ID A0A0K9HBA3_9BACI Unreviewed; 318 AA. AC A0A0K9HBA3; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 31-JAN-2018, entry version 20. DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_01400, ECO:0000256|HAMAP-Rule:MF_01401}; DE Includes: DE RecName: Full=Peptide methionine sulfoxide reductase MsrB {ECO:0000256|HAMAP-Rule:MF_01400}; DE EC=1.8.4.12 {ECO:0000256|HAMAP-Rule:MF_01400}; DE AltName: Full=Peptide-methionine (R)-S-oxide reductase {ECO:0000256|HAMAP-Rule:MF_01400}; DE Includes: DE RecName: Full=Peptide methionine sulfoxide reductase MsrA {ECO:0000256|HAMAP-Rule:MF_01401}; DE Short=Protein-methionine-S-oxide reductase {ECO:0000256|HAMAP-Rule:MF_01401}; DE EC=1.8.4.11 {ECO:0000256|HAMAP-Rule:MF_01401}; DE AltName: Full=Peptide-methionine (S)-S-oxide reductase {ECO:0000256|HAMAP-Rule:MF_01401}; DE Short=Peptide Met(O) reductase {ECO:0000256|HAMAP-Rule:MF_01401}; GN Name=msrB {ECO:0000256|HAMAP-Rule:MF_01400}; GN Synonyms=msrA {ECO:0000256|HAMAP-Rule:MF_01401}; GN ORFNames=AC623_19320 {ECO:0000313|EMBL:KMY55822.1}; OS Bacillus sp. FJAT-27231. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1679168 {ECO:0000313|EMBL:KMY55822.1, ECO:0000313|Proteomes:UP000037077}; RN [1] {ECO:0000313|Proteomes:UP000037077} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FJAT-27231 {ECO:0000313|Proteomes:UP000037077}; RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Che J., Ge C., RA Shi H., Pan Z., Liu X.; RT "Genome sequencing project for genomic taxonomy and phylogenomics of RT Bacillus-like bacteria."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Has an important function as a repair enzyme for CC proteins that have been inactivated by oxidation. Catalyzes the CC reversible oxidation-reduction of methionine sulfoxide in proteins CC to methionine. {ECO:0000256|HAMAP-Rule:MF_01401}. CC -!- CATALYTIC ACTIVITY: L-methionine + thioredoxin disulfide + H(2)O = CC L-methionine (S)-S-oxide + thioredoxin. {ECO:0000256|HAMAP- CC Rule:MF_01401, ECO:0000256|SAAS:SAAS00970052}. CC -!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide + CC H(2)O = peptide-L-methionine (R)-S-oxide + thioredoxin. CC {ECO:0000256|HAMAP-Rule:MF_01400}. CC -!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide + CC H(2)O = peptide-L-methionine (S)-S-oxide + thioredoxin. CC {ECO:0000256|HAMAP-Rule:MF_01401, ECO:0000256|SAAS:SAAS00684647}. CC -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family. CC {ECO:0000256|HAMAP-Rule:MF_01401}. CC -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family. CC {ECO:0000256|HAMAP-Rule:MF_01400}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01400}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KMY55822.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; LFZU01000001; KMY55822.1; -; Genomic_DNA. DR RefSeq; WP_049665720.1; NZ_LFZU01000001.1. DR EnsemblBacteria; KMY55822; KMY55822; AC623_19320. DR PATRIC; fig|1679168.3.peg.4142; -. DR Proteomes; UP000037077; Unassembled WGS sequence. DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006464; P:cellular protein modification process; IEA:UniProtKB-UniRule. DR GO; GO:0030091; P:protein repair; IEA:InterPro. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR Gene3D; 3.30.1060.10; -; 1. DR HAMAP; MF_01401; MsrA; 1. DR HAMAP; MF_01400; MsrB; 1. DR InterPro; IPR028427; Met_Sox_Rdtase. DR InterPro; IPR002569; Met_Sox_Rdtase_MsrA. DR InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf. DR InterPro; IPR002579; Met_Sox_Rdtase_MsrB. DR InterPro; IPR011057; Mss4-like_sf. DR PANTHER; PTHR10173; PTHR10173; 1. DR Pfam; PF01625; PMSR; 1. DR Pfam; PF01641; SelR; 1. DR SUPFAM; SSF51316; SSF51316; 1. DR SUPFAM; SSF55068; SSF55068; 1. DR TIGRFAMs; TIGR00401; msrA; 1. DR TIGRFAMs; TIGR00357; TIGR00357; 1. DR PROSITE; PS51790; MSRB; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000037077}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01400, KW ECO:0000256|SAAS:SAAS00684651}; KW Reference proteome {ECO:0000313|Proteomes:UP000037077}. FT DOMAIN 180 302 MsrB. {ECO:0000259|PROSITE:PS51790}. FT ACT_SITE 14 14 {ECO:0000256|HAMAP-Rule:MF_01401}. FT ACT_SITE 291 291 Nucleophile. {ECO:0000256|HAMAP-Rule: FT MF_01400}. SQ SEQUENCE 318 AA; 36667 MW; C2B060499D7CDF29 CRC64; MAEQWKLATF AGGCFWCMVS PFDEQPGIKE VVSGYTGGHT ENPTYEEVCS DTTGHYEAVQ IKFDPAVFPY KKLVELFWQQ IDPTDAGGQF NDRGLSYKTA IFYHDEEQKE LAEASKTALE ASGRFQKPVV TAILPAGPFY RAEEKHQHYY KKNPFHYNLY REGSGRAKFI RENWKNRKTD EQLRQELTPL QYEVTKHNAT EPPFRNEYWN HIEEGIYVDI ISGEPLFSST DKYDAGCGWP SFTKPLRRIE LEEKLDTSHG MRRIEVRAKT SDSHLGHVFD DGPGPDRARY CINSAALRFV PKDKLDEEGY GEFKSLFE //