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Multifunctional fusion protein [Includes: Peptide methionine sulfoxide reductase MsrB (EC 1.8.4.12) (Peptide-methionine (R)-S-oxide reductase); Peptide methionine sulfoxide reductase MsrA (Protein-methionine-S-oxide reductase) (EC 1.8.4.11) (Peptide-methionine (S)-S-oxide reductase) (Peptide Met(O) reductase)]

 F8DF02_STREP            Unreviewed;       373 AA.
F8DF02;
21-SEP-2011, integrated into UniProtKB/TrEMBL.
21-SEP-2011, sequence version 1.
27-SEP-2017, entry version 44.
RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_01400, ECO:0000256|HAMAP-Rule:MF_01401};
Includes:
RecName: Full=Peptide methionine sulfoxide reductase MsrB {ECO:0000256|HAMAP-Rule:MF_01400};
EC=1.8.4.12 {ECO:0000256|HAMAP-Rule:MF_01400};
AltName: Full=Peptide-methionine (R)-S-oxide reductase {ECO:0000256|HAMAP-Rule:MF_01400};
Includes:
RecName: Full=Peptide methionine sulfoxide reductase MsrA {ECO:0000256|HAMAP-Rule:MF_01401};
Short=Protein-methionine-S-oxide reductase {ECO:0000256|HAMAP-Rule:MF_01401};
EC=1.8.4.11 {ECO:0000256|HAMAP-Rule:MF_01401};
AltName: Full=Peptide-methionine (S)-S-oxide reductase {ECO:0000256|HAMAP-Rule:MF_01401};
Short=Peptide Met(O) reductase {ECO:0000256|HAMAP-Rule:MF_01401};
Name=msrB {ECO:0000256|HAMAP-Rule:MF_01400,
ECO:0000313|EMBL:AEH55075.1};
Synonyms=msrA {ECO:0000256|HAMAP-Rule:MF_01401};
OrderedLocusNames=HMPREF0833_10044 {ECO:0000313|EMBL:AEH55075.1};
Streptococcus parasanguinis (strain ATCC 15912 / DSM 6778 / CIP 104372
/ LMG 14537).
Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
Streptococcus.
NCBI_TaxID=760570 {ECO:0000313|EMBL:AEH55075.1, ECO:0000313|Proteomes:UP000001502};
[1] {ECO:0000313|Proteomes:UP000001502}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 15912 / DSM 6778 / CIP 104372 / LMG 14537
{ECO:0000313|Proteomes:UP000001502};
Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G.,
Hawes A., Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W.,
Liu X., Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J.,
Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D.,
Johnson A., Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A.,
Song B.-B., Dinh H., Thornton R., Coyle M., Francisco L., Jackson L.,
Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R.,
Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D.,
Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R.,
San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S.,
Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K.,
Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
Petrosino J., Highlander S., Gibbs R.;
"Complete sequence of Streptococcus parasanguinis strain ATCC 15912.";
Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Has an important function as a repair enzyme for
proteins that have been inactivated by oxidation. Catalyzes the
reversible oxidation-reduction of methionine sulfoxide in proteins
to methionine. {ECO:0000256|HAMAP-Rule:MF_01401}.
-!- CATALYTIC ACTIVITY: L-methionine + thioredoxin disulfide + H(2)O =
L-methionine (S)-S-oxide + thioredoxin. {ECO:0000256|HAMAP-
Rule:MF_01401}.
-!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide +
H(2)O = peptide-L-methionine (R)-S-oxide + thioredoxin.
{ECO:0000256|HAMAP-Rule:MF_01400}.
-!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide +
H(2)O = peptide-L-methionine (S)-S-oxide + thioredoxin.
{ECO:0000256|HAMAP-Rule:MF_01401, ECO:0000256|SAAS:SAAS00684647}.
-!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
{ECO:0000256|HAMAP-Rule:MF_01401}.
-!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
{ECO:0000256|HAMAP-Rule:MF_01400}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01400}.
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EMBL; CP002843; AEH55075.1; -; Genomic_DNA.
RefSeq; WP_013903203.1; NC_015678.1.
ProteinModelPortal; F8DF02; -.
EnsemblBacteria; AEH55075; AEH55075; HMPREF0833_10044.
GeneID; 10834537; -.
KEGG; scp:HMPREF0833_10044; -.
KO; K12267; -.
Proteomes; UP000001502; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IEA:UniProtKB-UniRule.
GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:UniProtKB-UniRule.
GO; GO:0006464; P:cellular protein modification process; IEA:UniProtKB-UniRule.
GO; GO:0030091; P:protein repair; IEA:InterPro.
GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
Gene3D; 3.30.1060.10; -; 1.
HAMAP; MF_01401; MsrA; 1.
HAMAP; MF_01400; MsrB; 1.
InterPro; IPR028427; Met_Sox_Rdtase.
InterPro; IPR002569; Met_Sox_Rdtase_MsrA.
InterPro; IPR002579; Met_Sox_Rdtase_MsrB.
InterPro; IPR011057; Mss4-like.
PANTHER; PTHR10173; PTHR10173; 1.
Pfam; PF01625; PMSR; 1.
Pfam; PF01641; SelR; 1.
SUPFAM; SSF51316; SSF51316; 1.
SUPFAM; SSF55068; SSF55068; 1.
TIGRFAMs; TIGR00401; msrA; 1.
TIGRFAMs; TIGR00357; TIGR00357; 1.
PROSITE; PS51790; MSRB; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000001502};
Membrane {ECO:0000256|SAM:Phobius};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01401,
ECO:0000256|SAAS:SAAS00684651, ECO:0000313|EMBL:AEH55075.1};
Transmembrane {ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|SAM:Phobius}.
TRANSMEM 6 23 Helical. {ECO:0000256|SAM:Phobius}.
DOMAIN 235 358 MsrB. {ECO:0000259|PROSITE:PS51790}.
ACT_SITE 73 73 {ECO:0000256|HAMAP-Rule:MF_01401}.
ACT_SITE 347 347 Nucleophile. {ECO:0000256|HAMAP-
Rule:MF_01400}.
SEQUENCE 373 AA; 42467 MW; C382A0D407F0E5C9 CRC64;
METKWKVGLI LLIGLLSIGF FFFSKGSNGM DRSETSTEMI KKASMSQTPV AKKETKETVD
PKDQREIYLA GGCFWGVEEY FSRVPGVIDA VSGYANGKGE TTKYELVPQT GHAETVHITY
NVKKVSLKEL LLHYFRIIDP TSKNRQGNDQ GTQYRTGVYY VSQEDLPTIN QVFEEEAKKY
DKPLVVEKEP LTNFIKAEDY HQDYLKKHPN GYCHIDVNQA SYPVIDASRY SKTSDEEIKK
KLSPEEYAVT QKNDTERAFS NRYWDQFDAG IYVDVVTGEP LFSSKDKFDS GCGWPSFSRP
ISPDVAIYKE DKSFNMTRTE VRSRVGNSHL GHVFTDGPKE KGGLRYCINS LSITFIPKAE
MKEKGYGYLL DYV


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