MSRP_RHIE6
ID MSRP_RHIE6 Reviewed; 315 AA.
AC B3PWV0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
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};
GN OrderedLocusNames=RHECIAT_CH0001778;
OS Rhizobium etli (strain CIAT 652).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=491916;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIAT 652;
RA Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P.,
RA Hernandez-Gonzalez I.L., Fernandez J.L., Diaz R., Flores M., Mora J.,
RA Palacios R., Davila G.;
RT "Genome diversity and DNA divergence of Rhizobium etli.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001074; ACE90748.1; -; Genomic_DNA.
DR RefSeq; WP_012483485.1; NC_010994.1.
DR AlphaFoldDB; B3PWV0; -.
DR SMR; B3PWV0; -.
DR EnsemblBacteria; ACE90748; ACE90748; RHECIAT_CH0001778.
DR GeneID; 45957098; -.
DR KEGG; rec:RHECIAT_CH0001778; -.
DR eggNOG; COG2041; Bacteria.
DR HOGENOM; CLU_045520_0_0_5; -.
DR OMA; WPYTEGL; -.
DR Proteomes; UP000008817; 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 InterPro; IPR006311; TAT_signal.
DR Pfam; PF00174; Oxidored_molyb; 1.
DR SUPFAM; SSF56524; SSF56524; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Metal-binding; Molybdenum; Oxidoreductase; Periplasm; Signal.
FT SIGNAL 1..45
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT CHAIN 46..315
FT /note="Protein-methionine-sulfoxide reductase catalytic
FT subunit MsrP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT /id="PRO_1000138719"
FT BINDING 71
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT BINDING 74..75
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 214
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT BINDING 219
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT BINDING 230..232
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
SQ SEQUENCE 315 AA; 35137 MW; 6D1200579D2E8BAD CRC64;
MPSYRPPKIA SSEITPRRIY MRRREFLGAA ALGAVALYGA GKASAAALPA VESKYKLDEK
PTPLKDVTTY NNFYEFGLDK GDPAANSGAF KPLPWTVKVD GMVNKPGTFD LEALMKEFPI
EERTYRMRCV EAWSMVIPWD GFPLASLLDK VEPLGSAKYV AFETIVRPEE MPGQKGFFQS
LDWPYVEGLR LDEARHPLTL LAVGLYGETL ANQNGAPIRL VVPWKYGFKG IKSIVRITLT
DQQPKNTWQV TNPQEYGFYA NVNPAVDHPR WSQASERRIG EGGFFGASRH PTLPFNGYAD
EVASLYAGMD LKANF
