P0A746 (MSRB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptide methionine sulfoxide reductase MsrB
EC=1.8.4.12

Alternative name(s):
Peptide-methionine (R)-S-oxide reductase

Gene names

Name:	msrB
Synonyms:	yeaA
Ordered Locus Names:	b1778, JW1767

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	137 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin. Ref.7
Cofactor	Binds 1 zinc ion per subunit. The zinc ion is important for the structural integrity of the protein. Ref.7
Sequence similarities	Belongs to the MsrB Met sulfoxide reductase family.
Mass spectrometry	Molecular mass is 15319±1 Da from positions 2 - 137. Determined by ESI. Ref.7
Sequence caution	The sequence X02662 differs from that shown. Reason: Frameshift at position 5.

Ontologies

Keywords
Ligand	Metal-binding Zinc
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	cytoplasm Inferred by curator Ref.7. Source: EcoliWiki
Molecular function	iron ion binding Inferred from direct assay Ref.7. Source: EcoliWiki peptide-methionine (R)-S-oxide reductase activity Inferred from direct assay Ref.7. Source: EcoliWiki peptide-methionine-(S)-S-oxide reductase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from direct assay Ref.7. Source: EcoliWiki
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed HAMAP MF_01400
	Chain	2 – 137	136	Peptide methionine sulfoxide reductase MsrB HAMAP MF_01400		PRO_0000140271
Sites
	Active site	118	1	Nucleophile By similarity
	Metal binding	46	1	Zinc
	Metal binding	49	1	Zinc
	Metal binding	95	1	Zinc
	Metal binding	98	1	Zinc
Experimental info
	Mutagenesis	46	1	C → D: Loss of activity; when associated with S-49; S-95 and S-98. Ref.7
	Mutagenesis	49	1	C → S: Loss of activity; when associated with S-46; S-95 and S-98. Ref.7
	Mutagenesis	95	1	C → S: Loss of activity; when associated with S-46; S-49 and S-98. Ref.7
	Mutagenesis	98	1	C → S: Loss of activity; when associated with S-46; S-49 and S-95. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	P0A746 [UniParc]. Last modified June 7, 2005. Version 1. Checksum: 7B9B783DBEBE0F71	FASTA	137	15,451
	10 20 30 40 50 60 MANKPSAEEL KKNLSEMQFY VTQNHGTEPP FTGRLLHNKR DGVYHCLICD APLFHSQTKY 70 80 90 100 110 120 DSGCGWPSFY EPVSEESIRY IKDLSHGMQR IEIRCGNCDA HLGHVFPDGP QPTGERYCVN 130 SASLRFTDGE NGEEING

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:363-377(1996) [PubMed: 9097039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] 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: 16738553] [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: 2990926] [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: 7984428] [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: 11677230] [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: 16251365] [Abstract] Cited for: CATALYTIC ACTIVITY, COFACTOR, MASS SPECTROMETRY, MUTAGENESIS OF CYS-46; CYS-49; CYS-95 AND CYS-98. Strain: K12.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U00096 Genomic DNA. Translation: AAC74848.1. AP009048 Genomic DNA. Translation: BAA15575.2. X02662 Genomic DNA. No translation available.
PIR	B64938.
RefSeq	NP_416292.1. NC_000913.2.
3D structure databases
ProteinModelPortal	P0A746.
SMR	P0A746. Positions 3-134.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-48167N.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000001178; EBESCP00000001178; EBESCG00000000973. EBESCT00000017612; EBESCP00000016903; EBESCG00000016668.
GeneID	947188.
GenomeReviews	Gene locus JW1767 in contig AP009048_GR. Gene locus b1778 in contig U00096_GR.
KEGG	ecj:JW1767. eco:b1778.
PATRIC	32118867. VBIEscCol129921_1851.
Organism-specific databases
EchoBASE	EB2295.
EcoGene	EG12394. msrB.
Phylogenomic databases
eggNOG	COG0229.
GeneTree	EBGT00050000011436.
HOGENOM	HBG715255.
OMA	FTDGPVD.
PhylomeDB	P0A746.
ProtClustDB	PRK00222.
Enzyme and pathway databases
BioCyc	EcoCyc:EG12394-MONOMER. MetaCyc:EG12394-MONOMER.
Gene expression databases
Genevestigator	P0A746.
Family and domain databases
HAMAP	MF_01400. MsrB. [Tree]
InterPro	IPR002579. Methionine_sulphoxide_MsrB. IPR011057. Mss4-like. [Graphical view]
Gene3D	G3DSA:2.170.150.20. MsrB. 1 hit.
KO	K07305.
Pfam	PF01641. SelR. 1 hit. [Graphical view]
SUPFAM	SSF51316. Mss4_like. 1 hit.
TIGRFAMs	TIGR00357. TIGR00357. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MSRB_ECOLI

Accession

Primary (citable) accession number: P0A746
Secondary accession number(s): P39903, P76232, P76912

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	June 7, 2005
Last modified:	January 25, 2012
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program