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B0VR86 (MSRB_ACIBS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptide methionine sulfoxide reductase MsrB

EC=1.8.4.12
Alternative name(s):
Peptide-methionine (R)-S-oxide reductase
Gene names
Name:msrB
Ordered Locus Names:ABSDF2180
OrganismAcinetobacter baumannii (strain SDF) [Complete proteome] [HAMAP]
Taxonomic identifier509170 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex

Protein attributes

Sequence length139 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit. The zinc ion is important for the structural integrity of the protein By similarity.

Sequence similarities

Belongs to the MsrB Met sulfoxide reductase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 139139Peptide methionine sulfoxide reductase MsrB HAMAP MF_01400
PRO_1000145346

Sites

Active site1191Nucleophile By similarity
Metal binding471Zinc By similarity
Metal binding501Zinc By similarity
Metal binding961Zinc By similarity
Metal binding991Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
B0VR86 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 5B583F9B4E5C8D86

FASTA13915,837
        10         20         30         40         50         60 
MGKVNKTDRE WQRELSPEEY RITRQKGTEP AFTGQYWNTK QHGTYVCRCC GAELFSSDAK 

        70         80         90        100        110        120 
YDSGCGWPSF FRPLNGSVID EHEDLTHGMV RTEIVCHDCE AHLGHVFEDG PQPTGLRYCV 

       130 
NSASLQLKTQ EKNDEGTYP 

« Hide

References

[1]"Comparative analysis of Acinetobacters: three genomes for three lifestyles."
Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E., Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J., Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C., Weissenbach J., Cruveiller S.
PLoS ONE 3:E1805-E1805(2008) [PubMed: 18350144] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SDF.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU468230 Genomic DNA. Translation: CAP01505.1.
RefSeqYP_001707473.1. NC_010400.1.

3D structure databases

ProteinModelPortalB0VR86.
SMRB0VR86. Positions 3-128.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0VR86.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5986835.
GenomeReviewsGene locus ABSDF2180 in contig CU468230_GR.
KEGGabm:ABSDF2180.
PATRIC20735127. VBIAciBau88365_2073.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG715255.
OMAAPLFRSD.
ProtClustDBCLSK707445.

Family and domain databases

HAMAPMF_01400. MsrB.
[Tree]
InterProIPR002579. Methionine_sulphoxide_MsrB.
IPR011057. Mss4-like.
[Graphical view]
Gene3DG3DSA:2.170.150.20. MsrB. 1 hit.
KOK07305.
PfamPF01641. SelR. 1 hit.
[Graphical view]
SUPFAMSSF51316. Mss4_like. 1 hit.
TIGRFAMsTIGR00357. TIGR00357. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMSRB_ACIBS
AccessionPrimary (citable) accession number: B0VR86
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 8, 2008
Last modified: January 25, 2012
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families