AC MF_01206; DC Protein; auto TR HAMAP; MF_01206; -; 1; level=0 XX Names: MsrP XX ID MSRP DE RecName: Full=Protein-methionine-sulfoxide reductase catalytic subunit MsrP; DE EC=1.8.5.-; DE Flags: Precursor; GN Name=msrP; XX case or or 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, including the primary periplasmic chaperone SurA CC and the lipoprotein Pal. The catalytic subunit MsrP is non- CC stereospecific, being able to reduce both (R-) and (S-) CC diastereoisomers of methionine sulfoxide. else case 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. else CC -!- FUNCTION: Part of the MsrPQ system that repairs oxidized cell envelope 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. MsrPQ is essential for the maintenance of envelope integrity CC under bleach stress, rescuing a wide series of structurally unrelated CC cell envelope proteins from methionine oxidation. The catalytic subunit CC MsrP is non-stereospecific, being able to reduce both (R-) and (S-) CC diastereoisomers of methionine sulfoxide. end case 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; 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; CC -!- COFACTOR: CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.; CC -!- SUBUNIT: Heterodimer of a catalytic subunit (MsrP) and a heme-binding CC subunit (MsrQ). case defined and CC -!- SUBCELLULAR LOCATION: Periplasm. Note=Is attached to the inner membrane CC when interacting with the MsrQ subunit. end case case and CC -!- SUBCELLULAR LOCATION: Cell envelope. Note=Is attached to the cell CC membrane when interacting with the MsrQ subunit. CC -!- PTM: Predicted to be exported by the Tat system. The position of the CC signal peptide cleavage has not been experimentally proven. else case CC -!- PTM: Predicted to be exported by the Tat system. The position of the CC signal peptide cleavage has not been experimentally proven. end case CC -!- SIMILARITY: Belongs to the MsrP family. XX DR Pfam; PF00174; Oxidored_molyb; 1; trigger=no DR NCBIfam; TIGR01409; TAT_signal_seq; 1; trigger=no DR PROSITE; PS51318; TAT; 0-1; trigger=yes case not DR General; Signal; -; 1; trigger=yes end case XX KW Metal-binding KW Molybdenum KW Oxidoreductase case defined and KW Periplasm end case KW Signal XX GO GO:0016672; F:oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor GO GO:0043546; F:molybdopterin cofactor binding GO GO:0030091; P:protein repair case defined and GO GO:0042597; C:periplasmic space end case XX FT From: MSRP_ECOLI (P76342) FT BINDING 91..92 FT /ligand="Mo-molybdopterin" FT /ligand_id="ChEBI:CHEBI:71302" FT Condition: Y-E FT BINDING 249..251 FT /ligand="Mo-molybdopterin" FT /ligand_id="ChEBI:CHEBI:71302" FT Condition: x-x-K 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 Condition: C FT BINDING 88 FT /ligand="Mo-molybdopterin" FT /ligand_id="ChEBI:CHEBI:71302" FT Optional; Condition: N FT BINDING 181 FT /ligand="Mo-molybdopterin" FT /ligand_id="ChEBI:CHEBI:71302" FT Optional; Condition: [TS] FT BINDING 233 FT /ligand="Mo-molybdopterin" FT /ligand_id="ChEBI:CHEBI:71302" FT Condition: N FT BINDING 238 FT /ligand="Mo-molybdopterin" FT /ligand_id="ChEBI:CHEBI:71302" FT Condition: R XX Size: 297-366; Related: None; Template: P76342; Scope: Bacteria Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.39 2023/06/01 //