Reviewed, UniProtKB/Swiss-Prot Q9JWM8 (MSRAB_NEIMA)

Names and origin

Protein names

Recommended name:
    Peptide methionine sulfoxide reductase msrA/msrB
Including the following 3 domains:
    1- Recommended name:
            Thioredoxin
    2- Recommended name:
            Peptide methionine sulfoxide reductase msrA
                Short name=Protein-methionine-S-oxide reductase
              EC=1.8.4.11
        Alternative name(s):
            Peptide-methionine (S)-S-oxide reductase
              Short name=Peptide Met(O) reductase
    3- Recommended name:
            Peptide methionine sulfoxide reductase msrB
              EC=1.8.4.12
        Alternative name(s):
            Peptide-methionine (R)-S-oxide reductase

Gene names

Name:	msrAB
Synonyms:	pilB
Ordered Locus Names:	NMA0290

Organism

Neisseria meningitidis serogroup A [Complete proteome] [HAMAP]

Taxonomic identifier

65699 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria

Protein attributes

Sequence length	522 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

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.
Catalytic activity	Peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin. HAMAP MF_01400 L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin. HAMAP MF_01400 Peptide-L-methionine + thioredoxin disulfide + H2O = 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. HAMAP MF_01400
Miscellaneous	The domain msrB is stereospecific for the R isomer of the sulfoxide of MetSO whereas the domain msrA is stereospecific for the S isomer. HAMAP MF_01400
Sequence similarities	In the N-terminal section; belongs to the thioredoxin family. In the central section; belongs to the msrA Met sulfoxide reductase family. In the C-terminal section; belongs to the msrB Met sulfoxide reductase family. Contains 1 thioredoxin domain.

Ontologies

Keywords
Biological process	Electron transport Transport
Domain	Redox-active center
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW protein modification process Inferred from electronic annotation. Source: HAMAP transport Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	peptide-methionine (R)-S-oxide reductase activity Inferred from electronic annotation. Source: EC peptide-methionine-(S)-S-oxide reductase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 522

522

Peptide methionine sulfoxide reductase msrA/msrB HAMAP MF_01400

PRO_0000138509

Regions

Domain

17 – 174

158

Thioredoxin

Region

199 – 354

156

Peptide methionine sulfoxide reductase A HAMAP MF_01400

Region

383 – 506

124

Peptide methionine sulfoxide reductase B HAMAP MF_01400

Sites

Active site

207

1

By similarity

Amino acid modifications

Disulfide bond

68 ↔ 71

Redox-active By similarity

Disulfide bond

440 ↔ 495

Probable

Secondary structure

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522

Helix Strand Turn

Details...

Helix

35 – 39

5

Helix

49 – 52

4

Beta strand

59 – 64

6

Helix

69 – 72

4

Helix

75 – 83

9

Helix

85 – 87

3

Beta strand

90 – 96

7

Helix

108 – 113

6

Beta strand

123 – 125

3

Helix

130 – 134

5

Beta strand

139 – 146

8

Beta strand

152 – 158

7

Helix

162 – 170

9

Beta strand

198 – 206

9

Helix

208 – 216

9

Beta strand

221 – 230

10

Beta strand

232 – 235

4

Helix

238 – 243

6

Beta strand

249 – 257

9

Turn

258 – 260

3

Helix

263 – 273

11

Beta strand

285 – 287

3

Helix

288 – 290

3

Beta strand

292 – 298

7

Helix

301 – 314

14

Beta strand

323 – 326

4

Beta strand

330 – 332

3

Helix

335 – 337

3

Helix

340 – 343

4

Helix

353 – 357

5

Sequences

	Sequence		Length	Mass (Da)
	Q9JWM8-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: F61E8EA7189F0667	FASTA	522	58,015
	10 20 30 40 50 60 MKHRTFFSLC AKFGCLLALG ACSPKIVDAG AATVPHTLST LKTADNRPAS VYLKKDKPTL 70 80 90 100 110 120 IKFWASWCPL CLSELGQTEK WAQDAKFSSA NLITVASPGF LHEKKDGDFQ KWYAGLNYPK 130 140 150 160 170 180 LPVVTDNGGT IAQSLNISVY PSWALIGKDG DVQRIVKGSI NEAQALALIR DPNADLGSLK 190 200 210 220 230 240 HSFYKPDTQK KDSKIMNTRT IYLAGGCFWG LEAYFQRIDG VVDAVSGYAN GNTKNPSYED 250 260 270 280 290 300 VSYRHTGHAE TVKVTYDADK LSLDDILQYF FRVVDPTSLN KQGNDTGTQY RSGVYYTDPA 310 320 330 340 350 360 EKAVIAAALK REQQKYQLPL VVENEPLKNF YDAEEYHQDY LIKNPNGYCH IDIRKADEPL 370 380 390 400 410 420 PGKTKTAPQG KGFDAATYKK PSDAELKRTL TEEQYQVTQN SATEYAFSHE YDHLFKPGIY 430 440 450 460 470 480 VDVVSGEPLF SSADKYDSGC GWPSFTRPID AKSVTEHDDF SYNMRRTEVR SHAADSHLGH 490 500 510 520 VFPDGPRDKG GLRYCINGAS LKFIPLEQMD AAGYGALKSK VK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete DNA sequence of a serogroup A strain of Neisseria meningitidis Z2491." Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M., Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M., Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K., Leather S. , Moule S., Mungall K.L., Quail M.A., Rajandream M.A., Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G., Barrell B.G. Nature 404:502-506(2000) [PubMed: 10761919] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Z2491 / Serogroup A / Serotype 4A.
[2]	"Characterization of the methionine sulfoxide reductase activities of PILB, a probable virulence factor from Neisseria meningitidis." Olry A., Boschi-Muller S., Marraud M., Sanglier-Cianferani S., van Dorsselaer A., Branlant G. J. Biol. Chem. 277:12016-12022(2002) [PubMed: 11812798] [Abstract] Cited for: IDENTIFICATION OF THE METHIONINE SULFOXIDE REDUCTASE ACTIVITIES (MSRA AND MSRB). Strain: Z2491 / Serogroup A / Serotype 4A.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AL157959 Genomic DNA. Translation: CAM07595.1.

PIR

E82024.

RefSeq

YP_002341814.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FY6	X-ray	1.90	A	34-176	[»]
2JZR	NMR	-	A	34-176	[»]
2JZS	NMR	-	A	34-176	[»]
3BQE	X-ray	2.00	A	196-389	[»]
3BQF	X-ray	2.24	A	196-389	[»]
3BQG	X-ray	2.00	A	196-389	[»]
3BQH	X-ray	1.95	A	197-389	[»]

SMR

Q9JWM8. Positions 375-521.

ModBase

Search...

Genome annotation databases

GeneID

906298.

GenomeReviews

Gene locus NMA0290 in contig AL157959_GR.

KEGG

nma:NMA0290.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

Q9JWM8.

OMA

Q9JWM8. YYFRVVD.

Enzyme and pathway databases

BioCyc

NMEN122587:NMA0290-MON.

BRENDA

1.8.4.11. 292829.
1.8.4.12. 292829.

Family and domain databases

HAMAP

MF_01400. Fused.
[Tree]
MF_01401. Fused.
[Tree]

InterPro

IPR002579. Methionine_sulphoxide_MsrB.
IPR002569. MsrA.
IPR013740. Redoxin.
IPR017936. Thioredoxin-like.
IPR012335. Thioredoxin_fold.
[Graphical view]

Gene3D

G3DSA:3.30.1060.10. MsrA. 1 hit.
G3DSA:2.170.150.20. MsrB. 1 hit.
G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

Pfam

PF01625. PMSR. 1 hit.
PF08534. Redoxin. 1 hit.
PF01641. SelR. 1 hit.
[Graphical view]

ProDom

PD004057. DUF25. 1 hit.
PD003489. PMSR. 1 hit.
PD003679. Thioredoxin_like. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR00401. msrA. 1 hit.
TIGR00357. MsrB. 1 hit.

PROSITE

PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

MSRAB_NEIMA

Accession

Primary (citable) accession number: Q9JWM8
Secondary accession number(s): A1IPD1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2002
Last sequence update:	October 1, 2000
Last modified:	June 16, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)