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UniProtKB/Swiss-Prot entry P0A746

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MSRB_ECOLI
Primary accession number P0A746
Secondary accession numbers P39903 P76232 P76912
Integrated into Swiss-Prot on June 7, 2005
Sequence was last modified on June 7, 2005 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 35)
Name and origin of the protein
Protein name Peptide methionine sulfoxide reductase msrB
Synonyms EC 1.8.4.12
Peptide-methionine (R)-S-oxide reductase
Gene name
Name: msrB
Synonyms: yeaA
OrderedLocusNames: b1778, JW1767
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1093/dnares/3.6.363; PubMed=9097039 [NCBI, ExPASy, EBI, Israel, Japan]
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map.";
DNA Res. 3:363-377(1996).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-48.
PubMed=2990926 [NCBI, ExPASy, EBI, Israel, Japan]
Branlant G., Branlant C.;
"Nucleotide sequence of the Escherichia coli gap gene. Different evolutionary behavior of the NAD+-binding domain and of the catalytic domain of D-glyceraldehyde-3-phosphate dehydrogenase.";
Eur. J. Biochem. 150:61-66(1985).
[5]
 IDENTIFICATION.
DOI=10.1093/nar/22.22.4756; PubMed=7984428 [NCBI, ExPASy, EBI, Israel, Japan]
Borodovsky M., Rudd K.E., Koonin E.V.;
"Intrinsic and extrinsic approaches for detecting genes in a bacterial genome.";
Nucleic Acids Res. 22:4756-4767(1994).
[6]
 FUNCTION.
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1074/jbc.M105509200; PubMed=11677230 [NCBI, ExPASy, EBI, Israel, Japan]
Grimaud R., Ezraty B., Mitchell J.K., Lafitte D., Briand C., Derrick P.J., Barras F.;
"Repair of oxidized proteins. Identification of a new methionine sulfoxide reductase.";
J. Biol. Chem. 276:48915-48920(2001).
[7]
 CATALYTIC ACTIVITY, COFACTOR, MASS SPECTROMETRY, AND MUTAGENESIS OF CYS-46; CYS-49; CYS-95 AND CYS-98.
STRAIN=K12;
DOI=10.1110/ps.051711105; PubMed=16251365 [NCBI, ExPASy, EBI, Israel, Japan]
Olry A., Boschi-Muller S., Yu H., Burnel D., Branlant G.;
"Insights into the role of the metal binding site in methionine-R-sulfoxide reductases B.";
Protein Sci. 14:2828-2837(2005).
Comments
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
U00096; AAC74848.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA15575.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X02662; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
PIR B64938; B64938.
RefSeq AP_002397.1; -.
NP_416292.1; -.
3D structure databases
HSSP P14930; 1L1D. [HSSP ENTRY / PDB]
ModBase P0A746.
Enzyme and pathway databases
BioCyc EcoCyc:EG12394-MON; -.
Organism-specific databases
EchoBASE EB2295; -.
EcoGene EG12394; msrB.
Ontologies
GO
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:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
HAMAP MF_01400; -; 1.
PBIL [Tree]
InterPro IPR002579; MsrB.
Graphical view of domain structure.
Gene3D G3DSA:2.170.150.20; MsrB; 1.
Pfam PF01641; SelR; 1.
Pfam graphical view of domain structure.
ProDom PD004057; DUF25; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00357; MsrB; 1.
Genome annotation databases
GeneID 947188; -.
GenomeReviews AP009048_GR; JW1767.
U00096_GR; b1778.
KEGG ecj:JW1767; -.
eco:b1778; -.
Phylogenomic databases
HOGENOM P0A746; -.
Genome annotation databases
CMR P0A746; b1778.
Other
ProtoNet P0A746.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Metal-binding; Oxidoreductase; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   137  136     Peptide methionine sulfoxide reductase msrB. PRO_0000140271
ACT_SITE   118   118        Nucleophile (By similarity). 
METAL   46    46        Zinc. 
METAL   49    49        Zinc. 
METAL   95    95        Zinc. 
METAL   98    98        Zinc. 
MUTAGEN   46    46        C->D: Loss of activity; when associated with S-49; S-95 and S-98. 
MUTAGEN   49    49        C->S: Loss of activity; when associated with S-46; S-95 and S-98. 
MUTAGEN   95    95        C->S: Loss of activity; when associated with S-46; S-49 and S-98. 
MUTAGEN   98    98        C->S: Loss of activity; when associated with S-46; S-49 and S-95. 
Sequence information
Length: 137 AA [This is the length of the unprocessed precursor] Molecular weight: 15451 Da [This is the MW of the unprocessed precursor] CRC64: 7B9B783DBEBE0F71 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MANKPSAEEL KKNLSEMQFY VTQNHGTEPP FTGRLLHNKR DGVYHCLICD APLFHSQTKY 

        70         80         90        100        110        120 
DSGCGWPSFY EPVSEESIRY IKDLSHGMQR IEIRCGNCDA HLGHVFPDGP QPTGERYCVN 

       130 
SASLRFTDGE NGEEING
P0A746 in FASTA format

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