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Protein-methionine-sulfoxide reductase catalytic subunit MsrP (EC 1.8.5.-)

 A0A166AUD9_9RHOB        Unreviewed;       324 AA.
A0A166AUD9;
06-JUL-2016, integrated into UniProtKB/TrEMBL.
06-JUL-2016, sequence version 1.
25-OCT-2017, entry version 13.
RecName: Full=Protein-methionine-sulfoxide reductase catalytic subunit MsrP {ECO:0000256|HAMAP-Rule:MF_01206, ECO:0000256|SAAS:SAAS00634581};
EC=1.8.5.- {ECO:0000256|HAMAP-Rule:MF_01206, ECO:0000256|SAAS:SAAS00634589};
Name=yedY {ECO:0000313|EMBL:KZL21562.1};
Synonyms=msrP {ECO:0000256|HAMAP-Rule:MF_01206};
ORFNames=PsAD2_00861 {ECO:0000313|EMBL:KZL21562.1};
Pseudovibrio axinellae.
Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
Rhodobacteraceae; Pseudovibrio.
NCBI_TaxID=989403 {ECO:0000313|EMBL:KZL21562.1, ECO:0000313|Proteomes:UP000076577};
[1] {ECO:0000313|EMBL:KZL21562.1, ECO:0000313|Proteomes:UP000076577}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Ad2 {ECO:0000313|EMBL:KZL21562.1,
ECO:0000313|Proteomes:UP000076577};
PubMed=27065959; DOI=10.3389/fmicb.2016.00387;
Romano S., Fernandez-Guerra A., Reen F.J., Glockner F.O.,
Crowley S.P., O'Sullivan O., Cotter P.D., Adams C., Dobson A.D.,
O'Gara F.;
"Comparative Genomic Analysis Reveals a Diverse Repertoire of Genes
Involved in Prokaryote-Eukaryote Interactions within the Pseudovibrio
Genus.";
Front. Microbiol. 7:387-387(2016).
-!- 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.
{ECO:0000256|HAMAP-Rule:MF_01206}.
-!- CATALYTIC ACTIVITY: [Protein]-L-methionine + a quinone + H(2)O =
[protein]-L-methionine (R)-S-oxide + a quinol. {ECO:0000256|HAMAP-
Rule:MF_01206, ECO:0000256|SAAS:SAAS00634593}.
-!- CATALYTIC ACTIVITY: [Protein]-L-methionine + a quinone + H(2)O =
[protein]-L-methionine (S)-S-oxide + a quinol. {ECO:0000256|HAMAP-
Rule:MF_01206}.
-!- COFACTOR:
Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
Evidence={ECO:0000256|HAMAP-Rule:MF_01206};
Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
{ECO:0000256|HAMAP-Rule:MF_01206};
-!- SUBUNIT: Heterodimer of a catalytic subunit (MsrP) and a heme-
binding subunit (MsrQ). {ECO:0000256|HAMAP-Rule:MF_01206,
ECO:0000256|SAAS:SAAS00634585}.
-!- PTM: Predicted to be exported by the Tat system. The position of
the signal peptide cleavage has not been experimentally proven.
{ECO:0000256|HAMAP-Rule:MF_01206}.
-!- SIMILARITY: Belongs to the MsrP family. {ECO:0000256|HAMAP-
Rule:MF_01206, ECO:0000256|SAAS:SAAS00634598}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01206}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KZL21562.1}.
-----------------------------------------------------------------------
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EMBL; LMCB01000004; KZL21562.1; -; Genomic_DNA.
RefSeq; WP_068002628.1; NZ_LMCB01000004.1.
EnsemblBacteria; KZL21562; KZL21562; PsAD2_00861.
PATRIC; fig|989403.3.peg.916; -.
Proteomes; UP000076577; Unassembled WGS sequence.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0043546; F:molybdopterin cofactor binding; IEA:UniProtKB-UniRule.
GO; GO:0016672; F:oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
GO; GO:0042128; P:nitrate assimilation; IEA:InterPro.
GO; GO:0030091; P:protein repair; IEA:UniProtKB-UniRule.
Gene3D; 3.90.420.10; -; 1.
HAMAP; MF_01206; MsrP; 1.
InterPro; IPR022867; MsrP.
InterPro; IPR000572; OxRdtase_Mopterin-bd_dom.
InterPro; IPR036374; OxRdtase_Mopterin-bd_sf.
InterPro; IPR006311; TAT_signal.
InterPro; IPR019546; TAT_signal_bac_arc.
Pfam; PF00174; Oxidored_molyb; 1.
SUPFAM; SSF56524; SSF56524; 1.
TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
PROSITE; PS51318; TAT; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000076577};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01206,
ECO:0000256|SAAS:SAAS00634574};
Molybdenum {ECO:0000256|HAMAP-Rule:MF_01206,
ECO:0000256|SAAS:SAAS00634600};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01206,
ECO:0000256|SAAS:SAAS00634602, ECO:0000313|EMBL:KZL21562.1};
Signal {ECO:0000256|HAMAP-Rule:MF_01206}.
DOMAIN 106 261 Oxidored_molyb.
{ECO:0000259|Pfam:PF00174}.
REGION 90 91 Molybdopterin binding.
{ECO:0000256|HAMAP-Rule:MF_01206}.
REGION 243 245 Molybdopterin binding.
{ECO:0000256|HAMAP-Rule:MF_01206}.
METAL 144 144 Molybdenum. {ECO:0000256|HAMAP-
Rule:MF_01206}.
BINDING 87 87 Molybdopterin. {ECO:0000256|HAMAP-
Rule:MF_01206}.
BINDING 179 179 Molybdopterin. {ECO:0000256|HAMAP-
Rule:MF_01206}.
BINDING 232 232 Molybdopterin. {ECO:0000256|HAMAP-
Rule:MF_01206}.
SEQUENCE 324 AA; 36670 MW; C8B773187FA82359 CRC64;
MNVIHRPEWI IPEREATPEG VFFNRRRFMK GLGAVGLGLA AGGPALMGNA FAQDGPDPTL
GLYPAKRNEA FTLKRAITPE SVTSVYNNFY EFGSHKRISR AAQALKIRPW AITIDGMVDN
PQTIDFDDLI KKMSLQERLY RHRCVEAWAM AVPWTGFPLS ELVKYAGPKN GAKYVRFETF
EDPDVASGQK QFWYPWPYVE GVSMAEAMND LAFVATGIYG KPLLKQYGAP IRLVLPWKYG
FKSIKSIVKI TFTDQRPVGF WEKIGASEYG FWANVNPEVP HPRWSQATER LLGTNERVPT
QLYNGYGAQV AQLYTNMDGQ NLFR


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