msrB:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.

Standard name

MsrB

Synonyms

methionine sulfoxide reductase B[1], B1778[2][1], YeaA[2][1], MsrB[2][1] , ECK1776, JW1767, yeaA, b1778

Product description

methionine sulfoxide reductase B[2][3]

Methionine sulfoxide reductase B; specific for met-R-(o) diastereoisomers within proteins; mutant is cadmium sensitive; free met-R-(o) is inefficiently reduced by MsrB[4]

EC number (for enzymes)
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Notes

Function

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<protect> Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0005737

cytoplasm

C

Seeded from Riley et al 2006 [1].

Missing: evidence, reference

GO:0008113

peptide-methionine-(S)-S-oxide reductase activity

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_01400

F

Seeded from EcoCyc (v14.0)

complete

GO:0008113

peptide-methionine-(S)-S-oxide reductase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR002579

F

Seeded from EcoCyc (v14.0)

complete

GO:0008270

zinc ion binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0862

F

Seeded from EcoCyc (v14.0)

complete

GO:0016491

oxidoreductase activity

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0560

F

Seeded from EcoCyc (v14.0)

complete

GO:0033743

peptide-methionine (R)-S-oxide reductase activity

GOA:spec
GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:1.8.4.12

F

Seeded from EcoCyc (v14.0)

complete

GO:0008270

zinc ion binding

PMID:16251365[5]

IDA: Inferred from Direct Assay

F

complete

GO:0046872

metal ion binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0479

F

Seeded from EcoCyc (v14.0)

complete

GO:0005506

iron ion binding

PMID:16251365[5]

IDA: Inferred from Direct Assay

F

complete

GO:0055114

oxidation reduction

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR002579

P

Seeded from EcoCyc (v14.0)

complete

GO:0005737

cytoplasm

PMID:16251365[5]

IC: Inferred by Curator

C

Missing: with/from

GO:0055114

oxidation reduction

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0560

P

Seeded from EcoCyc (v14.0)

complete

GO:0033743

peptide-methionine (R)-S-oxide reductase activity

PMID:16251365[5]

IDA: Inferred from Direct Assay

F

complete

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Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner Type Partner Notes References Evidence

Protein

torY

PMID:19402753[6]

LCMS(ID Probability):99.6

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Notes

Localization

See Help:Product_localization for how to add or edit information in this section of EcoliWiki.

Compartment Description Evidence Reference/Source Notes
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Notes

Structure and Physical Properties

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<protect> Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Name
Sequence

at EcoCyc 

MANKPSAEEL KKNLSEMQFY VTQNHGTEPP FTGRLLHNKR DGVYHCLICD APLFHSQTKY
DSGCGWPSFY EPVSEESIRY IKDLSHGMQR IEIRCGNCDA HLGHVFPDGP QPTGERYCVN
SASLRFTDGE NGEEING
Length

137

Mol. Wt

15.45 kDa

pI

5.9 (calculated)

Extinction coefficient

14,440 - 15,190 (calc based on 6 Y, 1 W, and 6 C residues)

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Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

Type Residues Description Notes References

Initiator Methionine

1

Removed

UniProt:P0A746

Domain

7..129

PF01641 SelR domain

PMID:19920124[7]

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Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures

<beststructure> gene=msrB taxon=562,83333 </beststructure>

Models

View models at:

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Structure figures

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Notes

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource type Source Notes/Reference
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Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

Database Accession Notes

NCBI (Protein) (EcoliWiki Page)

GI:16129732

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:947188

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0005916

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P0A746

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG12394

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG12394

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:947188

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120002257

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB2295

Escherichia coli str. K-12 substr. MG1655

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Notes

Links

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References

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See Help:References for how to manage references in EcoliWiki.

  1. ↑ 1.0 1.1 1.2 1.3 1.4 1.5 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 2.3 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. ↑ 5.0 5.1 5.2 5.3 Olry, A et al. (2005) Insights into the role of the metal binding site in methionine-R-sulfoxide reductases B. Protein Sci. 14 2828-37 PubMed
  6. ↑ Hu, P et al. (2009) Global functional atlas of Escherichia coli encompassing previously uncharacterized proteins. PLoS Biol. 7 e96 PubMed
  7. ↑ Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

Categories

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