Peptide methionine sulfoxide reductase msrA
     (Protein-methionine-S-oxide reductase)
     (EC 1.8.4.11)
     (Peptide-methionine (S)-S-oxide reductase)
     (Peptide Met(O) reductase)
Peptide methionine sulfoxide reductase msrB
     (EC 1.8.4.12)
     (Peptide-methionine (R)-S-oxide reductase)

Gene name

	Name:	msrAB
	Synonyms:	msrA
	OrderedLocusNames:	SPy_1557, M5005_Spy1282

From

Streptococcus pyogenes serotype M1

[TaxID: 301447]

[HAMAP proteome]

Taxonomy

Bacteria; Firmicutes; Lactobacillales; Streptococcaceae; Streptococcus.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700294 / SF370 / Serotype M1;
DOI=10.1073/pnas.071559398; PubMed=11296296 [NCBI, ExPASy, EBI, Israel, Japan]
Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K., Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P., Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X., Clifton S.W., Roe B.A., McLaughlin R.E.;
"Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
DOI=10.1086/432514; PubMed=16088826 [NCBI, ExPASy, EBI, Israel, Japan]
Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K., Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P., Musser J.M.;
"Evolutionary origin and emergence of a highly successful clone of serotype M1 group A Streptococcus involved multiple horizontal gene transfer events.";
J. Infect. Dis. 192:771-782(2005).

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).
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.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AE004092; AAK34345.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000017; AAZ51900.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_269624.1; -.
YP_282645.1; -.

3D structure databases

HSSP

P14930; 1L1D. [HSSP ENTRY / PDB]

ModBase

Q99YT1.

Enzyme and pathway databases

BioCyc

SPYO160490:SPY1557-MON; -.
SPYO293653:M5005_SPY1282-MON; -.

Ontologies

GO:0008113;	Molecular function: peptide-methionine-(S)-S-oxide reductase activity (inferred from electronic annotation from HAMAP).
GO:0006464;	Biological process: protein modification process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01400; fused; 1.
MF_01401; fused; 1.
PBIL [Tree]

InterPro

IPR002569; MsrA.
IPR002579; MsrB.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.1060.10; MsrA; 1.
G3DSA:2.170.150.20; MsrB; 1.

Pfam

PF01625; PMSR; 1.
PF01641; SelR; 1.
Pfam graphical view of domain structure.

ProDom

PD004057; DUF25; 1.
PD003489; PMSR; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR00401; msrA; 1.
TIGR00357; MsrB; 1.

BLOCKS

Q99YT1.

Genome annotation databases

GeneID

3571633; -.
901767; -.

GenomeReviews

CP000017_GR; M5005_Spy1282.
AE004092_GR; SPy_1557.

KEGG

spy:SPy_1557; -.
spz:M5005_Spy_1282; -.

Phylogenomic databases

HOGENOM

Q99YT1; -.

Genome annotation databases

CMR

Q99YT1; SPy_1557.

Other

ProtoNet

Q99YT1.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Multifunctional enzyme; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 309`	`309`	`Peptide methionine sulfoxide reductase msrA/msrB.`	`PRO_0000138521`
`REGION`	`1 153`	`153`	`Peptide methionine sulfoxide reductase A.`
`REGION`	`170 293`	`124`	`Peptide methionine sulfoxide reductase B.`
`ACT_SITE`	`8 8`		`By similarity.`
`ACT_SITE`	`282 282`		`By similarity.`
`CONFLICT`	`294 294`		`A -> S (in Ref. 2; AAZ51900).`

Sequence information

Length: 309 AA [This is the length of the unprocessed precursor]

Molecular weight: 35103 Da [This is the MW of the unprocessed precursor]

CRC64: 226E1374F1038ADF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIYLAGGCFW GVEEYFSQVD GVLDAVSGYA NGRGDTTNYQ LIHQTGHAET VEVAYDANRI 

        70         80         90        100        110        120 
SLKELLLHFF RIIDPTSLNK QGNDRGSQYR TGIYYTDKAD LAIIDEVFKE KAKDYKKKIV 

       130        140        150        160        170        180 
VEKAPLKHFI KAEDYHQDYL KKNPNGYCHI DINQATYPVI DESKYPKPSA TEIKEKLSAD 

       190        200        210        220        230        240 
EYRVTQKNET EKAFSNRYWD SFDAGIYVDV VTGEPLFSSK DKFESGCGWP SFSRPISPDV 

       250        260        270        280        290        300 
VRYKEDKSFN MTRTEVRSRS GNSHLGHVFT DGPKDQGGLR YCINSLSITF IPKADMEAKG 


YGYLLSSVE

Q99YT1 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools