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[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
DOI=10.1128/IAI.68.3.1061-1068.2000; PubMed=10678908 [NCBI, ExPASy, EBI, Israel, Japan]
Vriesema A.J.M.,
Dankert J.,
Zaat S.A.J.;
"A shift from oral to blood pH is a stimulus for adaptive gene expression of Streptococcus gordonii CH1 and induces protection against oxidative stress and enhanced bacterial growth by expression of msrA.";
Infect. Immun. 68:1061-1068(2000).
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JB.01023-07; PubMed=17720781 [NCBI, ExPASy, EBI, Israel, Japan]
Vickerman M.M.,
Iobst S.,
Jesionowski A.M.,
Gill S.R.;
"Genome-wide transcriptional changes in Streptococcus gordonii in response to competence signaling peptide.";
J. Bacteriol. 189:7799-7807(2007).
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- FUNCTION: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine (By similarity). Involved in protection against oxidative stress when the bacterium enters the host bloodstream and required for maximal growth under aerobic and anaerobic conditions.
- 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.
- 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: 311 AA [This is the length of the unprocessed precursor] |
Molecular weight: 35672 Da [This is the MW of the unprocessed precursor] |
CRC64: 7D4B7CAF81DBE692 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MAEIYLAGGC FWGLEEYFSR IEGVKKTTVG YANGQVESTN YQLIHQTDHA ETVHLIYDEK
70 80 90 100 110 120
RVSLREILLY YFRVIDPLSV NKQGNDVGRQ YRTGVYYTNQ ADKAVIEQVF AEQEKQLGQK
130 140 150 160 170 180
IAVELEPLRH YVLAEDYHQD YLKKNPGGYC HINVNDAYQP LVDPGQYEKP TDAELKEQLT
190 200 210 220 230 240
QEQYQVTQLS ATERPFHNAY NATFEEGIYV DVTTGEPLFF AGDKFESGCG WPSFSRPIAR
250 260 270 280 290 300
EVLRYYEDKS HGMERIEVRS RSGNAHLGHV FTDGPESAGG LRYCINSAAL RFIPKEKMEA
310
EGYAYLLQHM K
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Q9LAM9 in FASTA format |
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