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Reviewed, UniProtKB/Swiss-Prot Q9LAM9 (MSRAB_STRGC)

Last modified June 16, 2009. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peptide methionine sulfoxide reductase msrA/msrB
Including the following 2 domains:
    1- Recommended name:
            Peptide methionine sulfoxide reductase msrA
                Short name=Protein-methionine-S-oxide reductase
              EC=1.8.4.11
        Alternative name(s):
            Peptide-methionine (S)-S-oxide reductase
              Short name=Peptide Met(O) reductase
    2- Recommended name:
            Peptide methionine sulfoxide reductase msrB
              EC=1.8.4.12
        Alternative name(s):
            Peptide-methionine (R)-S-oxide reductase
Gene names
Name: msrAB
Synonyms: msrA
Ordered Locus Names: SGO_0278
OrganismStreptococcus gordonii (strain Challis / ATCC 35105 / CH1 / DL1 / V288) [Complete proteome] [HAMAP]
Taxonomic identifier29390 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length311 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

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. HAMAP MF_01400

L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin. HAMAP MF_01400

Peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin.

Sequence similarities

In the N-terminal section; belongs to the msrA Met sulfoxide reductase family.

In the C-terminal section; belongs to the msrB Met sulfoxide reductase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 311311Peptide methionine sulfoxide reductase msrA/msrB HAMAP MF_01400
PRO_0000138516

Regions

Region1 – 155155Peptide methionine sulfoxide reductase A HAMAP MF_01400
Region172 – 295124Peptide methionine sulfoxide reductase B HAMAP MF_01400

Sites

Active site101 By similarity
Active site2841 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9LAM9-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 7D4B7CAF81DBE692

FASTA31135,672
        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 

« Hide

References

« Hide 'large scale' references
[1]"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."
Vriesema A.J.M., Dankert J., Zaat S.A.J.
Infect. Immun. 68:1061-1068(2000) [PubMed: 10678908] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]"Genome-wide transcriptional changes in Streptococcus gordonii in response to competence signaling peptide."
Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.
J. Bacteriol. 189:7799-7807(2007) [PubMed: 17720781] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AF128264 Genomic DNA. Translation: AAF36477.1.
CP000725 Genomic DNA. Translation: ABV11083.1.
RefSeqYP_001449597.1.

3D structure databases

HSSPHSSP built from PDB template 1L1D based on UniProtKB P14930.
ModBaseSearch...

Genome annotation databases

GeneID5599737.
GenomeReviewsGene locus SGO_0278 in contig CP000725_GR.
KEGGsgo:SGO_0278.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAQ9LAM9. DERVIYL.

Family and domain databases

HAMAPMF_01400. Fused.
[Tree]
MF_01401. Fused.
[Tree]
InterProIPR002579. Methionine_sulphoxide_MsrB.
IPR002569. MsrA.
[Graphical view]
Gene3DG3DSA:3.30.1060.10. MsrA. 1 hit.
G3DSA:2.170.150.20. MsrB. 1 hit.
PfamPF01625. PMSR. 1 hit.
PF01641. SelR. 1 hit.
[Graphical view]
ProDomPD004057. DUF25. 1 hit.
PD003489. PMSR. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00401. msrA. 1 hit.
TIGR00357. MsrB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMSRAB_STRGC
AccessionPrimary (citable) accession number: Q9LAM9
Secondary accession number(s): A8AUY7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: October 1, 2000
Last modified: June 16, 2009
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents