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 12-APR-2017, entry version 113. 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; OC Neisseriaceae; 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., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA 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 CC proteins that have been inactivated by oxidation. Catalyzes the CC reversible oxidation-reduction of methionine sulfoxide in proteins CC to methionine (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide + CC H(2)O = peptide-L-methionine (S)-S-oxide + thioredoxin. CC -!- CATALYTIC ACTIVITY: L-methionine + thioredoxin disulfide + H(2)O = CC L-methionine (S)-S-oxide + thioredoxin. CC -!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide + CC H(2)O = peptide-L-methionine (R)-S-oxide + thioredoxin. CC -!- DOMAIN: Possesses 2 methionine sulfoxide reductase domains (A/MsrA CC and B/MsrB) and 1 N-terminal thioredoxin domain. The domain B CC exhibits a thioredoxin dependent methionine sulfoxide reductase CC activity; the Cys-495 is probably involved in the reduction of CC MetSO and in formation of the sulfenic acid derivative. The CC regeneration of Cys-495 is probably done via formation of a CC disulfide bond with Cys-440 followed by its reduction by CC 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 CC sulfoxide 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 ProteinModelPortal; Q9K1N8; -. DR SMR; Q9K1N8; -. DR STRING; 122586.NMB0044; -. DR PaxDb; Q9K1N8; -. DR EnsemblBacteria; AAF40515; AAF40515; NMB0044. DR GeneID; 902147; -. DR KEGG; nme:NMB0044; -. DR PATRIC; 20355045; VBINeiMen85645_0059. DR eggNOG; ENOG4105E0X; Bacteria. DR eggNOG; COG0225; LUCA. DR eggNOG; COG0229; LUCA. DR eggNOG; COG0526; LUCA. DR HOGENOM; HOG000243423; -. DR KO; K12267; -. DR OMA; WIDEKNG; -. DR OrthoDB; POG091H064P; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IEA:UniProtKB-EC. DR GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:UniProtKB-EC. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. 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 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; IPR002579; Met_Sox_Rdtase_MsrB. DR InterPro; IPR011057; Mss4-like. DR InterPro; IPR013740; Redoxin. DR InterPro; IPR012336; Thioredoxin-like_fold. 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 Complete proteome; Disulfide bond; Electron transport; KW Multifunctional enzyme; Oxidoreductase; Redox-active center; KW Reference proteome; Transport. FT CHAIN 1 522 Peptide methionine sulfoxide reductase FT MsrA/MsrB. FT /FTId=PRO_0000138510. FT DOMAIN 17 174 Thioredoxin. FT DOMAIN 383 506 MsrB. {ECO:0000255|PROSITE- FT ProRule:PRU01126}. FT REGION 199 354 Peptide methionine sulfoxide reductase A. FT ACT_SITE 207 207 {ECO:0000250}. FT ACT_SITE 495 495 Nucleophile. {ECO:0000255|PROSITE- FT ProRule:PRU01126}. FT DISULFID 68 71 Redox-active. {ECO:0000250}. FT DISULFID 440 495 {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 //