ID   MSAB1_STRPN             Reviewed;         312 AA.
AC   P0A3Q9; P35593;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   16-JUN-2009, entry version 28.
DE   RecName: Full=Peptide methionine sulfoxide reductase msrA/msrB 1;
DE   Includes:
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;
DE   Includes:
DE     RecName: Full=Peptide methionine sulfoxide reductase msrB;
DE              EC=1.8.4.12;
DE     AltName: Full=Peptide-methionine (R)-S-oxide reductase;
GN   Name=msrAB1; Synonyms=exp3, msrA; OrderedLocusNames=SP_1359;
OS   Streptococcus pneumoniae.
OC   Bacteria; Firmicutes; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1313;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   MEDLINE=21357209; PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T.,
RA   Hickey E.K., Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C.,
RA   Dougherty B.A., Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
CC   -!- FUNCTION: Has an important function as a repair enzyme for
CC       proteins that have been inactivated by oxidation (By similarity).
CC       Catalyzes the reversible oxidation-reduction of methionine
CC       sulfoxide in proteins to methionine (By similarity).
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   -!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide +
CC       H(2)O = peptide-L-methionine (R)-S-oxide + thioredoxin.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein
CC       (Potential).
CC   -!- SIMILARITY: In the N-terminal section; belongs to the msrA Met
CC       sulfoxide reductase family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the msrB Met
CC       sulfoxide reductase family.
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DR   EMBL; AE005672; AAK75457.1; -; Genomic_DNA.
DR   PIR; H95157; H95157.
DR   RefSeq; NP_345817.1; -.
DR   HSSP; P14930; 1L1D.
DR   GeneID; 931912; -.
DR   GenomeReviews; AE005672_GR; SP_1359.
DR   KEGG; spn:SP_1359; -.
DR   TIGR; SP_1359; -.
DR   HOGENOM; P0A3Q9; -.
DR   OMA; P0A3Q9; DERVIYL.
DR   BRENDA; 1.8.4.11; 600.
DR   BRENDA; 1.8.4.12; 600.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase ac...; IEA:EC.
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_01400; fused; 1.
DR   HAMAP; MF_01401; fused; 1.
DR   InterPro; IPR002579; Methionine_sulphoxide_MsrB.
DR   InterPro; IPR002569; MsrA.
DR   Gene3D; G3DSA:3.30.1060.10; MsrA; 1.
DR   Gene3D; G3DSA:2.170.150.20; MsrB; 1.
DR   Pfam; PF01625; PMSR; 1.
DR   Pfam; PF01641; SelR; 1.
DR   ProDom; PD004057; DUF25; 1.
DR   ProDom; PD003489; PMSR; 1.
DR   TIGRFAMs; TIGR00401; msrA; 1.
DR   TIGRFAMs; TIGR00357; MsrB; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Complete proteome; Membrane; Multifunctional enzyme;
KW   Oxidoreductase.
FT   CHAIN         1    312       Peptide methionine sulfoxide reductase
FT                                msrA/msrB 1.
FT                                /FTId=PRO_0000138517.
FT   REGION        1    155       Peptide methionine sulfoxide reductase.
FT   REGION      172    295       Peptide methionine sulfoxide reductase B.
FT   ACT_SITE     10     10       By similarity.
FT   ACT_SITE    284    284       By similarity.
SQ   SEQUENCE   312 AA;  35703 MW;  6F3873FCE9C1F6E1 CRC64;
     MAEIYLAGGC FWGLEEYFSR ISGVLETSVG YANGQVETTN YQLLKETDHA ETVQVIYDEK
     EVSLREILLY YFRVIDPLSI NQQGNDRGRQ YRTGIYYQDE ADLPAIYTVV QEQERMLGRK
     IAVEVEQLRH YILAEDYHQD YLRKNPSGYC HIDVTDADKP LIDAANYEKP SQEVLKASLS
     EESYRVTQEA ATEAPFTNAY DQTFEEGIYV DITTGEPLFF AKDKFASGCG WPSFSRPISK
     ELIHYYKDLS HGMERIEVRS RSGSAHLGHV FTDGPRELGG LRYCINSASL RFVAKDEMEK
     AGYGYLLPYL NK
//