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P54154 (MSRA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Peptide methionine sulfoxide reductase MsrA
Short name=Protein-methionine-S-oxide reductase
EC=1.8.4.11
Alternative name(s):
Peptide-methionine (S)-S-oxide reductase
Short name=Peptide Met(O) reductase
Gene names
Name:msrA
Synonyms:yppP
Ordered Locus Names:BSU21690
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length177 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. May deal with oxidative damage to alpha/beta-type SASP in spores. HAMAP MF_01401

Catalytic activity

Peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin. HAMAP MF_01401

L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin. HAMAP MF_01401

Sequence similarities

Belongs to the MsrA Met sulfoxide reductase family.

Ontologies

Keywords
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processprotein metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionpeptide-methionine-(S)-S-oxide reductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 177177Peptide methionine sulfoxide reductase MsrA HAMAP MF_01401
PRO_0000138530

Sites

Active site141 By similarity

Sequences

Sequence LengthMass (Da)Tools
P54154 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: DFEA7ADF34357D03

FASTA17720,182
        10         20         30         40         50         60 
MSEKKEIATF AGGCFWCMVK PFDEQPGIEK VVSGYTGGHT ENPTYEEVCS ETTGHREAVQ 

        70         80         90        100        110        120 
ITFHPDVFPY EKLLELFWQQ IDPTDAGGQF ADRGSSYRAA IFYHNDKQKE LAEASKQRLA 

       130        140        150        160        170 
ESGIFKDPIV TDILKAEPFY EAEGYHQHFY KKNPAHYQRY RTGSGRAGFI SEHWGAK

« Hide

References

« Hide 'large scale' references
[1]"Organization of the Bacillus subtilis 168 chromosome between kdg and the attachment site of the SP beta prophage: use of long accurate PCR and yeast artificial chromosomes for sequencing."
Capuano V., Galleron N., Pujic P., Sorokin A., Ehrlich S.D.
Microbiology 142:3005-3015(1996) [PubMed: 8969496] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"In vitro and in vivo oxidation of methionine residues in small, acid-soluble spore proteins from Bacillus species."
Hayes C.S., Illades-Aguiar B., Casillas-Martinez L., Setlow P.
J. Bacteriol. 180:2694-2700(1998) [PubMed: 9573155] [Abstract]
Cited for: CHARACTERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L77246 Genomic DNA. Translation: AAA96647.1.
AL009126 Genomic DNA. Translation: CAB14087.1.
PIRE69940.
RefSeqNP_390052.1. NC_000964.3.

3D structure databases

ProteinModelPortalP54154.
SMRP54154. Positions 1-162.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000000043; EBBACP00000000043; EBBACG00000000043.
GeneID939099.
GenomeReviewsGene locus BSU21690 in contig AL009126_GR.
KEGGbsu:BSU21690.
NMPDRfig|224308.1.peg.2175.
PATRIC18976143. VBIBacSub10457_2262.

Organism-specific databases

GenoListBSU21690. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000000580.
HOGENOMHBG748152.
OMALVELYWT.
PhylomeDBP54154.
ProtClustDBPRK14054.

Enzyme and pathway databases

BioCycBSUB:BSU21690-MONOMER.

Family and domain databases

HAMAPMF_01401. MsrA.
[Tree]
InterProIPR002569. Peptide_Met_Sox_Rdtase_MsrA.
[Graphical view]
Gene3DG3DSA:3.30.1060.10. MsrA. 1 hit.
KOK07304.
PfamPF01625. PMSR. 1 hit.
[Graphical view]
SUPFAMSSF55068. MsrA. 1 hit.
TIGRFAMsTIGR00401. MsrA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMSRA_BACSU
AccessionPrimary (citable) accession number: P54154
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: January 25, 2012
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents