ID MSRAB_NEIMB Reviewed; 522 AA. AC Q9K1N8; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 26-FEB-2020, entry version 127. DE RecName: Full=Peptide methionine sulfoxide reductase MsrA/MsrB; DE Includes: DE RecName: Full=Thioredoxin; DE Includes: DE RecName: Full=Peptide methionine sulfoxide reductase MsrA; DE Short=Protein-methionine-S-oxide reductase; DE EC=1.8.4.11; DE AltName: Full=Peptide-methionine (S)-S-oxide reductase; DE Short=Peptide Met(O) reductase; DE Includes: DE RecName: Full=Peptide methionine sulfoxide reductase MsrB; DE EC=1.8.4.12; DE AltName: Full=Peptide-methionine (R)-S-oxide reductase; GN Name=msrAB; Synonyms=pilB; OrderedLocusNames=NMB0044; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae; OC Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C., RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H., RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M., RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D., RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V., RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M., RA Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Has an important function as a repair enzyme for proteins CC that have been inactivated by oxidation. Catalyzes the reversible CC oxidation-reduction of methionine sulfoxide in proteins to methionine CC (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] = CC [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein]; CC Xref=Rhea:RHEA:14217, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, CC Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12315, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:44120, CC ChEBI:CHEBI:50058; EC=1.8.4.11; CC -!- CATALYTIC ACTIVITY: CC Reaction=[thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]- CC dithiol + L-methionine (S)-S-oxide; Xref=Rhea:RHEA:19993, Rhea:RHEA- CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57844, CC ChEBI:CHEBI:58772; EC=1.8.4.11; CC -!- CATALYTIC ACTIVITY: CC Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] = CC [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein]; CC Xref=Rhea:RHEA:24164, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, CC Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12314, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:45764, CC ChEBI:CHEBI:50058; EC=1.8.4.12; CC -!- DOMAIN: Possesses 2 methionine sulfoxide reductase domains (A/MsrA and CC B/MsrB) and 1 N-terminal thioredoxin domain. The domain B exhibits a CC thioredoxin dependent methionine sulfoxide reductase activity; the Cys- CC 495 is probably involved in the reduction of MetSO and in formation of CC the sulfenic acid derivative. The regeneration of Cys-495 is probably CC done via formation of a disulfide bond with Cys-440 followed by its CC reduction by thioredoxin. CC -!- SIMILARITY: In the N-terminal section; belongs to the thioredoxin CC family. {ECO:0000305}. CC -!- SIMILARITY: In the central section; belongs to the MsrA Met sulfoxide CC reductase family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the MsrB Met CC sulfoxide reductase family. {ECO:0000305}. 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; AE002098; AAF40515.1; -; Genomic_DNA. DR PIR; G81243; G81243. DR RefSeq; NP_273110.1; NC_003112.2. DR RefSeq; WP_010980745.1; NC_003112.2. DR SMR; Q9K1N8; -. DR PaxDb; Q9K1N8; -. DR EnsemblBacteria; AAF40515; AAF40515; NMB0044. DR GeneID; 902147; -. DR KEGG; nme:NMB0044; -. DR PATRIC; fig|122586.8.peg.59; -. DR eggNOG; ENOG4105E0X; Bacteria. DR eggNOG; COG0225; LUCA. DR eggNOG; COG0229; LUCA. DR eggNOG; COG0526; LUCA. DR HOGENOM; CLU_031040_11_0_4; -. DR KO; K12267; -. DR OMA; AQYDITQ; -. DR BioCyc; NMEN122586:G1G1B-43-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0036456; F:L-methionine-(S)-S-oxide reductase activity; IBA:GO_Central. 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; IBA:GO_Central. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR GO; GO:0006464; P:cellular protein modification process; IEA:UniProtKB-UniRule. DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central. DR GO; GO:0030091; P:protein repair; IEA:InterPro. DR Gene3D; 3.30.1060.10; -; 1. DR Gene3D; 3.40.30.10; -; 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 InterPro; IPR013740; Redoxin. DR InterPro; IPR036249; Thioredoxin-like_sf. DR InterPro; IPR013766; Thioredoxin_domain. DR PANTHER; PTHR10173; PTHR10173; 1. DR Pfam; PF01625; PMSR; 1. DR Pfam; PF08534; Redoxin; 1. DR Pfam; PF01641; SelR; 1. DR SUPFAM; SSF51316; SSF51316; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR SUPFAM; SSF55068; SSF55068; 1. DR TIGRFAMs; TIGR00401; msrA; 1. DR TIGRFAMs; TIGR00357; TIGR00357; 1. DR PROSITE; PS51790; MSRB; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 3: Inferred from homology; KW Disulfide bond; Electron transport; Multifunctional enzyme; Oxidoreductase; KW Redox-active center; Reference proteome; Transport. FT CHAIN 1..522 FT /note="Peptide methionine sulfoxide reductase MsrA/MsrB" FT /id="PRO_0000138510" FT DOMAIN 17..174 FT /note="Thioredoxin" FT DOMAIN 383..506 FT /note="MsrB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126" FT REGION 199..354 FT /note="Peptide methionine sulfoxide reductase A" FT ACT_SITE 207 FT /evidence="ECO:0000250" FT ACT_SITE 495 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126" FT DISULFID 68..71 FT /note="Redox-active" FT /evidence="ECO:0000250" FT DISULFID 440..495 FT /evidence="ECO:0000250" SQ SEQUENCE 522 AA; 58015 MW; 535A823EDB76BFD1 CRC64; MKHRTFFSLC AKFGCLLALG ACSPKIVDAG AATVPHTLST LKTADNRPAS VYLKKDKPTL IKFWASWCPL CLSELGQTEK WAQDAKFSSA NLITVASPGF LHEKKDGDFQ KWYAGLNYPK LPVVTDNGGT IAQSLNISVY PSWALIGKDS DVQRIVKGSI NEAQALALIR DPNADLGSLK HSFYKPDTQK KDSKIMNTRT IYLAGGCFWG LEAYFQRIDG VVDAVSGYAN GNTKNPSYED VSYRHTGHAE TVKVTYDADK LSLDDILQYF FRVVDPTSLN KQGNDTGTQY RSGVYYTDPA EKAVIAAALK REQQKYQLPL VVENEPLKNF YDAEEYHQDY LIKNPNGYCH IDIRKADEPL PGKTKTAPQG KGFDAATYKK PSDAELKRTL TEEQYQVTQN SATEYAFSHE YDHLFKPGIY VDVVSGEPLF SSADKYDSGC GWPSFTRPID AKSVTEHDDF SYNMRRTEVR SHAADSHLGH VFPDGPRDKG GLRYCINGAS LKFIPLEQMD AAGYGALKGK VK //