ID MSRAB_NEIGO Reviewed; 522 AA. AC P14930; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 02-MAY-2002, sequence version 2. DT 10-JUN-2026, entry version 153. 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; OS Neisseria gonorrhoeae. OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=485; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=MS11A; RX PubMed=2854063; DOI=10.1002/j.1460-2075.1988.tb03335.x; RA Taha M.K., So M., Seifert H.S., Billyard E., Marchal C.; RT "Pilin expression in Neisseria gonorrhoeae is under both positive and RT negative transcriptional control."; RL EMBO J. 7:4367-4378(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Lowther W.T., Brot N., Weissbach H., Honek J.F., Matthews B.W.; RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP IDENTIFICATION OF PEPTIDE METHIONINE SULFOXIDE REDUCTASE ACTIVITY, AND RP DISRUPTION PHENOTYPE. RX PubMed=8755589; DOI=10.1073/pnas.93.15.7985; RA Wizemann T.M., Moskovitz J., Pearce B.J., Cundell D., Arvidson C.G., So M., RA Weissbach H., Brot N., Masure H.R.; RT "Peptide methionine sulfoxide reductase contributes to the maintenance of RT adhesins in three major pathogens."; RL Proc. Natl. Acad. Sci. U.S.A. 93:7985-7990(1996). CC -!- FUNCTION: Has an important function as a repair enzyme for proteins CC that have been inactivated by oxidation (By similarity). Catalyzes the CC reversible oxidation-reduction of methionine sulfoxide in proteins to CC methionine. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-methionyl-[protein] + [thioredoxin]-disulfide + H2O = L- CC methionyl-(S)-S-oxide-[protein] + [thioredoxin]-dithiol; 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 + L-methionine + H2O = L-methionine CC (S)-S-oxide + [thioredoxin]-dithiol; 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=L-methionyl-[protein] + [thioredoxin]-disulfide + H2O = L- CC methionyl-(R)-S-oxide-[protein] + [thioredoxin]-dithiol; 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 -!- DISRUPTION PHENOTYPE: Hyperpiliated and hyperadherent. CC {ECO:0000269|PubMed:8755589}. 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 -!- CAUTION: Was originally thought to play a role along with PilA in the CC transcription regulation of PilE. {ECO:0000305|PubMed:2854063}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA32146.1; Type=Frameshift; Evidence={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; X13966; CAA32146.1; ALT_FRAME; Genomic_DNA. DR EMBL; AF482946; AAL89752.1; -; Genomic_DNA. DR PIR; S02018; S02018. DR RefSeq; WP_003696288.1; NZ_CAXBSX010000005.1. DR PDB; 1L1D; X-ray; 1.85 A; A/B=375-522. DR PDB; 2H30; X-ray; 1.60 A; A=23-182. DR AlphaFoldDB; P14930; -. DR BMRB; P14930; -. DR SMR; P14930; -. DR PATRIC; fig|485.49.peg.1916; -. DR BRENDA; 1.8.4.11; 3590. DR BRENDA; 1.8.4.12; 3590. DR EvolutionaryTrace; P14930; -. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. DR GO; GO:0033744; F:L-methionine (S)-S-oxide reductase activity; IEA:RHEA. 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:0034599; P:cellular response to oxidative stress; IEA:TreeGrafter. DR CDD; cd02966; TlpA_like_family; 1. DR FunFam; 3.40.30.10:FF:000321; Multifunctional fusion protein; 1. DR FunFam; 3.30.1060.10:FF:000007; Peptide methionine sulfoxide reductase msrA/msrB; 1. DR FunFam; 2.170.150.20:FF:000003; Peptide methionine sulfoxide reductase MsrB; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. DR Gene3D; 2.170.150.20; Peptide methionine sulfoxide reductase; 1. DR Gene3D; 3.30.1060.10; Peptide methionine sulphoxide reductase MsrA; 1. DR HAMAP; MF_01401; MsrA; 1. DR HAMAP; MF_01400; MsrB; 1. DR InterPro; IPR002569; Met_Sox_Rdtase_MsrA_dom. DR InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf. DR InterPro; IPR002579; Met_Sox_Rdtase_MsrB_dom. DR InterPro; IPR050162; MsrA_MetSO_reductase. DR InterPro; IPR011057; Mss4-like_sf. DR InterPro; IPR013740; Redoxin. DR InterPro; IPR036249; Thioredoxin-like_sf. DR InterPro; IPR013766; Thioredoxin_domain. DR NCBIfam; TIGR00401; msrA; 1. DR NCBIfam; TIGR00357; peptide-methionine (R)-S-oxide reductase MsrB; 1. DR NCBIfam; NF010625; PRK14018.1; 1. DR PANTHER; PTHR42799; MITOCHONDRIAL PEPTIDE METHIONINE SULFOXIDE REDUCTASE; 1. DR PANTHER; PTHR42799:SF2; MITOCHONDRIAL PEPTIDE METHIONINE SULFOXIDE REDUCTASE; 1. DR Pfam; PF01625; PMSR; 1. DR Pfam; PF08534; Redoxin; 1. DR Pfam; PF01641; SelR; 1. DR SUPFAM; SSF51316; Mss4-like; 1. DR SUPFAM; SSF55068; Peptide methionine sulfoxide reductase; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 1. DR PROSITE; PS51790; MSRB; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. DR PDBsum; 1L1D; -. DR PDBsum; 2H30; -. PE 1: Evidence at protein level; KW 3D-structure; Disulfide bond; Electron transport; Multifunctional enzyme; KW Oxidoreductase; Redox-active center; Transport. FT CHAIN 1..522 FT /note="Peptide methionine sulfoxide reductase MsrA/MsrB" FT /id="PRO_0000138508" 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 /note="Redox-active" FT /evidence="ECO:0000250" FT HELIX 34..38 FT /evidence="ECO:0007829|PDB:2H30" FT STRAND 46..48 FT /evidence="ECO:0007829|PDB:2H30" FT HELIX 49..52 FT /evidence="ECO:0007829|PDB:2H30" FT STRAND 59..63 FT /evidence="ECO:0007829|PDB:2H30" FT HELIX 69..82 FT /evidence="ECO:0007829|PDB:2H30" FT HELIX 85..87 FT /evidence="ECO:0007829|PDB:2H30" FT STRAND 90..96 FT /evidence="ECO:0007829|PDB:2H30" FT HELIX 103..105 FT /evidence="ECO:0007829|PDB:2H30" FT HELIX 108..113 FT /evidence="ECO:0007829|PDB:2H30" FT STRAND 123..125 FT /evidence="ECO:0007829|PDB:2H30" FT HELIX 130..134 FT /evidence="ECO:0007829|PDB:2H30" FT STRAND 139..146 FT /evidence="ECO:0007829|PDB:2H30" FT STRAND 152..158 FT /evidence="ECO:0007829|PDB:2H30" FT HELIX 162..170 FT /evidence="ECO:0007829|PDB:2H30" FT HELIX 177..179 FT /evidence="ECO:0007829|PDB:2H30" FT HELIX 383..386 FT /evidence="ECO:0007829|PDB:1L1D" FT TURN 387..389 FT /evidence="ECO:0007829|PDB:1L1D" FT HELIX 392..400 FT /evidence="ECO:0007829|PDB:1L1D" FT HELIX 410..413 FT /evidence="ECO:0007829|PDB:1L1D" FT STRAND 417..422 FT /evidence="ECO:0007829|PDB:1L1D" FT TURN 423..425 FT /evidence="ECO:0007829|PDB:1L1D" FT STRAND 428..431 FT /evidence="ECO:0007829|PDB:1L1D" FT HELIX 432..434 FT /evidence="ECO:0007829|PDB:1L1D" FT STRAND 439..442 FT /evidence="ECO:0007829|PDB:1L1D" FT STRAND 444..447 FT /evidence="ECO:0007829|PDB:1L1D" FT STRAND 453..459 FT /evidence="ECO:0007829|PDB:1L1D" FT STRAND 466..471 FT /evidence="ECO:0007829|PDB:1L1D" FT TURN 472..474 FT /evidence="ECO:0007829|PDB:1L1D" FT STRAND 477..483 FT /evidence="ECO:0007829|PDB:1L1D" FT HELIX 487..489 FT /evidence="ECO:0007829|PDB:1L1D" FT STRAND 493..496 FT /evidence="ECO:0007829|PDB:1L1D" FT HELIX 498..500 FT /evidence="ECO:0007829|PDB:1L1D" FT STRAND 501..505 FT /evidence="ECO:0007829|PDB:1L1D" FT HELIX 506..512 FT /evidence="ECO:0007829|PDB:1L1D" FT HELIX 515..520 FT /evidence="ECO:0007829|PDB:1L1D" SQ SEQUENCE 522 AA; 57959 MW; DDC8EC308B57B30C CRC64; MKHRTFFSLC AKFGCLLALG ACSPKIVDAG TATVPHTLST LKTADNRPAS VYLKKDKPTL IKFWASWCPL CLSELGQAEK WAQDAKFSSA NLITVASPGF LHEKKDGEFQ KWYAGLNYPK LPVVTDNGGT IAQNLNISVY PSWALIGKDG DVQRIVKGSI NEAQALALIR NPNADLGSLK HSFYKPDTQK KDSAIMNTRT IYLAGGCFWG LEAYFQRIDG VVDAVSGYAN GNTENPSYED VSYRHTGHAE TVKVTYDADK LSLDDILQYY FRVVDPTSLN KQGNDTGTQY RSGVYYTDPA EKAVIAAALK REQQKYQLPL VVENEPLKNF YDAEEYHQDY LIKNPNGYCH IDIRKADEPL PGKTKAAPQG KGFDAATYKK PSDAELKRTL TEEQYQVTQN SATEYAFSHE YDHLFKPGIY VDVVSGEPLF SSADKYDSGC GWPSFTRPID AKSVTEHDDF SFNMRRTEVR SRAADSHLGH VFPDGPRDKG GLRYCINGAS LKFIPLEQMD AAGYGALKGE VK //