RegulonDB RegulonDB 11.1: Gene Form
   

dmsB gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

dmsA dmsC dmsB dmsCp dmsCp TSS_1098 (cluster) TSS_1098 (cluster) TSS_1097 TSS_1097 TSS_1096 TSS_1096 TSS_1095 TSS_1095 TSS_1094 TSS_1094

Gene      
Name: dmsB    Texpresso search in the literature
Synonym(s): ECK0886, EG10233, b0895
Genome position(nucleotides): 943414 --> 944031
Strand: forward
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
51.78
External database links:  
ASAP:
ABE-0003046
CGSC:
31724
ECHOBASE:
EB0229
ECOLIHUB:
dmsB
OU-MICROARRAY:
b0895
STRING:
511145.b0895
COLOMBOS: dmsB


Product      
Name: dimethyl sulfoxide reductase subunit B
Synonym(s): DmsB, dimethyl sulfoxide reductase, chain B
Sequence: Get amino acid sequence Fasta Format
Cellular location: inner membrane
Molecular weight: 22.869
Isoelectric point: 6.59
Motif(s):
 
Type Positions Sequence Comment
2 -> 205 TTQYGFFIDSSRCTGCKTCELACKDYKDLTPEVSFRRIYEYAGGDWQEDNGVWHQNVFAYYLSISCNHCEDPACTKVCPSGAMHKREDGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMTKCDGCYDRVAEGKKPICVESCPLRALDFGPIDELRKKHGDLAAVAPLPRAHFTKPNIVIKPNANSRPTGDTTGYLANPKEV UniProt: Anaerobic dimethyl sulfoxide reductase chain B.
5 -> 33 YGFFIDSSRCTGCKTCELACKDYKDLTPE UniProt: 4Fe-4S ferredoxin-type 1.
12 -> 26 SRCTGCKTCELACKD
59 -> 153 FAYYLSISCNHCEDPACTKVCPSGAMHKREDGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMTKCDGCYDRVAEGKKPICVESCPLRALDFG
90 -> 119 GFVVVDEDVCIGCRYCHMACPYGAPQYNET UniProt: 4Fe-4S ferredoxin-type 3.

 

Classification:
Multifun Terms (GenProtEC)  
  1 - metabolism --> 1.3 - energy metabolism, carbon --> 1.3.7 - anaerobic respiration
  1 - metabolism --> 1.4 - energy production/transport --> 1.4.2 - electron acceptors
  6 - cell structure --> 6.1 - membrane
Gene Ontology Terms (GO)  
cellular_component GO:0005886 - plasma membrane
GO:0031237 - intrinsic component of periplasmic side of plasma membrane
GO:0009390 - dimethyl sulfoxide reductase complex
molecular_function GO:0005515 - protein binding
GO:0046872 - metal ion binding
GO:0051536 - iron-sulfur cluster binding
GO:0051539 - 4 iron, 4 sulfur cluster binding
GO:0009389 - dimethyl sulfoxide reductase activity
biological_process GO:0018907 - dimethyl sulfoxide metabolic process
GO:0009061 - anaerobic respiration
GO:0019645 - anaerobic electron transport chain
Note(s): Note(s): ...[more].
External database links:  
ALPHAFOLD:
P18776
DIP:
DIP-9453N
ECOCYC:
DMSB-MONOMER
ECOLIWIKI:
b0895
INTERPRO:
IPR014297
INTERPRO:
IPR017896
INTERPRO:
IPR017900
MODBASE:
P18776
PFAM:
PF13247
PFAM:
PF12800
PRIDE:
P18776
PRODB:
PRO_000022456
PROSITE:
PS00198
PROSITE:
PS51379
REFSEQ:
NP_415415
SMR:
P18776
UNIPROT:
P18776


Operon      
Name: dmsABC         
Operon arrangement:
Transcription unit        Promoter
dmsABC
dmsABC
dmsC


Transcriptional Regulation      
Display Regulation             
Activated by: FNR
Repressed by: IHF, NarL, ModE, 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 TSS_1094 941064 forward nd [RS-EPT-CBR] [1]
  promoter TSS_1095 941073 forward nd [RS-EPT-CBR] [1]
  promoter TSS_1096 942273 forward nd [RS-EPT-CBR] [1]
  promoter TSS_1097 942295 forward nd [RS-EPT-CBR] [1]
  promoter TSS_1098 (cluster) 943010 forward nd [RS-EPT-CBR] [1]


Evidence    

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



Reference(s)    

 [1] 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.


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