RegulonDB RegulonDB 10.8: Gene Form
   

msrA gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

tamA msrA unknown tamB Fis Fis terminator tamAp1 tamAp1 TSS_5075 (cluster) TSS_5075 (cluster) msrAp msrAp TSS_5074 TSS_5074 ytfLp3 ytfLp3

Gene      
Name: msrA    Texpresso search in the literature
Synonym(s): ECK4215, EG11433, b4219, pms, pmsR
Genome position(nucleotides): 4441538 <-- 4442176 Genome Browser
Strand: reverse
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
54.46
External database links:  
ASAP:
ABE-0013804
CGSC:
34400
ECHOBASE:
EB1403
OU-MICROARRAY:
b4219
PortEco:
msrA
STRING:
511145.b4219
COLOMBOS: msrA


Product      
Name: methionine sulfoxide reductase A
Synonym(s): MsrA, Pms, PmsR
Sequence: Get amino acid sequence Fasta Format
Cellular location: cytosol
Molecular weight: 23.315
Isoelectric point: 4.825
Motif(s):
 
Type Positions Sequence
2 -> 212 SLFDKKHLVSPADALPGRNTPMPVATLHAVNGHSMTNVPDGMEIAIFAMGCFWGVERLFWQLPGVYSTAAGYTGGYTPNPTYREVCSGDTGHAEAVRIVYDPSVISYEQLLQVFWENHDPAQGMRQGNDHGTQYRSAIYPLTPEQDAAARASLERFQAAMLAADDDRHITTEIANATPFYYAEDDHQQYLHKNPYGYCGIGGIGVCLPPEA
46 -> 199 AIFAMGCFWGVERLFWQLPGVYSTAAGYTGGYTPNPTYREVCSGDTGHAEAVRIVYDPSVISYEQLLQVFWENHDPAQGMRQGNDHGTQYRSAIYPLTPEQDAAARASLERFQAAMLAADDDRHITTEIANATPFYYAEDDHQQYLHKNPYGYC
87 -> 87 C
199 -> 199 C
52 -> 52 C

 

Classification:
Multifun Terms (GenProtEC)  
  2 - information transfer --> 2.3 - protein related --> 2.3.4 - chaperoning, repair (refolding)
  5 - cell processes --> 5.10 - defense/survival
  5 - cell processes --> 5.5 - adaptations --> 5.5.6 - other (mechanical, nutritional, oxidative stress)
Gene Ontology Terms (GO)  
cellular_component GO:0005737 - cytoplasm
GO:0005829 - cytosol
molecular_function GO:0016491 - oxidoreductase activity
GO:0016671 - oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor
GO:0008113 - peptide-methionine (S)-S-oxide reductase activity
GO:0036456 - L-methionine-(S)-S-oxide reductase activity
biological_process GO:0006464 - cellular protein modification process
GO:0006979 - response to oxidative stress
GO:0030091 - protein repair
GO:0055114 - oxidation-reduction process
GO:0034599 - cellular response to oxidative stress
Note(s): Note(s): ...[more].
Reference(s): [1] Alexander RW. 2000
[2] Brot N., et al., 1981
[3] Coudevylle N., et al., 2006
[4] Coudevylle N., et al., 2004
[5] Levine RL., et al., 1999
[6] Lin TY. 1999
[7] Rahman MA., et al., 1992
[8] Vaughan MD., et al., 2002
External database links:  
ECOCYC:
EG11433-MONOMER
ECOLIWIKI:
b4219
INTERPRO:
IPR036509
INTERPRO:
IPR002569
PANTHER:
PTHR10173
PDB:
2IEM
PDB:
1FF3
PDB:
2GT3
PFAM:
PF01625
PRIDE:
P0A744
PRODB:
PRO_000023298
REFSEQ:
NP_418640
SMR:
P0A744
UNIPROT:
P0A744


Operon      
Name: msrA         
Operon arrangement:
Transcription unit        Promoter
msrA


Transcriptional Regulation      
Display Regulation             
Repressed by: Fis


Elements in the selected gene context region unrelated to any object in RegulonDB      

  Type Name Post Left Post Right Strand Notes Evidence (Confirmed, Strong, Weak) References
  promoter ytfLp3 4441321 reverse Similarity to the consensus
Read more >
[ICWHO] [9]
  promoter TSS_5074 4442251 forward nd [RS-EPT-CBR] [10]
  promoter TSS_5075 (cluster) 4442263 reverse For this promoter, there
Read more >
[RS-EPT-CBR] [10]
  promoter tamAp1 4442270 forward Similarity to the consensus
Read more >
[ICWHO] [9]


Evidence    

 [ICWHO] Inferred computationally without human oversight

 [RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates



Reference(s)    

 [1] Alexander RW., 2000, Reducing (oxidative) stress: structure and mechanism., Trends Biochem Sci 25(12):643

 [2] Brot N., Weissbach L., Werth J., Weissbach H., 1981, Enzymatic reduction of protein-bound methionine sulfoxide., Proc Natl Acad Sci U S A 78(4):2155-8

 [3] Coudevylle N., Antoine M., Boschi-Muller S., Branlant G., Cung MT., 2006, 1H, 13C and 15N resonance assignment of an oxidized form (Cys51-Cys198) of methionine sulfoxide reductase A from Escherichia coli., J Biomol NMR 36 Suppl 1:19

 [4] Coudevylle N., Thureau A., Azza S., Boshi-Muller S., Branlant G., Cung MT., 2004, (1)H, (13)C and (15)N resonance assignment of the reduced form of methionine sulfoxide reductase A from Escherichia coli., J Biomol NMR 30(3):363-4

 [5] Levine RL., Berlett BS., Moskovitz J., Mosoni L., Stadtman ER., 1999, Methionine residues may protect proteins from critical oxidative damage., Mech Ageing Dev 107(3):323-32

 [6] Lin TY., 1999, G33D mutant thioredoxin primarily affects the kinetics of reaction with thioredoxin reductase. Probing the structure of the mutant protein., Biochemistry 38(47):15508-13

 [7] Rahman MA., Brot N., Weissbach H., 1992, High level expression and purification of peptide methionine sulfoxide reductase in Escherichia coli., Cell Mol Biol 38(5):529-42

 [8] Vaughan MD., Sampson PB., Honek JF., 2002, Methionine in and out of proteins: targets for drug design., Curr Med Chem 9(3):385-409

 [9] Huerta AM., Collado-Vides J., 2003, Sigma70 promoters in Escherichia coli: specific transcription in dense regions of overlapping promoter-like signals., J Mol Biol 333(2):261-78

 [10] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.


RegulonDB