ID MSAB1_STRR6 Reviewed; 312 AA. AC P0A3R0; P35593; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 16-JUN-2009, entry version 30. 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=spr1217; OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6). OC Bacteria; Firmicutes; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=171101; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, POSSIBLE RP FUNCTION IN VIRULENCE, AND DISRUPTION PHENOTYPE. RX MEDLINE=96353931; PubMed=8755589; DOI=10.1073/pnas.93.15.7985; RA Wizemann T.M., Moskovitz J., Pearce B.J., Cundell D., Arvidson C.G., RA So M., Weissbach H., Brot N., Masure H.R.; RT "Peptide methionine sulfoxide reductase contributes to the maintenance RT of adhesins in three major pathogens."; RL Proc. Natl. Acad. Sci. U.S.A. 93:7985-7990(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21429245; PubMed=11544234; RX DOI=10.1128/JB.183.19.5709-5717.2001; RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S., RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C., RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., RA LeBlanc D.J., Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., RA McAhren S.M., McHenney M., McLeaster K., Mundy C.W., Nicas T.I., RA Norris F.H., O'Gara M., Peery R.B., Robertson G.T., Rockey P., RA Sun P.-M., Winkler M.E., Yang Y., Young-Bellido M., Zhao G., RA Zook C.A., Baltz R.H., Jaskunas S.R., Rosteck P.R. Jr., Skatrud P.L., RA Glass J.I.; RT "Genome of the bacterium Streptococcus pneumoniae strain R6."; RL J. Bacteriol. 183:5709-5717(2001). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-249. RX MEDLINE=95020625; PubMed=7934910; RX DOI=10.1111/j.1365-2958.1993.tb01233.x; RA Pearce B.J., Yin Y.B., Masure H.R.; RT "Genetic identification of exported proteins in Streptococcus RT pneumoniae."; RL Mol. Microbiol. 9:1037-1050(1993). 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. 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 -!- DISRUPTION PHENOTYPE: Mutant exhibits decreased binding to CC GalNAcbeta1-4Gal containing receptors that are present on type II CC lung cells and vascular endothelial cells. 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U41735; AAC44298.1; -; Genomic_DNA. DR EMBL; AE007317; AAL00021.1; -; Genomic_DNA. DR PIR; H98023; H98023. DR RefSeq; NP_358810.1; -. DR HSSP; P14930; 1L1D. DR GeneID; 934434; -. DR GenomeReviews; AE007317_GR; spr1217. DR KEGG; spr:spr1217; -. DR HOGENOM; P0A3R0; -. DR OMA; P0A3R0; DERVIYL. DR BioCyc; SPNE171101:SPR1217-MON; -. 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 1: Evidence at protein level; 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_0000138518. 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. FT CONFLICT 29 29 V -> G (in Ref. 1; AAC44298). FT CONFLICT 45 45 K -> E (in Ref. 1; AAC44298). FT CONFLICT 52 57 TVQVIY -> AVRVIC (in Ref. 1; AAC44298). FT CONFLICT 61 61 E -> G (in Ref. 1; AAC44298). 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 //