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Protein

Protein-methionine-sulfoxide reductase catalytic subunit MsrP

Gene

msrP

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

Functioni

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons (PubMed:26641313). Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine (PubMed:26641313). MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal (PubMed:26641313). The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide (PubMed:26641313). Can catalyze the reduction of a variety of substrates in vitro, including dimethyl sulfoxide, trimethylamine N-oxide, phenylmethyl sulfoxide and L-methionine sulfoxide (PubMed:15355966). Cannot reduce cyclic N-oxides (PubMed:15355966). Shows no activity as sulfite oxidase (PubMed:15355966).2 Publications

Catalytic activityi

[Protein]-L-methionine + a quinone + H2O = [protein]-L-methionine (S)-S-oxide + a quinol.1 Publication
[Protein]-L-methionine + a quinone + H2O = [protein]-L-methionine (R)-S-oxide + a quinol.1 Publication

Cofactori

Mo-molybdopterin1 PublicationNote: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. The oxidation state of Mo is +5. Is inactive in the presence of the tungsten-substituted form (W-MPT) of the cofactor.1 Publication

Kineticsi

kcat is 30.5 sec(-1) with N-acetyl-Met-O as substrate. kcat is 36.0 sec(-1) with L-methionine (S)-S-oxide as substrate. kcat is 168.3 sec(-1) with L-methionine (R)-S-oxide as substrate.1 Publication

  1. KM=12 mM for dimethyl sulfoxide1 Publication
  2. KM=22 mM for trimethylamine N-oxide1 Publication
  3. KM=27.9 mM for tetramethylene sulfoxide1 Publication
  4. KM=119 mM for L-methionine sulfoxide1 Publication
  5. KM=3.8 mM for N-acetyl-Met-O1 Publication
  6. KM=8.0 mM for L-methionine (S)-S-oxide1 Publication
  7. KM=25.7 mM for L-methionine (R)-S-oxide1 Publication
  1. Vmax=56.3 µmol/min/mg enzyme with N-acetyl-Met-O as substrate1 Publication
  2. Vmax=67.2 µmol/min/mg enzyme with L-methionine (S)-S-oxide as substrate1 Publication
  3. Vmax=313.4 µmol/min/mg enzyme with L-methionine (R)-S-oxide as substrate1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei88 – 881Molybdopterin1 Publication
Metal bindingi146 – 1461Molybdenum1 Publication
Binding sitei181 – 1811Molybdopterin1 Publication
Binding sitei233 – 2331Molybdopterin1 Publication
Binding sitei238 – 2381Molybdopterin1 Publication

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • molybdopterin cofactor binding Source: EcoCyc
  • oxidoreductase activity, acting on a sulfur group of donors Source: EcoCyc
  • oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor Source: UniProtKB

GO - Biological processi

  • nitrate assimilation Source: InterPro
  • oxidation-reduction process Source: UniProtKB
  • protein repair Source: UniProtKB
  • response to hypochlorite Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, Molybdenum

Enzyme and pathway databases

BioCyciEcoCyc:G7059-MONOMER.
ECOL316407:JW1954-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein-methionine-sulfoxide reductase catalytic subunit MsrPUniRule annotation1 Publication (EC:1.8.5.-UniRule annotation1 Publication)
Gene namesi
Name:msrP1 Publication
Synonyms:yedYImported
Ordered Locus Names:b1971, JW1954
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG14047. yedY.

Subcellular locationi

  • Periplasm 1 Publication

  • Note: Is attached to the inner membrane when interacting with the MsrQ subunit.

GO - Cellular componenti

  • outer membrane-bounded periplasmic space Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Disruption phenotypei

Cells lacking the msrPQ genes display no visible growth defect.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi146 – 1461C → S: Loss of enzymatic activity. Enhances binding to MsrQ and targeting to the inner membrane. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4444Tat-type signal1 PublicationAdd
BLAST
Chaini45 – 334290Protein-methionine-sulfoxide reductase catalytic subunit MsrPPRO_0000070684Add
BLAST

Post-translational modificationi

Exported by the Tat system. Can also be exported by the Sec system.1 Publication

Proteomic databases

PaxDbiP76342.
PRIDEiP76342.

Expressioni

Inductioni

Is induced at protein level by hypochlorous acid (HOCl), a powerful antimicrobial released by neutrophils, but not by H2O2. Induction by HOCl is dependent on the presence of a functional YedV/YedW two-component system.1 Publication

Interactioni

Subunit structurei

Heterodimer of a catalytic subunit (MsrP) and a heme-binding subunit (MsrQ).1 Publication

Protein-protein interaction databases

BioGridi4259675. 12 interactions.
DIPiDIP-47888N.
IntActiP76342. 2 interactions.
STRINGi511145.b1971.

Structurei

Secondary structure

1
334
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi70 – 723Combined sources
Helixi81 – 844Combined sources
Helixi91 – 933Combined sources
Helixi99 – 1035Combined sources
Helixi104 – 1063Combined sources
Beta strandi113 – 12210Combined sources
Beta strandi124 – 1274Combined sources
Helixi128 – 1336Combined sources
Beta strandi138 – 1469Combined sources
Turni147 – 1493Combined sources
Beta strandi150 – 16011Combined sources
Helixi161 – 1688Combined sources
Beta strandi176 – 1816Combined sources
Turni185 – 1873Combined sources
Helixi189 – 1913Combined sources
Turni194 – 1996Combined sources
Beta strandi205 – 2095Combined sources
Helixi210 – 2145Combined sources
Beta strandi219 – 2246Combined sources
Helixi231 – 2333Combined sources
Beta strandi238 – 2403Combined sources
Helixi246 – 2483Combined sources
Beta strandi252 – 26110Combined sources
Helixi266 – 2705Combined sources
Turni272 – 2743Combined sources
Beta strandi293 – 2975Combined sources
Beta strandi308 – 3103Combined sources
Helixi313 – 3164Combined sources
Helixi318 – 3258Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XDQX-ray2.55A/B/C/D/E45-334[»]
1XDYX-ray2.20A/B/C/D/E/F/G/H/I/J45-334[»]
ProteinModelPortaliP76342.
SMRiP76342. Positions 62-330.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP76342.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni91 – 922Molybdopterin binding1 Publication
Regioni249 – 2513Molybdopterin binding1 Publication

Sequence similaritiesi

Belongs to the MsrP family.UniRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105CCD. Bacteria.
COG2041. LUCA.
HOGENOMiHOG000255004.
InParanoidiP76342.
KOiK07147.
OMAiDWPYVEG.
OrthoDBiEOG6FBWVX.
PhylomeDBiP76342.

Family and domain databases

Gene3Di3.90.420.10. 1 hit.
HAMAPiMF_01206. MsrP.
InterProiIPR022867. MsrP.
IPR000572. OxRdtase_Mopterin-bd_dom.
IPR006311. TAT_signal.
[Graphical view]
PfamiPF00174. Oxidored_molyb. 1 hit.
[Graphical view]
SUPFAMiSSF56524. SSF56524. 1 hit.
PROSITEiPS51318. TAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P76342-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKNQFLKES DVTAESVFFM KRRQVLKALG ISATALSLPH AAHADLLSWF
60 70 80 90 100
KGNDRPPAPA GKALEFSKPA AWQNNLPLTP ADKVSGYNNF YEFGLDKADP
110 120 130 140 150
AANAGSLKTD PWTLKISGEV AKPLTLDHDD LTRRFPLEER IYRMRCVEAW
160 170 180 190 200
SMVVPWIGFP LHKLLALAEP TSNAKYVAFE TIYAPEQMPG QQDRFIGGGL
210 220 230 240 250
KYPYVEGLRL DEAMHPLTLM TVGVYGKALP PQNGAPVRLI VPWKYGFKGI
260 270 280 290 300
KSIVSIKLTR ERPPTTWNLA APDEYGFYAN VNPYVDHPRW SQATERFIGS
310 320 330
GGILDVQRQP TLLFNGYAAQ VASLYRGLDL RENF
Length:334
Mass (Da):37,369
Last modified:February 1, 1997 - v1
Checksum:iA8B5E2AEE28040AD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75037.1.
AP009048 Genomic DNA. Translation: BAE76559.1.
PIRiG64961.
RefSeqiNP_416480.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC75037; AAC75037; b1971.
BAE76559; BAE76559; BAE76559.
GeneIDi946484.
KEGGiecj:JW1954.
eco:b1971.
PATRICi32119273. VBIEscCol129921_2051.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75037.1.
AP009048 Genomic DNA. Translation: BAE76559.1.
PIRiG64961.
RefSeqiNP_416480.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XDQX-ray2.55A/B/C/D/E45-334[»]
1XDYX-ray2.20A/B/C/D/E/F/G/H/I/J45-334[»]
ProteinModelPortaliP76342.
SMRiP76342. Positions 62-330.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259675. 12 interactions.
DIPiDIP-47888N.
IntActiP76342. 2 interactions.
STRINGi511145.b1971.

Proteomic databases

PaxDbiP76342.
PRIDEiP76342.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75037; AAC75037; b1971.
BAE76559; BAE76559; BAE76559.
GeneIDi946484.
KEGGiecj:JW1954.
eco:b1971.
PATRICi32119273. VBIEscCol129921_2051.

Organism-specific databases

EchoBASEiEB3800.
EcoGeneiEG14047. yedY.

Phylogenomic databases

eggNOGiENOG4105CCD. Bacteria.
COG2041. LUCA.
HOGENOMiHOG000255004.
InParanoidiP76342.
KOiK07147.
OMAiDWPYVEG.
OrthoDBiEOG6FBWVX.
PhylomeDBiP76342.

Enzyme and pathway databases

BioCyciEcoCyc:G7059-MONOMER.
ECOL316407:JW1954-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP76342.
PROiP76342.

Family and domain databases

Gene3Di3.90.420.10. 1 hit.
HAMAPiMF_01206. MsrP.
InterProiIPR022867. MsrP.
IPR000572. OxRdtase_Mopterin-bd_dom.
IPR006311. TAT_signal.
[Graphical view]
PfamiPF00174. Oxidored_molyb. 1 hit.
[Graphical view]
SUPFAMiSSF56524. SSF56524. 1 hit.
PROSITEiPS51318. TAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. "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.
  3. "Structural and biochemical identification of a novel bacterial oxidoreductase."
    Loschi L., Brokx S.J., Hills T.L., Zhang G., Bertero M.G., Lovering A.L., Weiner J.H., Strynadka N.C.
    J. Biol. Chem. 279:50391-50400(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 45-50, X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 45-334 IN COMPLEXES WITH MOLYBDOPTERIN AND MOLYBDENUM OR TUNGSTEN, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION BY MASS SPECTROMETRY.
  4. "Export pathway selectivity of Escherichia coli twin arginine translocation signal peptides."
    Tullman-Ercek D., DeLisa M.P., Kawarasaki Y., Iranpour P., Ribnicky B., Palmer T., Georgiou G.
    J. Biol. Chem. 282:8309-8316(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: EXPORT VIA THE TAT-SYSTEM AND THE SEC-SYSTEM.
  5. "Characterization of an Escherichia coli sulfite oxidase homologue reveals the role of a conserved active site cysteine in assembly and function."
    Brokx S.J., Rothery R.A., Zhang G., Ng D.P., Weiner J.H.
    Biochemistry 44:10339-10348(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, EPR SPECTROSCOPY, MUTAGENESIS OF CYS-146, SUBUNIT, INTERACTION WITH MSRQ.
    Strain: K12 / MG1655 / ATCC 47076.
  6. "Spectroscopic characterization of YedY: the role of sulfur coordination in a Mo(V) sulfite oxidase family enzyme form."
    Yang J., Rothery R., Sempombe J., Weiner J.H., Kirk M.L.
    J. Am. Chem. Soc. 131:15612-15614(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF MO ION WITH ELECTRONIC ABSORPTION; MAGNETIC CIRCULAR DICHROISM AND EPR SPECTROSCOPY.
  7. "Repairing oxidized proteins in the bacterial envelope using respiratory chain electrons."
    Gennaris A., Ezraty B., Henry C., Agrebi R., Vergnes A., Oheix E., Bos J., Leverrier P., Espinosa L., Szewczyk J., Vertommen D., Iranzo O., Collet J.F., Barras F.
    Nature 528:409-412(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PROTEIN SUBSTRATES, INDUCTION.
    Strain: K12.

Entry informationi

Entry nameiMSRP_ECOLI
AccessioniPrimary (citable) accession number: P76342
Secondary accession number(s): Q2MAZ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: February 1, 1997
Last modified: May 11, 2016
This is version 124 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Uncharacterized protein families (UPF)
    List of uncharacterized protein family (UPF) entries

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.