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:	msrAB1
	Synonyms:	exp3, msrA
	OrderedLocusNames:	SP_1359

From

Streptococcus pneumoniae

[TaxID: 1313]

[HAMAP proteome]

Taxonomy

Bacteria; Firmicutes; Lactobacillales; Streptococcaceae; Streptococcus.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-334 / TIGR4;
DOI=10.1126/science.1061217; PubMed=11463916 [NCBI, ExPASy, EBI, Israel, Japan]
Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D., Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J., Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D., Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D., Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L., McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K., Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A., Morrison D.A., Hollingshead S.K., Fraser C.M.;
"Complete genome sequence of a virulent isolate of Streptococcus pneumoniae.";
Science 293:498-506(2001).

Comments

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 (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.
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.

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

AE005672; AAK75457.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

H95157; H95157.

RefSeq

NP_345817.1; -.

3D structure databases

HSSP

P14930; 1L1D. [HSSP ENTRY / PDB]

ModBase

P0A3Q9.

Ontologies

GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0033743;	Molecular function: peptide-methionine (R)-S-oxide reductase activity (inferred from electronic annotation from EC).
GO:0008113;	Molecular function: peptide-methionine-(S)-S-oxide reductase activity (inferred from electronic annotation from HAMAP).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.

Genome annotation databases

GeneID

931912; -.

GenomeReviews

AE005672_GR; SP_1359.

KEGG

spn:SP_1359; -.

TIGR

SP_1359; -.

Phylogenomic databases

HOGENOM

P0A3Q9; -.

Other

ProtoNet

P0A3Q9.

UniRef

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

Keywords

Cell membrane; Complete proteome; Membrane; Multifunctional enzyme; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 312`	`312`	`Peptide methionine sulfoxide reductase msrA/msrB 1.`	`PRO_0000138517`
`REGION`	`1 155`	`155`	`Peptide methionine sulfoxide reductase.`
`REGION`	`172 295`	`124`	`Peptide methionine sulfoxide reductase B.`
`ACT_SITE`	`10 10`		`By similarity.`
`ACT_SITE`	`284 284`		`By similarity.`

Sequence information

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]

        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

P0A3Q9 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