HAMAP rule MF_01206
General rule information
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Accession | MF_01206 |
Dates | 15-MAR-2002 (Created)
1-JUN-2023 (Last updated, Version 39) |
Name | MsrP |
Scope(s) |
Bacteria |
Template(s) | P76342 (MSRP_ECOLI); [ Recover all ] |
Triggered by |
HAMAP; MF_01206 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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Identifier | MSRP |
Protein name | RecName: Full=Protein-methionine-sulfoxide reductase catalytic subunit MsrP; EC=1.8.5.-; Flags: Precursor; |
Gene name | Name=msrP; |
Comments
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case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella> | |
FUNCTION | Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. 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. The catalytic subunit MsrP is non- stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide. |
else case <OC:Pseudomonadota> | |
FUNCTION | Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide. |
else | |
FUNCTION | Part of the MsrPQ system that repairs oxidized cell envelope proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide. |
end case | |
CATALYTIC ACTIVITY | Reaction=a quinone + H2O + L-methionyl-[protein] = a quinol + L- methionyl-(S)-S-oxide-[protein]; Xref=Rhea:RHEA:51292, Rhea:RHEA- COMP:12313, Rhea:RHEA-COMP:12315, ChEBI:CHEBI:15377, ChEBI:CHEBI:16044, ChEBI:CHEBI:24646, ChEBI:CHEBI:44120, ChEBI:CHEBI:132124; |
CATALYTIC ACTIVITY | Reaction=a quinone + H2O + L-methionyl-[protein] = a quinol + L- methionyl-(R)-S-oxide-[protein]; Xref=Rhea:RHEA:51296, Rhea:RHEA- COMP:12313, Rhea:RHEA-COMP:12314, ChEBI:CHEBI:15377, ChEBI:CHEBI:16044, ChEBI:CHEBI:24646, ChEBI:CHEBI:45764, ChEBI:CHEBI:132124; |
COFACTOR | Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.; |
SUBUNIT | Heterodimer of a catalytic subunit (MsrP) and a heme-binding subunit (MsrQ). |
case defined <Property:Membrane> and <Property:Membrane=2> | |
SUBCELLULAR LOCATION | Periplasm. Note=Is attached to the inner membrane when interacting with the MsrQ subunit. |
end case | |
case <Property:Membrane=1> and <Feature:PS51318> | |
SUBCELLULAR LOCATION | Cell envelope. Note=Is attached to the cell membrane when interacting with the MsrQ subunit. |
PTM | Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. |
else case <Feature:PS51318> | |
PTM | Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. |
end case | |
SIMILARITY | Belongs to the MsrP family. |
Keywords
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Metal-binding | |
Molybdenum | |
Oxidoreductase | |
case defined <Property:Membrane> and <Property:Membrane=2> | |
Periplasm | |
end case | |
Signal |
Gene Ontology
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GO:0016672; Molecular function:oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor | |
GO:0043546; Molecular function:molybdopterin cofactor binding | |
GO:0030091; Biological process:protein repair | |
case defined <Property:Membrane> and <Property:Membrane=2> | |
GO:0042597; Cellular component:periplasmic space | |
end case |
Cross-references
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Pfam | PF00174; Oxidored_molyb; 1; |
NCBIfam | TIGR01409; TAT_signal_seq; 1; |
PROSITE | PS51318; TAT; 0-1; |
General | Signal; -; 1; |
Features
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From: MSRP_ECOLI (P76342) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 91 | 92 | /ligand="Mo-molybdopterin" /ligand_id="ChEBI:CHEBI:71302" |
Y-E | ||||||||
BINDING | 249 | 251 | /ligand="Mo-molybdopterin" /ligand_id="ChEBI:CHEBI:71302" |
x-x-K | ||||||||
BINDING | 146 | 146 | /ligand="Mo-molybdopterin" /ligand_id="ChEBI:CHEBI:71302" /ligand_part="Mo" /ligand_part_id="ChEBI:CHEBI:28685" |
C | ||||||||
BINDING | 88 | 88 | /ligand="Mo-molybdopterin" /ligand_id="ChEBI:CHEBI:71302" |
N | ||||||||
BINDING | 181 | 181 | /ligand="Mo-molybdopterin" /ligand_id="ChEBI:CHEBI:71302" |
[TS] | ||||||||
BINDING | 233 | 233 | /ligand="Mo-molybdopterin" /ligand_id="ChEBI:CHEBI:71302" |
N | ||||||||
BINDING | 238 | 238 | /ligand="Mo-molybdopterin" /ligand_id="ChEBI:CHEBI:71302" |
R |
Additional information
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Size range | 297-366 amino acids |
Related rules |
None |
Fusion | Nter: None Cter: None |