(data stored in SCRATCH zone)

SWISSPROT: A1AY37_PARDP

ID   A1AY37_PARDP            Unreviewed;       208 AA.
AC   A1AY37;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 71.
DE   RecName: Full=Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ {ECO:0000256|HAMAP-Rule:MF_01207, ECO:0000256|SAAS:SAAS01034031};
DE   AltName: Full=Flavocytochrome MsrQ {ECO:0000256|HAMAP-Rule:MF_01207};
GN   Name=msrQ {ECO:0000256|HAMAP-Rule:MF_01207};
GN   OrderedLocusNames=Pden_0064 {ECO:0000313|EMBL:ABL68181.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL68181.1, 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. MsrQ provides
CC       electrons for reduction to the reductase catalytic subunit MsrP,
CC       using the quinone pool of the respiratory chain.
CC       {ECO:0000256|HAMAP-Rule:MF_01207}.
CC   -!- SUBUNIT: Heterodimer of a catalytic subunit (MsrP) and a heme-
CC       binding subunit (MsrQ). {ECO:0000256|HAMAP-Rule:MF_01207,
CC       ECO:0000256|SAAS:SAAS01034021}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01207, ECO:0000256|SAAS:SAAS01034020}; Multi-pass membrane
CC       protein {ECO:0000256|HAMAP-Rule:MF_01207,
CC       ECO:0000256|SAAS:SAAS01034020}.
CC   -!- SIMILARITY: Belongs to the MsrQ family. {ECO:0000256|HAMAP-
CC       Rule:MF_01207, ECO:0000256|SAAS:SAAS01034023}.
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DR   EMBL; CP000489; ABL68181.1; -; Genomic_DNA.
DR   RefSeq; WP_011746414.1; NC_008686.1.
DR   STRING; 318586.Pden_0064; -.
DR   PRIDE; A1AY37; -.
DR   EnsemblBacteria; ABL68181; ABL68181; Pden_0064.
DR   KEGG; pde:Pden_0064; -.
DR   eggNOG; ENOG4105DQ2; Bacteria.
DR   eggNOG; COG2717; LUCA.
DR   HOGENOM; HOG000255015; -.
DR   KO; K17247; -.
DR   OMA; LHFFWMR; -.
DR   BioCyc; PDEN318586:G1GW1-65-MONOMER; -.
DR   Proteomes; UP000000361; Chromosome 1.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030091; P:protein repair; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01207; MsrQ; 1.
DR   InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR   InterPro; IPR022837; MsrQ.
DR   PANTHER; PTHR36964; PTHR36964; 1.
DR   Pfam; PF01794; Ferric_reduct; 1.
PE   3: Inferred from homology;
DR   PRODOM; A1AY37.
DR   SWISS-2DPAGE; A1AY37.
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01207,
KW   ECO:0000256|SAAS:SAAS01034016};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01207,
KW   ECO:0000256|SAAS:SAAS01034028};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000361};
KW   Electron transport {ECO:0000256|HAMAP-Rule:MF_01207,
KW   ECO:0000256|SAAS:SAAS01034025};
KW   Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01207,
KW   ECO:0000256|SAAS:SAAS01034030};
KW   FMN {ECO:0000256|HAMAP-Rule:MF_01207, ECO:0000256|SAAS:SAAS01034032};
KW   Heme {ECO:0000256|HAMAP-Rule:MF_01207, ECO:0000256|SAAS:SAAS01034029};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01207, ECO:0000256|SAAS:SAAS01034015};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01207,
KW   ECO:0000256|SAAS:SAAS01034034};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01207,
KW   ECO:0000256|SAAS:SAAS01034026};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000361};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01207,
KW   ECO:0000256|SAAS:SAAS01034027, ECO:0000313|EMBL:ABL68181.1};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01207,
KW   ECO:0000256|SAAS:SAAS01034018};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01207,
KW   ECO:0000256|SAAS:SAAS01034033}.
FT   TRANSMEM     12     33       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01207}.
FT   TRANSMEM     53     69       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01207}.
FT   TRANSMEM     81    105       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01207}.
FT   TRANSMEM    117    138       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01207}.
FT   TRANSMEM    150    168       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01207}.
FT   TRANSMEM    174    192       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01207}.
FT   DOMAIN       50    161       Ferric oxidoreductase. {ECO:0000259|Pfam:
FT                                PF01794}.
SQ   SEQUENCE   208 AA;  24011 MW;  010178039DAEB1FC CRC64;
     MVQHLNRWLR HVPVWAVWLL GLVPLGLLVW DALQGHLGVD PVRDIEHRLG RTAIYFLLAT
     LTVTPLLRLT RLNLMRFRQA LGLICFAYVA CHLVAWVVFD MAFLWAQMLK DVVKRPYLVF
     GMLAFAMLLA LALTSNRFSI RRMGAGWRKL HRLVYPAAIL AGVHWLWALK VWESWPLTIL
     GTILLLLFLR LLRKWGWSGV FGVVRRAG
//

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