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Protein

Peptide methionine sulfoxide reductase MsrB

Gene

msrB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin.1 Publication

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit. The zinc ion is important for the structural integrity of the protein.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi46 – 461ZincPROSITE-ProRule annotation
Metal bindingi49 – 491ZincPROSITE-ProRule annotation
Metal bindingi95 – 951ZincPROSITE-ProRule annotation
Metal bindingi98 – 981ZincPROSITE-ProRule annotation
Active sitei118 – 1181NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

  • iron ion binding Source: EcoliWiki
  • peptide-methionine (R)-S-oxide reductase activity Source: EcoliWiki
  • zinc ion binding Source: EcoliWiki

GO - Biological processi

  • protein repair Source: EcoCyc
  • response to oxidative stress Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:EG12394-MONOMER.
ECOL316407:JW1767-MONOMER.
MetaCyc:EG12394-MONOMER.
BRENDAi1.8.4.12. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptide methionine sulfoxide reductase MsrB (EC:1.8.4.12)
Alternative name(s):
Peptide-methionine (R)-S-oxide reductase
Gene namesi
Name:msrB
Synonyms:yeaA
Ordered Locus Names:b1778, JW1767
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12394. msrB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi46 – 461C → D: Loss of activity; when associated with S-49; S-95 and S-98. 1 Publication
Mutagenesisi49 – 491C → S: Loss of activity; when associated with S-46; S-95 and S-98. 1 Publication
Mutagenesisi95 – 951C → S: Loss of activity; when associated with S-46; S-49 and S-98. 1 Publication
Mutagenesisi98 – 981C → S: Loss of activity; when associated with S-46; S-49 and S-95. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 137136Peptide methionine sulfoxide reductase MsrBPRO_0000140271Add
BLAST

Proteomic databases

EPDiP0A746.
PaxDbiP0A746.
PRIDEiP0A746.

Interactioni

Protein-protein interaction databases

BioGridi4260307. 13 interactions.
DIPiDIP-48167N.
IntActiP0A746. 3 interactions.
STRINGi511145.b1778.

Structurei

3D structure databases

ProteinModelPortaliP0A746.
SMRiP0A746. Positions 8-128.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 129123MsrBPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 MsrB (methionine-R-sulfoxide reductase) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105E0X. Bacteria.
COG0229. LUCA.
HOGENOMiHOG000243425.
InParanoidiP0A746.
KOiK07305.
OMAiRSHGMLR.
OrthoDBiEOG6091JX.
PhylomeDBiP0A746.

Family and domain databases

Gene3Di2.170.150.20. 1 hit.
HAMAPiMF_01400. MsrB.
InterProiIPR028427. Met_Sox_Rdtase.
IPR002579. Met_Sox_Rdtase_MsrB.
IPR011057. Mss4-like.
[Graphical view]
PANTHERiPTHR10173. PTHR10173. 1 hit.
PfamiPF01641. SelR. 1 hit.
[Graphical view]
SUPFAMiSSF51316. SSF51316. 1 hit.
TIGRFAMsiTIGR00357. TIGR00357. 1 hit.
PROSITEiPS51790. MSRB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A746-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANKPSAEEL KKNLSEMQFY VTQNHGTEPP FTGRLLHNKR DGVYHCLICD
60 70 80 90 100
APLFHSQTKY DSGCGWPSFY EPVSEESIRY IKDLSHGMQR IEIRCGNCDA
110 120 130
HLGHVFPDGP QPTGERYCVN SASLRFTDGE NGEEING
Length:137
Mass (Da):15,451
Last modified:June 7, 2005 - v1
Checksum:i7B9B783DBEBE0F71
GO

Sequence cautioni

The sequence X02662 differs from that shown. Reason: Frameshift at position 5. Curated

Mass spectrometryi

Molecular mass is 15319±1 Da from positions 2 - 137. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74848.1.
AP009048 Genomic DNA. Translation: BAA15575.2.
X02662 Genomic DNA. No translation available.
PIRiB64938.
RefSeqiNP_416292.1. NC_000913.3.
WP_001284618.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74848; AAC74848; b1778.
BAA15575; BAA15575; BAA15575.
GeneIDi947188.
KEGGiecj:JW1767.
eco:b1778.
PATRICi32118867. VBIEscCol129921_1851.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74848.1.
AP009048 Genomic DNA. Translation: BAA15575.2.
X02662 Genomic DNA. No translation available.
PIRiB64938.
RefSeqiNP_416292.1. NC_000913.3.
WP_001284618.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP0A746.
SMRiP0A746. Positions 8-128.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260307. 13 interactions.
DIPiDIP-48167N.
IntActiP0A746. 3 interactions.
STRINGi511145.b1778.

Proteomic databases

EPDiP0A746.
PaxDbiP0A746.
PRIDEiP0A746.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74848; AAC74848; b1778.
BAA15575; BAA15575; BAA15575.
GeneIDi947188.
KEGGiecj:JW1767.
eco:b1778.
PATRICi32118867. VBIEscCol129921_1851.

Organism-specific databases

EchoBASEiEB2295.
EcoGeneiEG12394. msrB.

Phylogenomic databases

eggNOGiENOG4105E0X. Bacteria.
COG0229. LUCA.
HOGENOMiHOG000243425.
InParanoidiP0A746.
KOiK07305.
OMAiRSHGMLR.
OrthoDBiEOG6091JX.
PhylomeDBiP0A746.

Enzyme and pathway databases

BioCyciEcoCyc:EG12394-MONOMER.
ECOL316407:JW1767-MONOMER.
MetaCyc:EG12394-MONOMER.
BRENDAi1.8.4.12. 2026.

Miscellaneous databases

PROiP0A746.

Family and domain databases

Gene3Di2.170.150.20. 1 hit.
HAMAPiMF_01400. MsrB.
InterProiIPR028427. Met_Sox_Rdtase.
IPR002579. Met_Sox_Rdtase_MsrB.
IPR011057. Mss4-like.
[Graphical view]
PANTHERiPTHR10173. PTHR10173. 1 hit.
PfamiPF01641. SelR. 1 hit.
[Graphical view]
SUPFAMiSSF51316. SSF51316. 1 hit.
TIGRFAMsiTIGR00357. TIGR00357. 1 hit.
PROSITEiPS51790. MSRB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "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."
    Branlant G., Branlant C.
    Eur. J. Biochem. 150:61-66(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-48.
  5. "Intrinsic and extrinsic approaches for detecting genes in a bacterial genome."
    Borodovsky M., Rudd K.E., Koonin E.V.
    Nucleic Acids Res. 22:4756-4767(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  6. "Repair of oxidized proteins. Identification of a new methionine sulfoxide reductase."
    Grimaud R., Ezraty B., Mitchell J.K., Lafitte D., Briand C., Derrick P.J., Barras F.
    J. Biol. Chem. 276:48915-48920(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: K12 / MG1655 / ATCC 47076.
  7. "Insights into the role of the metal binding site in methionine-R-sulfoxide reductases B."
    Olry A., Boschi-Muller S., Yu H., Burnel D., Branlant G.
    Protein Sci. 14:2828-2837(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, COFACTOR, MASS SPECTROMETRY, MUTAGENESIS OF CYS-46; CYS-49; CYS-95 AND CYS-98.
    Strain: K12.

Entry informationi

Entry nameiMSRB_ECOLI
AccessioniPrimary (citable) accession number: P0A746
Secondary accession number(s): P39903, P76232, P76912
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: June 8, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.