Reviewed, UniProtKB/Swiss-Prot P14930 (MSRAB_NEIGO)

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

Organism

Neisseria gonorrhoeae

Taxonomic identifier

485 [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
Disruption phenotype	Hyperpiliated and hyperadherent. Ref.3
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.
Caution	Was originally (Ref.1) thought to play a role along with pilA in the transcription regulation of pilE.
Sequence caution	The sequence CAA32146.1 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
Biological process	Electron transport Transport
Domain	Redox-active center
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	3D-structure 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_0000138508

Regions

Domain

17 – 174

158

Thioredoxin

Region

199 – 354

156

Peptide methionine sulfoxide reductase A HAMAP MF_01400

Region

383 – 522

140

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

Redox-active By similarity

Secondary structure

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522

Helix Strand Turn

Details...

Helix

34 – 38

5

Beta strand

46 – 48

3

Helix

49 – 52

4

Beta strand

59 – 63

5

Helix

69 – 82

14

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

Helix

177 – 179

3

Helix

383 – 386

4

Turn

387 – 389

3

Helix

392 – 400

9

Helix

410 – 413

4

Beta strand

417 – 422

6

Turn

423 – 425

3

Beta strand

428 – 431

4

Helix

432 – 434

3

Beta strand

439 – 442

4

Beta strand

444 – 447

4

Beta strand

453 – 459

7

Beta strand

466 – 471

6

Turn

472 – 474

3

Beta strand

477 – 483

7

Helix

487 – 489

3

Beta strand

493 – 496

4

Helix

498 – 500

3

Beta strand

501 – 505

5

Helix

506 – 512

7

Helix

515 – 520

6

Sequences

	Sequence		Length	Mass (Da)
	P14930-1 [UniParc]. Last modified May 2, 2002. Version 2. Checksum: DDC8EC308B57B30C	FASTA	522	57,959
	10 20 30 40 50 60 MKHRTFFSLC AKFGCLLALG ACSPKIVDAG TATVPHTLST LKTADNRPAS VYLKKDKPTL 70 80 90 100 110 120 IKFWASWCPL CLSELGQAEK WAQDAKFSSA NLITVASPGF LHEKKDGEFQ KWYAGLNYPK 130 140 150 160 170 180 LPVVTDNGGT IAQNLNISVY PSWALIGKDG DVQRIVKGSI NEAQALALIR NPNADLGSLK 190 200 210 220 230 240 HSFYKPDTQK KDSAIMNTRT IYLAGGCFWG LEAYFQRIDG VVDAVSGYAN GNTENPSYED 250 260 270 280 290 300 VSYRHTGHAE TVKVTYDADK LSLDDILQYY FRVVDPTSLN KQGNDTGTQY RSGVYYTDPA 310 320 330 340 350 360 EKAVIAAALK REQQKYQLPL VVENEPLKNF YDAEEYHQDY LIKNPNGYCH IDIRKADEPL 370 380 390 400 410 420 PGKTKAAPQG KGFDAATYKK PSDAELKRTL TEEQYQVTQN SATEYAFSHE YDHLFKPGIY 430 440 450 460 470 480 VDVVSGEPLF SSADKYDSGC GWPSFTRPID AKSVTEHDDF SFNMRRTEVR SRAADSHLGH 490 500 510 520 VFPDGPRDKG GLRYCINGAS LKFIPLEQMD AAGYGALKGE VK

References

[1]	"Pilin expression in Neisseria gonorrhoeae is under both positive and negative transcriptional control." Taha M.K., So M., Seifert H.S., Billyard E., Marchal C. EMBO J. 7:4367-4378(1988) [PubMed: 2854063] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: MS11A.
[2]	Lowther W.T., Brot N., Weissbach H., Honek J.F., Matthews B.W. Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Peptide methionine sulfoxide reductase contributes to the maintenance of adhesins in three major pathogens." Wizemann T.M., Moskovitz J., Pearce B.J., Cundell D., Arvidson C.G., So M., Weissbach H., Brot N., Masure H.R. Proc. Natl. Acad. Sci. U.S.A. 93:7985-7990(1996) [PubMed: 8755589] [Abstract] Cited for: IDENTIFICATION OF PEPTIDE METHIONINE SULFOXIDE REDUCTASE ACTIVITY, DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X13966 Genomic DNA. Translation: CAA32146.1. Frameshift.
AF482946 Genomic DNA. Translation: AAL89752.1.

PIR

S02018.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1L1D	X-ray	1.85	A/B	375-522	[»]
2H30	X-ray	1.60	A	23-182	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

1.8.4.11. 588.
1.8.4.12. 588.

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_NEIGO

Accession

Primary (citable) accession number: P14930

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	May 2, 2002
Last modified:	March 3, 2009
This is version 81 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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