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UniProtKB/Swiss-Prot entry P0A747


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

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Entry information
Entry name MSRB_ECOL6
Primary accession number P0A747
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    November 4, 2008 (Entry version 25)
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
OrderedLocusNames: c2183
From
Escherichia coli O6 [TaxID: 217992] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC;
DOI=10.1073/pnas.252529799; PubMed=12471157 [NCBI, ExPASy, EBI, Israel, Japan]
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli.";
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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
AE014075; AAN80642.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_754077.1; -.
3D structure databases
HSSP P14930; 1L1D. [HSSP ENTRY / PDB]
ModBase P0A747.
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 1036623; -.
GenomeReviews AE014075_GR; c2183.
KEGG ecc:c2183; -.
Phylogenomic databases
HOGENOM P0A747; -.
Genome annotation databases
CMR P0A747; c2183.
Other
ProtoNet P0A747.
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 (By similarity). 
CHAIN   2   137  136     Peptide methionine sulfoxide reductase msrB. PRO_0000140273
ACT_SITE   118   118        Nucleophile (By similarity). 
METAL   46    46        Zinc (By similarity). 
METAL   49    49        Zinc (By similarity). 
METAL   95    95        Zinc (By similarity). 
METAL   98    98        Zinc (By similarity). 
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 

P0A747 in FASTA format

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

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