RegulonDB RegulonDB 10.8: Gene Form
   

aspS gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

aspS yecD nudB yecE terminator anti-terminator anti-anti-terminator TSS_2220 TSS_2220 yecDp4 yecDp4 yecDp7 yecDp7 aspSp1 aspSp1 yecDp8 yecDp8 aspSp aspSp TSS_2218 TSS_2218 TSS_2217 TSS_2217 TSS_2216 (cluster) TSS_2216 (cluster) TSS_2215 TSS_2215 TSS_2214 TSS_2214 nudBp nudBp TSS_2213 TSS_2213 TSS_2212 TSS_2212 yebCp yebCp

Gene      
Name: aspS    Texpresso search in the literature
Synonym(s): ECK1867, EG10097, b1866, tls
Genome position(nucleotides): 1948750 <-- 1950522 Genome Browser
Strand: reverse
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
53.75
External database links:  
ASAP:
ABE-0006226
CGSC:
32508
ECHOBASE:
EB0095
MIM:
611105
OU-MICROARRAY:
b1866
PortEco:
aspS
STRING:
511145.b1866
COLOMBOS: aspS


Product      
Name: aspartate—tRNA ligase
Synonym(s): AspRS, AspS, Tls
Sequence: Get amino acid sequence Fasta Format
Cellular location: cytosol
Molecular weight: 65.913
Isoelectric point: 5.359
Motif(s):
 
Type Positions Sequence
195 -> 198 QLFK
118 -> 558 EEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLAYIKVNERAKGLEGINSPVAKFLNAEIIEDILDRTAAQDGDMIFFGADNKKIVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMTAAELKAAPENAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTT
307 -> 406 FAGPANDPKGRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLAYIKVNERAKGLEGINSPVAKFLNAEIIEDILDRTAAQDGDMIFFGADNKKIVADAM
18 -> 102 VTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDEKNINRDMATGEIEVLASSLTII
217 -> 219 RDE

 

Classification:
Multifun Terms (GenProtEC)  
  2 - information transfer --> 2.3 - protein related --> 2.3.1 - amino acid -activation
Gene Ontology Terms (GO)  
cellular_component GO:0005737 - cytoplasm
GO:0005829 - cytosol
molecular_function GO:0003676 - nucleic acid binding
GO:0016874 - ligase activity
GO:0004812 - aminoacyl-tRNA ligase activity
GO:0004815 - aspartate-tRNA ligase activity
GO:0000166 - nucleotide binding
GO:0005524 - ATP binding
biological_process GO:0006412 - translation
GO:0006418 - tRNA aminoacylation for protein translation
GO:0006422 - aspartyl-tRNA aminoacylation
Note(s): Note(s): ...[more].
Reference(s): [1] Akesson B., et al., 1978
[2] Neuenfeldt A., et al., 2013
External database links:  
DIP:
DIP-9182N
ECOCYC:
ASPS-MONOMER
ECOLIWIKI:
b1866
INTERPRO:
IPR004365
INTERPRO:
IPR029351
INTERPRO:
IPR012340
INTERPRO:
IPR006195
INTERPRO:
IPR004524
INTERPRO:
IPR004364
INTERPRO:
IPR004115
INTERPRO:
IPR002312
MINT:
MINT-1249167
MODBASE:
P21889
PANTHER:
PTHR22594:SF5
PDB:
1C0A
PDB:
1EQR
PDB:
1IL2
PFAM:
PF01336
PFAM:
PF02938
PFAM:
PF00152
PRIDE:
P21889
PRINTS:
PR01042
PRODB:
PRO_000022173
PROSITE:
PS50862
REFSEQ:
NP_416380
SMR:
P21889
UNIPROT:
P21889


Operon      
Name: aspS         
Operon arrangement:
Transcription unit        Promoter
aspS
aspS


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_2212 1948376 reverse nd [RS-EPT-CBR] [3]
  promoter TSS_2213 1948462 reverse nd [RS-EPT-CBR] [3]
  promoter TSS_2214 1949007 reverse nd [RS-EPT-CBR] [3]
  promoter TSS_2215 1949515 reverse nd [RS-EPT-CBR] [3]
  promoter TSS_2216 (cluster) 1950222 reverse For this promoter, there
Read more >
[RS-EPT-CBR] [3]
  promoter TSS_2217 1950276 reverse nd [RS-EPT-CBR] [3]
  promoter TSS_2218 1950278 reverse nd [RS-EPT-CBR] [3]
  promoter yecDp8 1950636 forward Similarity to the consensus
Read more >
[ICWHO] [4]
  promoter yecDp7 1950760 forward Similarity to the consensus
Read more >
[ICWHO] [4]
  promoter yecDp4 1950778 forward Similarity to the consensus
Read more >
[ICWHO] [4]
  promoter TSS_2220 1950822 reverse nd [RS-EPT-CBR] [3]


Evidence    

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

 [ICWHO] Inferred computationally without human oversight



Reference(s)    

 [1] Akesson B., Lundvik L., 1978, Simultaneous purification and some properties of aspartate: tRNA ligase and seven other amino-acid:tRNA ligases from Escherichia coli., Eur J Biochem 83(1):29-36

 [2] Neuenfeldt A., Lorber B., Ennifar E., Gaudry A., Sauter C., Sissler M., Florentz C., 2013, Thermodynamic properties distinguish human mitochondrial aspartyl-tRNA synthetase from bacterial homolog with same 3D architecture., Nucleic Acids Res 41(4):2698-708

 [3] 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.

 [4] 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


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