(data stored in ACNUC7421 zone)

SWISSPROT: A1AY36_PARDP

ID   A1AY36_PARDP            Unreviewed;       298 AA.
AC   A1AY36;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 86.
DE   RecName: Full=Protein-methionine-sulfoxide reductase catalytic subunit MsrP {ECO:0000256|HAMAP-Rule:MF_01206, ECO:0000256|SAAS:SAAS00531094};
DE            EC=1.8.5.- {ECO:0000256|HAMAP-Rule:MF_01206, ECO:0000256|SAAS:SAAS00531097};
GN   Name=msrP {ECO:0000256|HAMAP-Rule:MF_01206};
GN   OrderedLocusNames=Pden_0063 {ECO:0000313|EMBL:ABL68180.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL68180.1, ECO:0000313|Proteomes:UP000000361};
RN   [1] {ECO:0000313|Proteomes:UP000000361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of the MsrPQ system that repairs oxidized
CC       periplasmic proteins containing methionine sulfoxide residues
CC       (Met-O), using respiratory chain electrons. Thus protects these
CC       proteins from oxidative-stress damage caused by reactive species
CC       of oxygen and chlorine generated by the host defense mechanisms.
CC       MsrPQ is essential for the maintenance of envelope integrity under
CC       bleach stress, rescuing a wide series of structurally unrelated
CC       periplasmic proteins from methionine oxidation. The catalytic
CC       subunit MsrP is non-stereospecific, being able to reduce both (R-)
CC       and (S-) diastereoisomers of methionine sulfoxide.
CC       {ECO:0000256|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,
CC         Rhea:RHEA-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:0000256|HAMAP-Rule:MF_01206,
CC         ECO:0000256|SAAS:SAAS01115928};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + H2O + L-methionyl-[protein] = a quinol + L-
CC         methionyl-(S)-S-oxide-[protein]; Xref=Rhea:RHEA:51292,
CC         Rhea:RHEA-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:0000256|HAMAP-Rule:MF_01206};
CC   -!- COFACTOR:
CC       Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01206};
CC       Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC       {ECO:0000256|HAMAP-Rule:MF_01206};
CC   -!- SUBUNIT: Heterodimer of a catalytic subunit (MsrP) and a heme-
CC       binding subunit (MsrQ). {ECO:0000256|HAMAP-Rule:MF_01206,
CC       ECO:0000256|SAAS:SAAS00531099}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|HAMAP-Rule:MF_01206}.
CC       Note=Is attached to the inner membrane when interacting with the
CC       MsrQ subunit. {ECO:0000256|HAMAP-Rule:MF_01206}.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of
CC       the signal peptide cleavage has not been experimentally proven.
CC       {ECO:0000256|HAMAP-Rule:MF_01206}.
CC   -!- SIMILARITY: Belongs to the MsrP family. {ECO:0000256|HAMAP-
CC       Rule:MF_01206, ECO:0000256|SAAS:SAAS00541482}.
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DR   EMBL; CP000489; ABL68180.1; -; Genomic_DNA.
DR   RefSeq; WP_011746413.1; NC_008686.1.
DR   STRING; 318586.Pden_0063; -.
DR   PRIDE; A1AY36; -.
DR   EnsemblBacteria; ABL68180; ABL68180; Pden_0063.
DR   KEGG; pde:Pden_0063; -.
DR   eggNOG; ENOG4105CCD; Bacteria.
DR   eggNOG; COG2041; LUCA.
DR   HOGENOM; HOG000255004; -.
DR   KO; K07147; -.
DR   OMA; DWPYVEG; -.
DR   BioCyc; PDEN318586:G1GW1-64-MONOMER; -.
DR   Proteomes; UP000000361; Chromosome 1.
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:0042128; P:nitrate assimilation; IEA:InterPro.
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;
DR   PRODOM; A1AY36.
DR   SWISS-2DPAGE; A1AY36.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000361};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01206,
KW   ECO:0000256|SAAS:SAAS00016467};
KW   Molybdenum {ECO:0000256|HAMAP-Rule:MF_01206,
KW   ECO:0000256|SAAS:SAAS00016461};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01206,
KW   ECO:0000256|SAAS:SAAS00016458};
KW   Periplasm {ECO:0000256|HAMAP-Rule:MF_01206};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000361};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_01206}.
FT   DOMAIN       79    233       Oxidored_molyb. {ECO:0000259|Pfam:
FT                                PF00174}.
FT   REGION       61     62       Molybdopterin binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01206}.
FT   REGION      215    217       Molybdopterin binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01206}.
FT   METAL       116    116       Molybdenum. {ECO:0000256|HAMAP-Rule:
FT                                MF_01206}.
FT   BINDING      58     58       Molybdopterin. {ECO:0000256|HAMAP-Rule:
FT                                MF_01206}.
FT   BINDING     151    151       Molybdopterin. {ECO:0000256|HAMAP-Rule:
FT                                MF_01206}.
FT   BINDING     199    199       Molybdopterin. {ECO:0000256|HAMAP-Rule:
FT                                MF_01206}.
FT   BINDING     204    204       Molybdopterin. {ECO:0000256|HAMAP-Rule:
FT                                MF_01206}.
SQ   SEQUENCE   298 AA;  32883 MW;  F96529392AD977A3 CRC64;
     MTMKWSEVTP EADYLNRRAF LAAGIAALAT PALGLGGAPS AFSTDEAVNS LEDITHYNNF
     YEFGTGKSDP AQYSGSLKTS PWSVTIDGMV DRPGNYGVED LAPESALEER IYRLRCVEAW
     SMVIPWLGVP LAGALDKAGV QPGAKFVAFR TLHDPEQMPG QRSRILDWPY REGLRLDEAM
     HPLTILATGL YGRVLPNQNG APIRLVVPWK YGFKSIKSVV GITLTDTQPQ CSWQMMQPGE
     YGFYANVNPQ VDHPRWSQAT ERRIGKGLFG GRQDTLMFNG YGDQVAGLYA GMDLAKHY
//

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