Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Peptide methionine sulfoxide reductase MsrA/MsrB

Gene

msrAB

Organism
Neisseria gonorrhoeae
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity

Catalytic activityi

Peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin.
L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin.
Peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei207 – 2071By similarity
Active sitei495 – 4951NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Enzyme and pathway databases

BRENDAi1.8.4.11. 3590.
1.8.4.12. 3590.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptide methionine sulfoxide reductase MsrA/MsrB
Including the following 3 domains:
Thioredoxin
Peptide methionine sulfoxide reductase MsrA (EC:1.8.4.11)
Short name:
Protein-methionine-S-oxide reductase
Alternative name(s):
Peptide-methionine (S)-S-oxide reductase
Short name:
Peptide Met(O) reductase
Peptide methionine sulfoxide reductase MsrB (EC:1.8.4.12)
Alternative name(s):
Peptide-methionine (R)-S-oxide reductase
Gene namesi
Name:msrAB
Synonyms:pilB
OrganismiNeisseria gonorrhoeae
Taxonomic identifieri485 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Pathology & Biotechi

Disruption phenotypei

Hyperpiliated and hyperadherent.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 522522Peptide methionine sulfoxide reductase MsrA/MsrBPRO_0000138508Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi68 ↔ 71Redox-activeBy similarity
Disulfide bondi440 ↔ 495Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi528357.NgonPI_010100000505.

Structurei

Secondary structure

1
522
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi34 – 385Combined sources
Beta strandi46 – 483Combined sources
Helixi49 – 524Combined sources
Beta strandi59 – 635Combined sources
Helixi69 – 8214Combined sources
Helixi85 – 873Combined sources
Beta strandi90 – 967Combined sources
Helixi108 – 1136Combined sources
Beta strandi123 – 1253Combined sources
Helixi130 – 1345Combined sources
Beta strandi139 – 1468Combined sources
Beta strandi152 – 1587Combined sources
Helixi162 – 1709Combined sources
Helixi177 – 1793Combined sources
Helixi383 – 3864Combined sources
Turni387 – 3893Combined sources
Helixi392 – 4009Combined sources
Helixi410 – 4134Combined sources
Beta strandi417 – 4226Combined sources
Turni423 – 4253Combined sources
Beta strandi428 – 4314Combined sources
Helixi432 – 4343Combined sources
Beta strandi439 – 4424Combined sources
Beta strandi444 – 4474Combined sources
Beta strandi453 – 4597Combined sources
Beta strandi466 – 4716Combined sources
Turni472 – 4743Combined sources
Beta strandi477 – 4837Combined sources
Helixi487 – 4893Combined sources
Beta strandi493 – 4964Combined sources
Helixi498 – 5003Combined sources
Beta strandi501 – 5055Combined sources
Helixi506 – 5127Combined sources
Helixi515 – 5206Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L1DX-ray1.85A/B375-522[»]
2H30X-ray1.60A23-182[»]
ProteinModelPortaliP14930.
SMRiP14930. Positions 32-182, 196-364, 375-521.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14930.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 174158ThioredoxinAdd
BLAST
Domaini383 – 506124MsrBPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni199 – 354156Peptide methionine sulfoxide reductase AAdd
BLAST

Domaini

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.

Sequence similaritiesi

In the N-terminal section; belongs to the thioredoxin family.Curated
In the central section; belongs to the MsrA Met sulfoxide reductase family.Curated
In the C-terminal section; belongs to the MsrB Met sulfoxide reductase family.Curated
Contains 1 MsrB (methionine-R-sulfoxide reductase) domain.PROSITE-ProRule annotation
Contains 1 thioredoxin domain.Curated

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG4105E0X. Bacteria.
COG0225. LUCA.
COG0229. LUCA.
COG0526. LUCA.

Family and domain databases

Gene3Di2.170.150.20. 1 hit.
3.30.1060.10. 1 hit.
3.40.30.10. 1 hit.
HAMAPiMF_01400. MsrB.
MF_01401. MsrA.
InterProiIPR028427. Met_Sox_Rdtase.
IPR002569. Met_Sox_Rdtase_MsrA.
IPR002579. Met_Sox_Rdtase_MsrB.
IPR011057. Mss4-like.
IPR013740. Redoxin.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERiPTHR10173. PTHR10173. 2 hits.
PfamiPF01625. PMSR. 1 hit.
PF08534. Redoxin. 1 hit.
PF01641. SelR. 1 hit.
[Graphical view]
SUPFAMiSSF51316. SSF51316. 1 hit.
SSF52833. SSF52833. 1 hit.
SSF55068. SSF55068. 1 hit.
TIGRFAMsiTIGR00401. msrA. 1 hit.
TIGR00357. TIGR00357. 1 hit.
PROSITEiPS51790. MSRB. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P14930-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKHRTFFSLC AKFGCLLALG ACSPKIVDAG TATVPHTLST LKTADNRPAS
60 70 80 90 100
VYLKKDKPTL IKFWASWCPL CLSELGQAEK WAQDAKFSSA NLITVASPGF
110 120 130 140 150
LHEKKDGEFQ KWYAGLNYPK LPVVTDNGGT IAQNLNISVY PSWALIGKDG
160 170 180 190 200
DVQRIVKGSI NEAQALALIR NPNADLGSLK HSFYKPDTQK KDSAIMNTRT
210 220 230 240 250
IYLAGGCFWG LEAYFQRIDG VVDAVSGYAN GNTENPSYED VSYRHTGHAE
260 270 280 290 300
TVKVTYDADK LSLDDILQYY FRVVDPTSLN KQGNDTGTQY RSGVYYTDPA
310 320 330 340 350
EKAVIAAALK REQQKYQLPL VVENEPLKNF YDAEEYHQDY LIKNPNGYCH
360 370 380 390 400
IDIRKADEPL PGKTKAAPQG KGFDAATYKK PSDAELKRTL TEEQYQVTQN
410 420 430 440 450
SATEYAFSHE YDHLFKPGIY VDVVSGEPLF SSADKYDSGC GWPSFTRPID
460 470 480 490 500
AKSVTEHDDF SFNMRRTEVR SRAADSHLGH VFPDGPRDKG GLRYCINGAS
510 520
LKFIPLEQMD AAGYGALKGE VK
Length:522
Mass (Da):57,959
Last modified:May 2, 2002 - v2
Checksum:iDDC8EC308B57B30C
GO

Sequence cautioni

The sequence CAA32146.1 differs from that shown. Reason: Frameshift at several positions. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13966 Genomic DNA. Translation: CAA32146.1. Frameshift.
AF482946 Genomic DNA. Translation: AAL89752.1.
PIRiS02018.
RefSeqiWP_003696288.1. NZ_CQNF01000032.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13966 Genomic DNA. Translation: CAA32146.1. Frameshift.
AF482946 Genomic DNA. Translation: AAL89752.1.
PIRiS02018.
RefSeqiWP_003696288.1. NZ_CQNF01000032.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L1DX-ray1.85A/B375-522[»]
2H30X-ray1.60A23-182[»]
ProteinModelPortaliP14930.
SMRiP14930. Positions 32-182, 196-364, 375-521.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi528357.NgonPI_010100000505.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105E0X. Bacteria.
COG0225. LUCA.
COG0229. LUCA.
COG0526. LUCA.

Enzyme and pathway databases

BRENDAi1.8.4.11. 3590.
1.8.4.12. 3590.

Miscellaneous databases

EvolutionaryTraceiP14930.

Family and domain databases

Gene3Di2.170.150.20. 1 hit.
3.30.1060.10. 1 hit.
3.40.30.10. 1 hit.
HAMAPiMF_01400. MsrB.
MF_01401. MsrA.
InterProiIPR028427. Met_Sox_Rdtase.
IPR002569. Met_Sox_Rdtase_MsrA.
IPR002579. Met_Sox_Rdtase_MsrB.
IPR011057. Mss4-like.
IPR013740. Redoxin.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERiPTHR10173. PTHR10173. 2 hits.
PfamiPF01625. PMSR. 1 hit.
PF08534. Redoxin. 1 hit.
PF01641. SelR. 1 hit.
[Graphical view]
SUPFAMiSSF51316. SSF51316. 1 hit.
SSF52833. SSF52833. 1 hit.
SSF55068. SSF55068. 1 hit.
TIGRFAMsiTIGR00401. msrA. 1 hit.
TIGR00357. TIGR00357. 1 hit.
PROSITEiPS51790. MSRB. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF PEPTIDE METHIONINE SULFOXIDE REDUCTASE ACTIVITY, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiMSRAB_NEIGO
AccessioniPrimary (citable) accession number: P14930
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: May 2, 2002
Last modified: April 13, 2016
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Was originally thought to play a role along with PilA in the transcription regulation of PilE.1 Publication

Keywords - Technical termi

3D-structure, Multifunctional enzyme

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.