MSRP_WOLSU
ID MSRP_WOLSU Reviewed; 311 AA.
AC Q7MR39;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Protein-methionine-sulfoxide reductase catalytic subunit MsrP {ECO:0000255|HAMAP-Rule:MF_01206};
DE EC=1.8.5.- {ECO:0000255|HAMAP-Rule:MF_01206};
DE Flags: Precursor;
GN Name=msrP {ECO:0000255|HAMAP-Rule:MF_01206}; OrderedLocusNames=WS1748;
OS Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC
OS 11488 / FDC 602W) (Vibrio succinogenes).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Wolinella.
OX NCBI_TaxID=273121;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC
RC 11488 / FDC 602W;
RX PubMed=14500908; DOI=10.1073/pnas.1932838100;
RA Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O.,
RA Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B.,
RA Meyer F., Lederer H., Schuster S.C.;
RT "Complete genome sequence and analysis of Wolinella succinogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003).
CC -!- FUNCTION: Part of the MsrPQ system that repairs oxidized periplasmic
CC proteins containing methionine sulfoxide residues (Met-O), using
CC respiratory chain electrons. Thus protects these proteins from
CC oxidative-stress damage caused by reactive species of oxygen and
CC chlorine generated by the host defense mechanisms. MsrPQ is essential
CC for the maintenance of envelope integrity under bleach stress, rescuing
CC a wide series of structurally unrelated periplasmic proteins from
CC methionine oxidation. The catalytic subunit MsrP is non-stereospecific,
CC being able to reduce both (R-) and (S-) diastereoisomers of methionine
CC sulfoxide. {ECO:0000255|HAMAP-Rule:MF_01206}.
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:0000255|HAMAP-Rule:MF_01206};
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:0000255|HAMAP-Rule:MF_01206};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01206};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000255|HAMAP-Rule:MF_01206};
CC -!- SUBUNIT: Heterodimer of a catalytic subunit (MsrP) and a heme-binding
CC subunit (MsrQ). {ECO:0000255|HAMAP-Rule:MF_01206}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_01206}.
CC Note=Is attached to the inner membrane when interacting with the MsrQ
CC subunit. {ECO:0000255|HAMAP-Rule:MF_01206}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC {ECO:0000255|HAMAP-Rule:MF_01206}.
CC -!- SIMILARITY: Belongs to the MsrP family. {ECO:0000255|HAMAP-
CC Rule:MF_01206}.
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DR EMBL; BX571661; CAE10770.1; -; Genomic_DNA.
DR RefSeq; WP_011139553.1; NC_005090.1.
DR AlphaFoldDB; Q7MR39; -.
DR SMR; Q7MR39; -.
DR STRING; 273121.WS1748; -.
DR EnsemblBacteria; CAE10770; CAE10770; WS1748.
DR KEGG; wsu:WS1748; -.
DR eggNOG; COG2041; Bacteria.
DR HOGENOM; CLU_045520_0_0_7; -.
DR OMA; WPYTEGL; -.
DR OrthoDB; 1729032at2; -.
DR Proteomes; UP000000422; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016672; F:oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0030091; P:protein repair; IEA:UniProtKB-UniRule.
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 Pfam; PF00174; Oxidored_molyb; 1.
DR SUPFAM; SSF56524; SSF56524; 1.
PE 3: Inferred from homology;
KW Metal-binding; Molybdenum; Oxidoreductase; Periplasm; Reference proteome;
KW Signal.
FT SIGNAL 1..45
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT CHAIN 46..311
FT /note="Protein-methionine-sulfoxide reductase catalytic
FT subunit MsrP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT /id="PRO_0000070700"
FT BINDING 75..76
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT BINDING 129
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT BINDING 164
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT BINDING 215
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT BINDING 220
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT BINDING 231..233
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
SQ SEQUENCE 311 AA; 35143 MW; 4523F4D4EC9464BC CRC64;
MKPKPSDVTP KELFDQRRSF LKLGAASVVA TGSVSNLLAA LKTKAPSPLS FIPSENLENL
KPNSFEQASG YVNFYEFSTS KTAPVGLSKT LRPYPWELLA SGEVENPQSL SIDELYQFPL
EERIYRFRCV EGWSMVVPWI GFPLSALLER LKPTTKARYV KFTTLLDPTQ FPDQKRGALG
VIPHPYVEGL RLDEAMHPLT LLAVGMYGEK LPAQNGAPLR LIVPWKYGFK SIKSIAKIEL
TQEEPLNTWK LLNPREYGFY ANVNPEVDHP RWSQASERLL GSLLKQKTLK FNGYEKEVAS
LYAGMDLKRD F
