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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

Manual assertion based on experiment ini

  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)DescriptionActionsGraphical viewLength
Binding sitei88Molybdopterin1 Publication1
Metal bindingi146Molybdenum1 Publication1
Binding sitei181Molybdopterin1 Publication1
Binding sitei233Molybdopterin1 Publication1
Binding sitei238Molybdopterin1 Publication1

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.
MetaCyc:G7059-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Mutagenesisi146C → S: Loss of enzymatic activity. Enhances binding to MsrQ and targeting to the inner membrane. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 44Tat-type signal1 PublicationAdd BLAST44
ChainiPRO_000007068445 – 334Protein-methionine-sulfoxide reductase catalytic subunit MsrPAdd BLAST290

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 interactors.
DIPiDIP-47888N.
IntActiP76342. 2 interactors.
STRINGi511145.b1971.

Structurei

Secondary structure

1334
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi70 – 72Combined sources3
Helixi81 – 84Combined sources4
Helixi91 – 93Combined sources3
Helixi99 – 103Combined sources5
Helixi104 – 106Combined sources3
Beta strandi113 – 122Combined sources10
Beta strandi124 – 127Combined sources4
Helixi128 – 133Combined sources6
Beta strandi138 – 146Combined sources9
Turni147 – 149Combined sources3
Beta strandi150 – 160Combined sources11
Helixi161 – 168Combined sources8
Beta strandi176 – 181Combined sources6
Turni185 – 187Combined sources3
Helixi189 – 191Combined sources3
Turni194 – 199Combined sources6
Beta strandi205 – 209Combined sources5
Helixi210 – 214Combined sources5
Beta strandi219 – 224Combined sources6
Helixi231 – 233Combined sources3
Beta strandi238 – 240Combined sources3
Helixi246 – 248Combined sources3
Beta strandi252 – 261Combined sources10
Helixi266 – 270Combined sources5
Turni272 – 274Combined sources3
Beta strandi293 – 297Combined sources5
Beta strandi308 – 310Combined sources3
Helixi313 – 316Combined sources4
Helixi318 – 325Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP76342.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni91 – 92Molybdopterin binding1 Publication2
Regioni249 – 251Molybdopterin binding1 Publication3

Sequence similaritiesi

Belongs to the MsrP family.UniRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

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

Family and domain databases

Gene3Di3.90.420.10. 1 hit.
HAMAPiMF_01206. MsrP. 1 hit.
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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259675. 12 interactors.
DIPiDIP-47888N.
IntActiP76342. 2 interactors.
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.
PhylomeDBiP76342.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP76342.
PROiP76342.

Family and domain databases

Gene3Di3.90.420.10. 1 hit.
HAMAPiMF_01206. MsrP. 1 hit.
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...

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: November 2, 2016
This is version 127 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.