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[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND POSSIBLE FUNCTION IN VIRULENCE.
DOI=10.1073/pnas.93.15.7985; PubMed=8755589 [NCBI, ExPASy, EBI, Israel, Japan]
Wizemann T.M.,
Moskovitz J.,
Pearce B.J.,
Cundell D.,
Arvidson C.G.,
So M.,
Weissbach H.,
Brot N.,
Masure H.R.;
"Peptide methionine sulfoxide reductase contributes to the maintenance of adhesins in three major pathogens.";
Proc. Natl. Acad. Sci. U.S.A. 93:7985-7990(1996).
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JB.183.19.5709-5717.2001; PubMed=11544234 [NCBI, ExPASy, EBI, Israel, Japan]
Hoskins J.,
Alborn W.E. Jr.,
Arnold J.,
Blaszczak L.C.,
Burgett S.,
DeHoff B.S.,
Estrem S.T.,
Fritz L.,
Fu D.-J.,
Fuller W.,
Geringer C.,
Gilmour R.,
Glass J.S.,
Khoja H.,
Kraft A.R.,
Lagace R.E.,
LeBlanc D.J.,
Lee L.N.,
Lefkowitz E.J., ![]()
Lu J.,
Matsushima P.,
McAhren S.M.,
McHenney M.,
McLeaster K.,
Mundy C.W.,
Nicas T.I.,
Norris F.H.,
O'Gara M.,
Peery R.B.,
Robertson G.T.,
Rockey P.,
Sun P.-M.,
Winkler M.E.,
Yang Y.,
Young-Bellido M.,
Zhao G.,
Zook C.A.,
Baltz R.H.,
Jaskunas S.R.,
Rosteck P.R. Jr.,
Skatrud P.L.,
Glass J.I.;
"Genome of the bacterium Streptococcus pneumoniae strain R6.";
J. Bacteriol. 183:5709-5717(2001).
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[3]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-249.
DOI=10.1111/j.1365-2958.1993.tb01233.x; PubMed=7934910 [NCBI, ExPASy, EBI, Israel, Japan]
Pearce B.J.,
Yin Y.B.,
Masure H.R.;
"Genetic identification of exported proteins in Streptococcus pneumoniae.";
Mol. Microbiol. 9:1037-1050(1993).
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- FUNCTION: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation (By similarity). Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. Mutant with defects in msrA exhibits decreased binding to GalNAcbeta1-4Gal containing receptors that are present on type II lung cells and vascular endothelial cells.
- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin.
- CATALYTIC ACTIVITY: L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin.
- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin.
- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein (Potential).
- SIMILARITY: In the N-terminal section; belongs to the msrA Met sulfoxide reductase family.
- SIMILARITY: In the C-terminal section; belongs to the msrB Met sulfoxide reductase family.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 312 AA [This is the length of the unprocessed precursor] |
Molecular weight: 35703 Da [This is the MW of the unprocessed precursor] |
CRC64: 6F3873FCE9C1F6E1 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MAEIYLAGGC FWGLEEYFSR ISGVLETSVG YANGQVETTN YQLLKETDHA ETVQVIYDEK
70 80 90 100 110 120
EVSLREILLY YFRVIDPLSI NQQGNDRGRQ YRTGIYYQDE ADLPAIYTVV QEQERMLGRK
130 140 150 160 170 180
IAVEVEQLRH YILAEDYHQD YLRKNPSGYC HIDVTDADKP LIDAANYEKP SQEVLKASLS
190 200 210 220 230 240
EESYRVTQEA ATEAPFTNAY DQTFEEGIYV DITTGEPLFF AKDKFASGCG WPSFSRPISK
250 260 270 280 290 300
ELIHYYKDLS HGMERIEVRS RSGSAHLGHV FTDGPRELGG LRYCINSASL RFVAKDEMEK
310
AGYGYLLPYL NK
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P0A3R0 in FASTA format |
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