Reviewed, UniProtKB/Swiss-Prot Q9K1N8 (MSRAB_NEIMB)

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:	NMB0044

Organism

Neisseria meningitidis serogroup B [Complete proteome] [HAMAP]

Taxonomic identifier

491 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria

Protein attributes

Sequence length	522 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine By similarity. HAMAP MF_01400
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
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	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_0000138510
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		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9K1N8-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 535A823EDB76BFD1	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 PSWALIGKDS 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 AAGYGALKGK VK

References

[1]

"Complete genome sequence of Neisseria meningitidis serogroup B strain MC58." Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H., Salzberg S.L., White O. , Fleischmann R.D., Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C. Science 287:1809-1815(2000) [PubMed: 10710307] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MC58 / Serogroup B.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE002098 Genomic DNA. Translation: AAF40515.1.
PIR	G81243.
RefSeq	NP_273110.1.
3D structure databases
SMR	Q9K1N8. Positions 32-182, 196-364, 375-521.
ModBase	Search...
Genome annotation databases
GeneID	902147.
GenomeReviews	Gene locus NMB0044 in contig AE002098_GR.
KEGG	nme:NMB0044.
NMPDR	fig|122586.1.peg.44.
TIGR	NMB0044.
Phylogenomic databases
HOGENOM	HBG715255.
OMA	YYFRVVD.
Enzyme and pathway databases
BioCyc	NMEN122586:NMB_0044-MONOMER.
BRENDA	1.8.4.11. 293828. 1.8.4.12. 293828.
Family and domain databases
HAMAP	MF_01400. MsrB. Fused. [Tree] MF_01401. MsrA. Fused. [Tree]
InterPro	IPR002579. Methionine_sulphoxide_MsrB. IPR011057. Mss4-like. IPR002569. Peptide_Met_Sox_Rdtase_MsrA. IPR013740. Redoxin. IPR017936. Thioredoxin-like. IPR012336. Thioredoxin-like_fold. 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]
TIGRFAMs	TIGR00401. msrA. 1 hit. TIGR00357. MsrB. 1 hit.
PROSITE	PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MSRAB_NEIMB

Accession

Primary (citable) accession number: Q9K1N8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2002
Last sequence update:	October 1, 2000
Last modified:	February 9, 2010
This is version 66 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)