MSRP_AZOOP
ID MSRP_AZOOP Reviewed; 312 AA.
AC G8QMC2;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 1.
DT 03-AUG-2022, entry version 59.
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 Synonyms=yedY2 {ECO:0000303|PubMed:25968643}; OrderedLocusNames=Dsui_1300;
OS Azospira oryzae (strain ATCC BAA-33 / DSM 13638 / PS) (Dechlorosoma
OS suillum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Azospira.
OX NCBI_TaxID=640081;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-33 / DSM 13638 / PS;
RX PubMed=22535943; DOI=10.1128/jb.00124-12;
RA Byrne-Bailey K.G., Coates J.D.;
RT "Complete genome sequence of the anaerobic perchlorate-reducing bacterium
RT Azospira suillum strain PS.";
RL J. Bacteriol. 194:2767-2768(2012).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-33 / DSM 13638 / PS;
RX PubMed=25968643; DOI=10.1128/mbio.00233-15;
RA Melnyk R.A., Youngblut M.D., Clark I.C., Carlson H.K., Wetmore K.M.,
RA Price M.N., Iavarone A.T., Deutschbauer A.M., Arkin A.P., Coates J.D.;
RT "Novel mechanism for scavenging of hypochlorite involving a periplasmic
RT methionine-rich peptide and methionine sulfoxide reductase.";
RL MBio 6:E00233-E00233(2015).
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 (By similarity). Involved in protection against reactive
CC chlorine species (RCS) generated by chlorite and hypochlorite
CC (PubMed:25968643). {ECO:0000255|HAMAP-Rule:MF_01206,
CC ECO:0000269|PubMed:25968643}.
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 -!- DISRUPTION PHENOTYPE: No effect when grown in presence of chlorite,
CC growth of a double sigF-yedY2 mutant is completely inhibited by 20 mM
CC chlorite. {ECO:0000269|PubMed:25968643}.
CC -!- SIMILARITY: Belongs to the MsrP family. {ECO:0000255|HAMAP-
CC Rule:MF_01206}.
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DR EMBL; CP003153; AEV25700.1; -; Genomic_DNA.
DR RefSeq; WP_014236401.1; NC_016616.1.
DR AlphaFoldDB; G8QMC2; -.
DR SMR; G8QMC2; -.
DR STRING; 640081.Dsui_1300; -.
DR EnsemblBacteria; AEV25700; AEV25700; Dsui_1300.
DR KEGG; dsu:Dsui_1300; -.
DR eggNOG; COG2041; Bacteria.
DR HOGENOM; CLU_045520_0_0_4; -.
DR OMA; WPYTEGL; -.
DR OrthoDB; 1729032at2; -.
DR Proteomes; UP000005633; 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 InterPro; IPR019546; TAT_signal_bac_arc.
DR Pfam; PF00174; Oxidored_molyb; 1.
DR SUPFAM; SSF56524; SSF56524; 1.
DR TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Metal-binding; Molybdenum; Oxidoreductase; Periplasm; Reference proteome;
KW Signal.
FT SIGNAL 1..47
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 48..312
FT /note="Protein-methionine-sulfoxide reductase catalytic
FT subunit MsrP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT /id="PRO_0000440889"
FT BINDING 74
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT BINDING 77..78
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT BINDING 133
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 168
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT BINDING 216
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT BINDING 221
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT BINDING 232..234
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
SQ SEQUENCE 312 AA; 35047 MW; F427A01ABA7A1064 CRC64;
MLIRRPPDLL PSEITPEPLA RGRRALLKGL GAGAALAGLG LPQISQAGSL GTLRPSPLSS
DEKLTPLKSV TGYNNFYEFG TDKEDPARHA PGRLKTRPWT VTVEGEIKRP RTFSIDDLLK
LAPLEERIYR MRCVEGWSMV IPWVGFPLAE LIRQVEPNGQ ARFVEFVTLA DPQQMPGVRS
PLLDWPYVEG LRLDEAQHPL TLLAVGLYGE VLPAQNGAPI RLVVPWKYGF KSAKSIVRIR
FVREQPRSTW MKAGPSEYGF YSNVNPAVDH PRWSQATERR IGEFIKRKTL PFNGYADQVA
GLYSGMDLRR FF
