible oxidation-reduction of methionine sulfoxide in proteins
CC       to methionine. May deal with oxidative damage to alpha/beta-type
CC       SASP in spores.
CC   -!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide +
CC       H(2)O = peptide-L-methionine (S)-S-oxide + thioredoxin.
CC   -!- CATALYTIC ACTIVITY: L-methionine + thioredoxin disulfide + H(2)O =
CC       L-methionine (S)-S-oxide + thioredoxin.
CC   -!- SIMILARITY: Belongs to the msrA Met sulfoxide reductase family.
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DR   EMBL; L77246; AAA96647.1; -; Genomic_DNA.
DR   EMBL; Z99115; CAB14087.1; -; Genomic_DNA.
DR   PIR; E69940; E69940.
DR   RefSeq; NP_390052.1; -.
DR   HSSP; P27110; 1FF3.
DR   GeneID; 939099; -.
DR   GenomeReviews; AL009126_GR; BSU21690.
DR   KEGG; bsu:BSU21690; -.
DR   NMPDR; fig|224308.1.peg.2175; -.
DR   SubtiList; BG11627; msrA.
DR   HOGENOM; P54154; -.
DR   BioCyc; BSUB224308:BSU2170-MON; -.
DR   GO; GO:0008113; F:peptide-methionine-(S)-S-oxide reductase ac...; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006464; P:protein modification process; IEA:HAMAP.
DR   HAMAP; MF_01401; -; 1.
DR   InterPro; IPR002569; MsrA.
DR   Gene3D; G3DSA:3.30.1060.10; MsrA; 1.
DR   Pfam; PF01625; PMSR; 1.
DR   ProDom; PD003489; PMSR; 1.
DR   TIGRFAMs; TIGR00401; msrA; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Oxidoreductase.
FT   CHAIN         1    177       Peptide methionine sulfoxide reductase
FT                                msrA.
FT                                /FTId=PRO_0000138530.
FT   ACT_SITE     14     14       By similarity.
SQ   SEQUENCE   177 AA;  20182 MW;  DFEA7ADF34357D03 CRC64;
     MSEKKEIATF AGGCFWCMVK PFDEQPGIEK VVSGYTGGHT ENPTYEEVCS ETTGHREAVQ
     ITFHPDVFPY EKLLELFWQQ IDPTDAGGQF ADRGSSYRAA IFYHNDKQKE LAEASKQRLA
     ESGIFKDPIV TDILKAEPFY EAEGYHQHFY KKNPAHYQRY RTGSGRAGFI SEHWGAK
//