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Peptide methionine sulfoxide reductase MsrA/MsrB [Includes: Thioredoxin; Peptide methionine sulfoxide reductase MsrA (Protein-methionine-S-oxide reductase) (EC 1.8.4.11) (Peptide-methionine (S)-S-oxide reductase) (Peptide Met(O) reductase); Peptide methionine sulfoxide reductase MsrB (EC 1.8.4.12) (Peptide-methionine (R)-S-oxide reductase)]

 MSRAB_NEIGO             Reviewed;         522 AA.
P14930;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
02-MAY-2002, sequence version 2.
22-NOV-2017, entry version 124.
RecName: Full=Peptide methionine sulfoxide reductase MsrA/MsrB;
Includes:
RecName: Full=Thioredoxin;
Includes:
RecName: Full=Peptide methionine sulfoxide reductase MsrA;
Short=Protein-methionine-S-oxide reductase;
EC=1.8.4.11;
AltName: Full=Peptide-methionine (S)-S-oxide reductase;
Short=Peptide Met(O) reductase;
Includes:
RecName: Full=Peptide methionine sulfoxide reductase MsrB;
EC=1.8.4.12;
AltName: Full=Peptide-methionine (R)-S-oxide reductase;
Name=msrAB; Synonyms=pilB;
Neisseria gonorrhoeae.
Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
Neisseriaceae; Neisseria.
NCBI_TaxID=485;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=MS11A;
PubMed=2854063;
Taha M.K., So M., Seifert H.S., Billyard E., Marchal C.;
"Pilin expression in Neisseria gonorrhoeae is under both positive and
negative transcriptional control.";
EMBO J. 7:4367-4378(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Lowther W.T., Brot N., Weissbach H., Honek J.F., Matthews B.W.;
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
[3]
IDENTIFICATION OF PEPTIDE METHIONINE SULFOXIDE REDUCTASE ACTIVITY, AND
DISRUPTION PHENOTYPE.
PubMed=8755589; DOI=10.1073/pnas.93.15.7985;
Wizemann T.M., Moskovitz J., Pearce B.J., Cundell D., Arvidson C.G.,
So M., Weissbach H., Brot N., Masure H.R.;
"Peptide methionine sulfoxide reductase contributes to the maintenance
of adhesins in three major pathogens.";
Proc. Natl. Acad. Sci. U.S.A. 93:7985-7990(1996).
-!- FUNCTION: Has an important function as a repair enzyme for
proteins that have been inactivated by oxidation (By similarity).
Catalyzes the reversible oxidation-reduction of methionine
sulfoxide in proteins to methionine. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide +
H(2)O = peptide-L-methionine (S)-S-oxide + thioredoxin.
-!- CATALYTIC ACTIVITY: L-methionine + thioredoxin disulfide + H(2)O =
L-methionine (S)-S-oxide + thioredoxin.
-!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide +
H(2)O = peptide-L-methionine (R)-S-oxide + thioredoxin.
-!- DOMAIN: Possesses 2 methionine sulfoxide reductase domains (A/MsrA
and B/MsrB) and 1 N-terminal thioredoxin domain. The domain B
exhibits a thioredoxin dependent methionine sulfoxide reductase
activity; the Cys-495 is probably involved in the reduction of
MetSO and in formation of the sulfenic acid derivative. The
regeneration of Cys-495 is probably done via formation of a
disulfide bond with Cys-440 followed by its reduction by
thioredoxin.
-!- DISRUPTION PHENOTYPE: Hyperpiliated and hyperadherent.
{ECO:0000269|PubMed:8755589}.
-!- SIMILARITY: In the N-terminal section; belongs to the thioredoxin
family. {ECO:0000305}.
-!- SIMILARITY: In the central section; belongs to the MsrA Met
sulfoxide reductase family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the MsrB Met
sulfoxide reductase family. {ECO:0000305}.
-!- CAUTION: Was originally thought to play a role along with PilA in
the transcription regulation of PilE.
{ECO:0000305|PubMed:2854063}.
-!- SEQUENCE CAUTION:
Sequence=CAA32146.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; X13966; CAA32146.1; ALT_FRAME; Genomic_DNA.
EMBL; AF482946; AAL89752.1; -; Genomic_DNA.
PIR; S02018; S02018.
RefSeq; WP_003696288.1; NZ_MBCV01000007.1.
PDB; 1L1D; X-ray; 1.85 A; A/B=375-522.
PDB; 2H30; X-ray; 1.60 A; A=23-182.
PDBsum; 1L1D; -.
PDBsum; 2H30; -.
ProteinModelPortal; P14930; -.
SMR; P14930; -.
PATRIC; fig|485.49.peg.1916; -.
eggNOG; ENOG4105E0X; Bacteria.
eggNOG; COG0225; LUCA.
eggNOG; COG0229; LUCA.
eggNOG; COG0526; LUCA.
BRENDA; 1.8.4.11; 3590.
BRENDA; 1.8.4.12; 3590.
EvolutionaryTrace; P14930; -.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IEA:UniProtKB-EC.
GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:UniProtKB-EC.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0030091; P:protein repair; IEA:InterPro.
GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
Gene3D; 3.30.1060.10; -; 1.
HAMAP; MF_01401; MsrA; 1.
HAMAP; MF_01400; MsrB; 1.
InterPro; IPR028427; Met_Sox_Rdtase.
InterPro; IPR002569; Met_Sox_Rdtase_MsrA.
InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
InterPro; IPR002579; Met_Sox_Rdtase_MsrB.
InterPro; IPR011057; Mss4-like_sf.
InterPro; IPR013740; Redoxin.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR013766; Thioredoxin_domain.
PANTHER; PTHR10173; PTHR10173; 1.
Pfam; PF01625; PMSR; 1.
Pfam; PF08534; Redoxin; 1.
Pfam; PF01641; SelR; 1.
SUPFAM; SSF51316; SSF51316; 1.
SUPFAM; SSF52833; SSF52833; 1.
SUPFAM; SSF55068; SSF55068; 1.
TIGRFAMs; TIGR00401; msrA; 1.
TIGRFAMs; TIGR00357; TIGR00357; 1.
PROSITE; PS51790; MSRB; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
1: Evidence at protein level;
3D-structure; Disulfide bond; Electron transport;
Multifunctional enzyme; Oxidoreductase; Redox-active center;
Transport.
CHAIN 1 522 Peptide methionine sulfoxide reductase
MsrA/MsrB.
/FTId=PRO_0000138508.
DOMAIN 17 174 Thioredoxin.
DOMAIN 383 506 MsrB. {ECO:0000255|PROSITE-
ProRule:PRU01126}.
REGION 199 354 Peptide methionine sulfoxide reductase A.
ACT_SITE 207 207 {ECO:0000250}.
ACT_SITE 495 495 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU01126}.
DISULFID 68 71 Redox-active. {ECO:0000250}.
DISULFID 440 495 Redox-active. {ECO:0000250}.
HELIX 34 38 {ECO:0000244|PDB:2H30}.
STRAND 46 48 {ECO:0000244|PDB:2H30}.
HELIX 49 52 {ECO:0000244|PDB:2H30}.
STRAND 59 63 {ECO:0000244|PDB:2H30}.
HELIX 69 82 {ECO:0000244|PDB:2H30}.
HELIX 85 87 {ECO:0000244|PDB:2H30}.
STRAND 90 96 {ECO:0000244|PDB:2H30}.
HELIX 108 113 {ECO:0000244|PDB:2H30}.
STRAND 123 125 {ECO:0000244|PDB:2H30}.
HELIX 130 134 {ECO:0000244|PDB:2H30}.
STRAND 139 146 {ECO:0000244|PDB:2H30}.
STRAND 152 158 {ECO:0000244|PDB:2H30}.
HELIX 162 170 {ECO:0000244|PDB:2H30}.
HELIX 177 179 {ECO:0000244|PDB:2H30}.
HELIX 383 386 {ECO:0000244|PDB:1L1D}.
TURN 387 389 {ECO:0000244|PDB:1L1D}.
HELIX 392 400 {ECO:0000244|PDB:1L1D}.
HELIX 410 413 {ECO:0000244|PDB:1L1D}.
STRAND 417 422 {ECO:0000244|PDB:1L1D}.
TURN 423 425 {ECO:0000244|PDB:1L1D}.
STRAND 428 431 {ECO:0000244|PDB:1L1D}.
HELIX 432 434 {ECO:0000244|PDB:1L1D}.
STRAND 439 442 {ECO:0000244|PDB:1L1D}.
STRAND 444 447 {ECO:0000244|PDB:1L1D}.
STRAND 453 459 {ECO:0000244|PDB:1L1D}.
STRAND 466 471 {ECO:0000244|PDB:1L1D}.
TURN 472 474 {ECO:0000244|PDB:1L1D}.
STRAND 477 483 {ECO:0000244|PDB:1L1D}.
HELIX 487 489 {ECO:0000244|PDB:1L1D}.
STRAND 493 496 {ECO:0000244|PDB:1L1D}.
HELIX 498 500 {ECO:0000244|PDB:1L1D}.
STRAND 501 505 {ECO:0000244|PDB:1L1D}.
HELIX 506 512 {ECO:0000244|PDB:1L1D}.
HELIX 515 520 {ECO:0000244|PDB:1L1D}.
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


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