HAMAP rule MF_01206
General rule information
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| PURL | https://purl.expasy.org/hamap/rule/MF_01206 |
| Accession | MF_01206 |
| Dates | 28-FEB-2005 (Created)
03-SEP-2024 (Last updated, Version 34) |
| Name | MsrP |
| Scope(s) |
Bacteria |
| Template(s) | P76342; [ 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=L-methionyl-[protein] + a quinone + H2O = L-methionyl-(S)-S- oxide-[protein] + a quinol; 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=L-methionyl-[protein] + a quinone + H2O = L-methionyl-(R)-S- oxide-[protein] + a quinol; 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 |