MSRAB_NEIGO
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 03-AUG-2022, entry version 140.
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; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC 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=[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 -!- 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};
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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_RJYO01000004.1.
DR PDB; 1L1D; X-ray; 1.85 A; A/B=375-522.
DR PDB; 2H30; X-ray; 1.60 A; A=23-182.
DR PDBsum; 1L1D; -.
DR PDBsum; 2H30; -.
DR AlphaFoldDB; P14930; -.
DR BMRB; P14930; -.
DR SMR; P14930; -.
DR PRIDE; 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:0033744; F:L-methionine:thioredoxin-disulfide S-oxidoreductase 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: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; IPR002569; Met_Sox_Rdtase_MsrA_dom.
DR InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
DR InterPro; IPR028427; Met_Sox_Rdtase_MsrB.
DR InterPro; IPR002579; Met_Sox_Rdtase_MsrB_dom.
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 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 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
