MSRP_ECOLI
ID MSRP_ECOLI Reviewed; 334 AA.
AC P76342; Q2MAZ7;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Protein-methionine-sulfoxide reductase catalytic subunit MsrP {ECO:0000255|HAMAP-Rule:MF_01206, ECO:0000305|PubMed:26641313};
DE EC=1.8.5.- {ECO:0000255|HAMAP-Rule:MF_01206, ECO:0000269|PubMed:26641313};
DE Flags: Precursor;
GN Name=msrP {ECO:0000303|PubMed:26641313};
GN Synonyms=yedY {ECO:0000312|EMBL:AAC75037.1};
GN OrderedLocusNames=b1971, JW1954;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP PROTEIN SEQUENCE OF 45-50, X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 45-334
RP IN COMPLEXES WITH MOLYBDOPTERIN AND MOLYBDENUM OR TUNGSTEN, FUNCTION,
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15355966; DOI=10.1074/jbc.m408876200;
RA Loschi L., Brokx S.J., Hills T.L., Zhang G., Bertero M.G., Lovering A.L.,
RA Weiner J.H., Strynadka N.C.;
RT "Structural and biochemical identification of a novel bacterial
RT oxidoreductase.";
RL J. Biol. Chem. 279:50391-50400(2004).
RN [4]
RP EXPORT VIA THE TAT-SYSTEM AND THE SEC-SYSTEM.
RX PubMed=17218314; DOI=10.1074/jbc.m610507200;
RA Tullman-Ercek D., DeLisa M.P., Kawarasaki Y., Iranpour P., Ribnicky B.,
RA Palmer T., Georgiou G.;
RT "Export pathway selectivity of Escherichia coli twin arginine translocation
RT signal peptides.";
RL J. Biol. Chem. 282:8309-8316(2007).
RN [5]
RP SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, EPR SPECTROSCOPY, MUTAGENESIS
RP OF CYS-146, SUBUNIT, AND INTERACTION WITH MSRQ.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=16042411; DOI=10.1021/bi050621a;
RA Brokx S.J., Rothery R.A., Zhang G., Ng D.P., Weiner J.H.;
RT "Characterization of an Escherichia coli sulfite oxidase homologue reveals
RT the role of a conserved active site cysteine in assembly and function.";
RL Biochemistry 44:10339-10348(2005).
RN [6]
RP CHARACTERIZATION OF MO ION WITH ELECTRONIC ABSORPTION; MAGNETIC CIRCULAR
RP DICHROISM AND EPR SPECTROSCOPY.
RX PubMed=19860477; DOI=10.1021/ja903087k;
RA Yang J., Rothery R., Sempombe J., Weiner J.H., Kirk M.L.;
RT "Spectroscopic characterization of YedY: the role of sulfur coordination in
RT a Mo(V) sulfite oxidase family enzyme form.";
RL J. Am. Chem. Soc. 131:15612-15614(2009).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PROTEIN
RP SUBSTRATES, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=26641313; DOI=10.1038/nature15764;
RA Gennaris A., Ezraty B., Henry C., Agrebi R., Vergnes A., Oheix E., Bos J.,
RA Leverrier P., Espinosa L., Szewczyk J., Vertommen D., Iranzo O.,
RA Collet J.F., Barras F.;
RT "Repairing oxidized proteins in the bacterial envelope using respiratory
RT chain electrons.";
RL Nature 528:409-412(2015).
CC -!- FUNCTION: Part of the MsrPQ system that repairs oxidized periplasmic
CC proteins containing methionine sulfoxide residues (Met-O), using
CC respiratory chain electrons (PubMed:26641313). Thus protects these
CC proteins from oxidative-stress damage caused by reactive species of
CC oxygen and chlorine (PubMed:26641313). MsrPQ is essential for the
CC maintenance of envelope integrity under bleach stress, rescuing a wide
CC series of structurally unrelated periplasmic proteins from methionine
CC oxidation, including the primary periplasmic chaperone SurA and the
CC lipoprotein Pal (PubMed:26641313). The catalytic subunit MsrP is non-
CC stereospecific, being able to reduce both (R-) and (S-)
CC diastereoisomers of methionine sulfoxide (PubMed:26641313). Can
CC catalyze the reduction of a variety of substrates in vitro, including
CC dimethyl sulfoxide, trimethylamine N-oxide, phenylmethyl sulfoxide and
CC L-methionine sulfoxide (PubMed:15355966). Cannot reduce cyclic N-oxides
CC (PubMed:15355966). Shows no activity as sulfite oxidase
CC (PubMed:15355966). {ECO:0000269|PubMed:15355966,
CC ECO:0000269|PubMed:26641313}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + H2O + L-methionyl-[protein] = a quinol + L-
CC methionyl-(S)-S-oxide-[protein]; Xref=Rhea:RHEA:51292, Rhea:RHEA-
CC COMP:12313, Rhea:RHEA-COMP:12315, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16044, ChEBI:CHEBI:24646, ChEBI:CHEBI:44120,
CC ChEBI:CHEBI:132124; Evidence={ECO:0000269|PubMed:26641313};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + H2O + L-methionyl-[protein] = a quinol + L-
CC methionyl-(R)-S-oxide-[protein]; Xref=Rhea:RHEA:51296, Rhea:RHEA-
CC COMP:12313, Rhea:RHEA-COMP:12314, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16044, ChEBI:CHEBI:24646, ChEBI:CHEBI:45764,
CC ChEBI:CHEBI:132124; Evidence={ECO:0000269|PubMed:26641313};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC Evidence={ECO:0000269|PubMed:15355966};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. The
CC oxidation state of Mo is +5. Is inactive in the presence of the
CC tungsten-substituted form (W-MPT) of the cofactor.
CC {ECO:0000269|PubMed:15355966};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12 mM for dimethyl sulfoxide {ECO:0000269|PubMed:15355966};
CC KM=22 mM for trimethylamine N-oxide {ECO:0000269|PubMed:15355966};
CC KM=27.9 mM for tetramethylene sulfoxide
CC {ECO:0000269|PubMed:15355966};
CC KM=119 mM for L-methionine sulfoxide {ECO:0000269|PubMed:15355966};
CC KM=3.8 mM for N-acetyl-Met-O {ECO:0000269|PubMed:26641313};
CC KM=8.0 mM for L-methionine (S)-S-oxide {ECO:0000269|PubMed:26641313};
CC KM=25.7 mM for L-methionine (R)-S-oxide
CC {ECO:0000269|PubMed:26641313};
CC Vmax=56.3 umol/min/mg enzyme with N-acetyl-Met-O as substrate
CC {ECO:0000269|PubMed:26641313};
CC Vmax=67.2 umol/min/mg enzyme with L-methionine (S)-S-oxide as
CC substrate {ECO:0000269|PubMed:26641313};
CC Vmax=313.4 umol/min/mg enzyme with L-methionine (R)-S-oxide as
CC substrate {ECO:0000269|PubMed:26641313};
CC Note=kcat is 30.5 sec(-1) with N-acetyl-Met-O as substrate. kcat is
CC 36.0 sec(-1) with L-methionine (S)-S-oxide as substrate. kcat is
CC 168.3 sec(-1) with L-methionine (R)-S-oxide as substrate.
CC {ECO:0000269|PubMed:26641313};
CC -!- SUBUNIT: Heterodimer of a catalytic subunit (MsrP) and a heme-binding
CC subunit (MsrQ). {ECO:0000269|PubMed:16042411}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:16042411}. Note=Is
CC attached to the inner membrane when interacting with the MsrQ subunit.
CC -!- INDUCTION: Is induced at protein level by hypochlorous acid (HOCl), a
CC powerful antimicrobial released by neutrophils, but not by H(2)O(2).
CC Induction by HOCl is dependent on the presence of a functional
CC YedV/YedW two-component system. {ECO:0000269|PubMed:26641313}.
CC -!- PTM: Exported by the Tat system. Can also be exported by the Sec
CC system. {ECO:0000269|PubMed:17218314}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking the msrPQ genes display no visible
CC growth defect. {ECO:0000269|PubMed:16042411}.
CC -!- SIMILARITY: Belongs to the MsrP family. {ECO:0000255|HAMAP-
CC Rule:MF_01206}.
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DR EMBL; U00096; AAC75037.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76559.1; -; Genomic_DNA.
DR PIR; G64961; G64961.
DR RefSeq; NP_416480.1; NC_000913.3.
DR RefSeq; WP_000740106.1; NZ_CP064683.1.
DR PDB; 1XDQ; X-ray; 2.55 A; A/B/C/D/E=45-334.
DR PDB; 1XDY; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J=45-334.
DR PDBsum; 1XDQ; -.
DR PDBsum; 1XDY; -.
DR AlphaFoldDB; P76342; -.
DR SMR; P76342; -.
DR BioGRID; 4259675; 54.
DR DIP; DIP-47888N; -.
DR IntAct; P76342; 2.
DR STRING; 511145.b1971; -.
DR jPOST; P76342; -.
DR PaxDb; P76342; -.
DR PRIDE; P76342; -.
DR EnsemblBacteria; AAC75037; AAC75037; b1971.
DR EnsemblBacteria; BAE76559; BAE76559; BAE76559.
DR GeneID; 946484; -.
DR KEGG; ecj:JW1954; -.
DR KEGG; eco:b1971; -.
DR PATRIC; fig|511145.12.peg.2051; -.
DR EchoBASE; EB3800; -.
DR eggNOG; COG2041; Bacteria.
DR HOGENOM; CLU_045520_0_0_6; -.
DR InParanoid; P76342; -.
DR PhylomeDB; P76342; -.
DR BioCyc; EcoCyc:G7059-MON; -.
DR BioCyc; MetaCyc:G7059-MON; -.
DR BRENDA; 1.8.5.B1; 2026.
DR EvolutionaryTrace; P76342; -.
DR PRO; PR:P76342; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IDA:EcoCyc.
DR GO; GO:0016675; F:oxidoreductase activity, acting on a heme group of donors; IDA:EcoCyc.
DR GO; GO:0016672; F:oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor; IGI:UniProtKB.
DR GO; GO:0030091; P:protein repair; IDA:UniProtKB.
DR GO; GO:1901530; P:response to hypochlorite; IDA:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IEP:EcoCyc.
DR Gene3D; 3.90.420.10; -; 1.
DR HAMAP; MF_01206; MsrP; 1.
DR InterPro; IPR022867; MsrP.
DR InterPro; IPR000572; OxRdtase_Mopterin-bd_dom.
DR InterPro; IPR036374; OxRdtase_Mopterin-bd_sf.
DR InterPro; IPR006311; TAT_signal.
DR Pfam; PF00174; Oxidored_molyb; 1.
DR SUPFAM; SSF56524; SSF56524; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Metal-binding; Molybdenum;
KW Oxidoreductase; Periplasm; Reference proteome; Signal.
FT SIGNAL 1..44
FT /note="Tat-type signal"
FT /evidence="ECO:0000269|PubMed:17218314"
FT CHAIN 45..334
FT /note="Protein-methionine-sulfoxide reductase catalytic
FT subunit MsrP"
FT /id="PRO_0000070684"
FT BINDING 88
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000269|PubMed:15355966"
FT BINDING 91..92
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000269|PubMed:15355966"
FT BINDING 146
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000269|PubMed:15355966"
FT BINDING 181
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000269|PubMed:15355966"
FT BINDING 233
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000269|PubMed:15355966"
FT BINDING 238
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000269|PubMed:15355966"
FT BINDING 249..251
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000269|PubMed:15355966"
FT MUTAGEN 146
FT /note="C->S: Loss of enzymatic activity. Enhances binding
FT to MsrQ and targeting to the inner membrane."
FT /evidence="ECO:0000269|PubMed:16042411"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:1XDY"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:1XDY"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:1XDY"
FT HELIX 99..103
FT /evidence="ECO:0007829|PDB:1XDY"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:1XDY"
FT STRAND 113..122
FT /evidence="ECO:0007829|PDB:1XDY"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:1XDY"
FT HELIX 128..133
FT /evidence="ECO:0007829|PDB:1XDY"
FT STRAND 138..146
FT /evidence="ECO:0007829|PDB:1XDY"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:1XDY"
FT STRAND 150..160
FT /evidence="ECO:0007829|PDB:1XDY"
FT HELIX 161..168
FT /evidence="ECO:0007829|PDB:1XDY"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:1XDY"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:1XDY"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:1XDY"
FT TURN 194..199
FT /evidence="ECO:0007829|PDB:1XDY"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:1XDY"
FT HELIX 210..214
FT /evidence="ECO:0007829|PDB:1XDY"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:1XDY"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:1XDY"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:1XDY"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:1XDY"
FT STRAND 252..261
FT /evidence="ECO:0007829|PDB:1XDY"
FT HELIX 266..270
FT /evidence="ECO:0007829|PDB:1XDY"
FT TURN 272..274
FT /evidence="ECO:0007829|PDB:1XDY"
FT STRAND 293..297
FT /evidence="ECO:0007829|PDB:1XDY"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:1XDQ"
FT HELIX 313..316
FT /evidence="ECO:0007829|PDB:1XDY"
FT HELIX 318..325
FT /evidence="ECO:0007829|PDB:1XDY"
SQ SEQUENCE 334 AA; 37369 MW; A8B5E2AEE28040AD CRC64;
MKKNQFLKES DVTAESVFFM KRRQVLKALG ISATALSLPH AAHADLLSWF KGNDRPPAPA
GKALEFSKPA AWQNNLPLTP ADKVSGYNNF YEFGLDKADP AANAGSLKTD PWTLKISGEV
AKPLTLDHDD LTRRFPLEER IYRMRCVEAW SMVVPWIGFP LHKLLALAEP TSNAKYVAFE
TIYAPEQMPG QQDRFIGGGL KYPYVEGLRL DEAMHPLTLM TVGVYGKALP PQNGAPVRLI
VPWKYGFKGI KSIVSIKLTR ERPPTTWNLA APDEYGFYAN VNPYVDHPRW SQATERFIGS
GGILDVQRQP TLLFNGYAAQ VASLYRGLDL RENF
