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UniProtKB/Swiss-Prot entry P54154


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

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Entry information
Entry name MSRA_BACSU
Primary accession number P54154
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 1, 1996 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 56)
Name and origin of the protein
Protein name Peptide methionine sulfoxide reductase msrA
Synonyms Protein-methionine-S-oxide reductase
EC 1.8.4.11
Peptide-methionine (S)-S-oxide reductase
Peptide Met(O) reductase
Gene name
Name: msrA
Synonyms: yppP
OrderedLocusNames: BSU21690
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168 / Marburg;
PubMed=8969496 [NCBI, ExPASy, EBI, Israel, Japan]
Capuano V., Galleron N., Pujic P., Sorokin A., Ehrlich S.D.;
"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.";
Microbiology 142:3005-3015(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
[3]
CHARACTERIZATION.
PubMed=9573155 [NCBI, ExPASy, EBI, Israel, Japan]
Hayes C.S., Illades-Aguiar B., Casillas-Martinez L., Setlow P.;
"In vitro and in vivo oxidation of methionine residues in small, acid-soluble spore proteins from Bacillus species.";
J. Bacteriol. 180:2694-2700(1998).
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.
  • CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin.
  • CATALYTIC ACTIVITY: L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin.
  • SIMILARITY: Belongs to the msrA Met sulfoxide reductase family.
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
L77246; AAA96647.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99115; CAB14087.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR E69940; E69940.
RefSeq NP_390052.1; -.
3D structure databases
HSSP P27110; 1FF3. [HSSP ENTRY / PDB]
ModBase P54154.
Enzyme and pathway databases
BioCyc BSUB224308:BSU2170-MON; -.
Organism-specific databases
SubtiList BG11627; msrA. [Micado]
Ontologies
GO
GO:0008113; Molecular function: peptide-methionine-(S)-S-oxide reductase activity (inferred from electronic annotation from HAMAP).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006464; Biological process: protein modification process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01401; -; 1.
PBIL [Tree]
InterPro IPR002569; MsrA.
Graphical view of domain structure.
Gene3D G3DSA:3.30.1060.10; MsrA; 1.
Pfam PF01625; PMSR; 1.
Pfam graphical view of domain structure.
ProDom PD003489; PMSR; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00401; msrA; 1.
BLOCKS P54154.
ProtoNet P54154.
Genome annotation databases
GeneID 939099; -.
GenomeReviews AL009126_GR; BSU21690.
KEGG bsu:BSU21690; -.
NMPDR fig|224308.1.peg.2175; -.
Phylogenomic databases
HOGENOM P54154; -.
Genome annotation databases
CMR P54154; BSU21690.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
CHAIN   1   177  177     Peptide methionine sulfoxide reductase msrA. PRO_0000138530
ACT_SITE   14    14        By similarity. 
Sequence information
Length: 177 AA [This is the length of the unprocessed precursor] Molecular weight: 20182 Da [This is the MW of the unprocessed precursor] CRC64: DFEA7ADF34357D03 [This is a checksum on the sequence]
        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 

P54154 in FASTA format

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