RegulonDB RegulonDB 10.8: Gene Form
   

pepN gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

pepN pncB ssuB ssuC CRP CRP NadR anti-anti-terminator anti-terminator TSS_1246 TSS_1246 TSS_1245 (cluster) TSS_1245 (cluster) pepNp pepNp TSS_1243 TSS_1243 pncBp pncBp TSS_1241 TSS_1241

Gene      
Name: pepN    Texpresso search in the literature
Synonym(s): ECK0923, EG10696, b0932
Genome position(nucleotides): 990622 --> 993234 Genome Browser
Strand: forward
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
 53.46
Reference(s): [1] Bally M., et al., 1986
[2] Bally M., et al., 1984
[3] Bally M., et al., 1984
[4] Foglino M., et al., 1986
[5] Latil M., et al., 1976
[6] McCaman MT., et al., 1986
[7] McCaman MT., et al., 1986
External database links:  
ASAP:
 ABE-0003171
CGSC:
 414
ECHOBASE:
 EB0690
OU-MICROARRAY:
 b0932
PortEco:
 pepN
STRING:
 511145.b0932
COLOMBOS: pepN


Product      
Name: aminopeptidase N
Synonym(s): alpha;-aminoacylpeptide hydrolase, PepN
Sequence: Get amino acid sequence Fasta Format
Cellular location: cytosol,inner membrane
Molecular weight: 98.919
Isoelectric point: 4.952
Motif(s):
 
Type Positions Sequence
261 -> 265 GAMEN
444 -> 545 GTPIVTVKDDYNPETEQYTLTISQRTPATPDQAEKQPLHIPFAIELYDNEGKVIPLQKGGHPVNSVLNVTQAEQTFVFDNVYFQPVPALLCEFSAPVKLEYK
76 -> 76 E
548 -> 870 DQQLTFLMRHARNDFSRWDAAQSLLATYIKLNVARHQQGQPLSLPVHVADAFRAVLLDEKIDPALAAEILTLPSVNEMAELFDIIDPIAIAEVREALTRTLATELADELLAIYNANYQSEYRVEHEDIAKRTLRNACLRFLAFGETHLADVLVSKQFHEANNMTDALAALSAAVAAQLPCRDALMQEYDDKWHQNGLVMDKWFILQATSPAANVLETVRGLLQHRSFTMSNPNRIRSLIGAFAGSNPAAFHAEDGSGYLFLVEMLTDLNSRNPQVASRLIEPLIRLKRYDAKRQEKMRAALEQLKGLENLSGDLYEKITKALA
22 -> 186 DIDLTFDLDAQKTVVTAVSQAVRHGASDAPLRLNGEDLKLVSVHINDEPWTAWKEEEGALVISNLPERFTLKIINEISPAANTALEGLYQSGDALCTQCEAEGFRHITYYLDRPDVLARFTTKIIADKIKYPFLLSNGNRVAQGELENGRHWVQWQDPFPKPCYL

 
Classification:
Multifun Terms (GenProtEC)  
  1 - metabolism --> 1.2 - degradation of macromolecules --> 1.2.3 - proteins/peptides/glycopeptides
  2 - information transfer --> 2.3 - protein related --> 2.3.6 - turnover, degradation
Gene Ontology Terms (GO)  
cellular_component GO:0005737 - cytoplasm
GO:0016020 - membrane
GO:0005886 - plasma membrane
molecular_function GO:0005515 - protein binding
GO:0008233 - peptidase activity
GO:0016787 - hydrolase activity
GO:0046872 - metal ion binding
GO:0008270 - zinc ion binding
GO:0004177 - aminopeptidase activity
GO:0008237 - metallopeptidase activity
GO:0042802 - identical protein binding
biological_process GO:0006508 - proteolysis
GO:0043171 - peptide catabolic process
Note(s): Note(s): ...[more].
Reference(s): [8] Miller CG., et al., 1978
External database links:  
DIP:
 DIP-10458N
ECOCYC:
 EG10696-MONOMER
ECOLIWIKI:
 b0932
INTERPRO:
 IPR027268
INTERPRO:
 IPR024601
INTERPRO:
 IPR014782
INTERPRO:
 IPR012779
INTERPRO:
 IPR001930
INTERPRO:
 IPR035414
INTERPRO:
 IPR037144
INTERPRO:
 IPR042097
INTERPRO:
 IPR038438
MINT:
 MINT-1310653
MODBASE:
 P04825
PANTHER:
 PTHR11533
PDB:
 4XMT
PDB:
 4XMU
PDB:
 4XMV
PDB:
 4XMW
PDB:
 4XMX
PDB:
 4XMZ
PDB:
 4XN1
PDB:
 4XN2
PDB:
 4XN4
PDB:
 4XN5
PDB:
 4XN8
PDB:
 4XN9
PDB:
 4XNA
PDB:
 4XNB
PDB:
 4XND
PDB:
 4XO3
PDB:
 4XO4
PDB:
 4XO5
PDB:
 5MFR
PDB:
 5MFS
PDB:
 5MFT
PDB:
 5YO1
PDB:
 5YQ1
PDB:
 5YQ2
PDB:
 5YQB
PDB:
 6G8B
PDB:
 4Q4I
PDB:
 4Q4E
PDB:
 3QJX
PDB:
 3PUU
PDB:
 3KED
PDB:
 3B3B
PDB:
 3B37
PDB:
 3B34
PDB:
 3B2X
PDB:
 3B2P
PDB:
 2ZXG
PDB:
 2HPT
PDB:
 2HPO
PDB:
 2DQM
PDB:
 2DQ6
PDB:
 4XN7
PFAM:
 PF11940
PFAM:
 PF17432
PFAM:
 PF01433
PRIDE:
 P04825
PRINTS:
 PR00756
PROSITE:
 PS00142
REFSEQ:
 NP_415452
SMR:
 P04825
UNIPROT:
 P04825


Operon      
Name: pepN         
Operon arrangement:
Transcription unit        Promoter
pepN


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_1241 989614 reverse nd [RS-EPT-CBR] [9]
  promoter TSS_1243 990515 forward nd [RS-EPT-CBR] [9]
  promoter TSS_1245 (cluster) 991200 forward For this promoter, there
Read more > 		[RS-EPT-CBR] [9]
  promoter TSS_1246 991492 forward nd [RS-EPT-CBR] [9]


Evidence    

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


Reference(s)    

 [1] Bally M., Foglino M., Bruschi M., Murgier M., Lazdunski A., 1986, Nucleotide sequence of the promoter and amino-terminal encoding region of the Escherichia coli pepN gene., Eur J Biochem 155(3):565-9

 [2] Bally M., Murgier M., Lazdunski A., 1984, Cloning and orientation of the gene encoding aminopeptidase N in Escherichia coli., Mol Gen Genet 195(3):507-10

 [3] Bally M., Murgier M., Tommassen J., Lazdunski A., 1984, Physical mapping of the gene for aminopeptidase N in Escherichia coli K12., Mol Gen Genet 193(1):190-1

 [4] Foglino M., Gharbi S., Lazdunski A., 1986, Nucleotide sequence of the pepN gene encoding aminopeptidase N of Escherichia coli., Gene 49(3):303-9

 [5] Latil M., Murgier M., Lazdunski A., Lazdunski C., 1976, Isolation and genetic mapping of Escherichia coli aminopeptidase mutants., Mol Gen Genet 148(1):43-7

 [6] McCaman MT., Gabe JD., 1986, Sequence of the promoter and 5' coding region of pepN, and the amino-terminus of peptidase N from Escherichia coli K-12., Mol Gen Genet 204(1):148-52

 [7] McCaman MT., Gabe JD., 1986, The nucleotide sequence of the pepN gene and its over-expression in Escherichia coli., Gene 48(1):145-53

 [8] Miller CG., Schwartz G., 1978, Peptidase-deficient mutants of Escherichia coli., J Bacteriol 135(2):603-11

 [9] 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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