RegulonDB RegulonDB 11.0: Gene Form
   

bamE gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

recN bamE yfjF ratA NsrR CpxR TSS_2970 TSS_2970 TSS_2969 TSS_2969 TSS_2968 TSS_2968 TSS_2967 TSS_2967 TSS_2966 TSS_2966 TSS_2965 TSS_2965 bamEp bamEp TSS_2964 TSS_2964

Gene      
Name: bamE    Texpresso search in the literature
Synonym(s): ECK2613, EG10952, b2617, smpA, smqA
Genome position(nucleotides): 2753605 --> 2753946
Strand: forward
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
 49.42
External database links:  
ASAP:
 ABE-0008614
ECHOBASE:
 EB0945
ECOLIHUB:
 smpA
OU-MICROARRAY:
 b2617
STRING:
 511145.b2617
COLOMBOS: bamE


Product      
Name: outer membrane protein assembly factor BamE
Synonym(s): BamE, SmpA, SmqA, small membrane protein A
Sequence: Get amino acid sequence Fasta Format
Cellular location: outer membrane
Molecular weight: 12.302
Isoelectric point: 8.726
Motif(s):
 
Type Positions Sequence Comment
1 -> 19 MRCKTLTAAAAVLLMLTAG
20 -> 20 C C → G; functionally critical mutation (results in increased sensitivity to vancomycin)
32 -> 32 I I → G; functionally critical mutation (results in increased sensitivity to vancomycin)
34 -> 34 Q Q → G or C; functionally critical mutation (results in increased sensitivity to vancomycin)
35 -> 35 G G → C; functionally critical mutation 9results in increased sensitivity to vancomycin)

 
Classification:
Multifun Terms (GenProtEC)  
  6 - cell structure --> 6.1 - membrane
Gene Ontology Terms (GO)  
cellular_component GO:0009279 - cell outer membrane
GO:0019867 - outer membrane
GO:0016020 - membrane
GO:1990063 - Bam protein complex
molecular_function GO:1901612 - cardiolipin binding
GO:0005515 - protein binding
GO:0030674 - protein-macromolecule adaptor activity
GO:0042802 - identical protein binding
biological_process GO:0046677 - response to antibiotic
GO:0043165 - Gram-negative-bacterium-type cell outer membrane assembly
GO:0051205 - protein insertion into membrane
Note(s): Note(s): ...[more].
Evidence: [APPH] Assay of protein purified to homogeneity
[IHBCE] Inferred by a human based on computational evidence
[IPI] Inferred from physical interaction
Reference(s): [1] Han L., et al., 2016
[2] Hart EM., et al., 2019
[3] Miczak A., et al., 1991
[4] Rao S., et al., 2020
[5] Sabina J., et al., 2003
[6] Sklar JG., et al., 2007
[7] Tata M., et al., 2019
[8] Wei Y., et al., 2001
External database links:  
ALPHAFOLD:
 P0A937
DIP:
 DIP-10895N
ECOCYC:
 EG10952-MONOMER
ECOLIWIKI:
 b2617
INTERPRO:
 IPR026592
INTERPRO:
 IPR037873
INTERPRO:
 IPR007450
MINT:
 P0A937
PANTHER:
 PTHR37482
PDB:
 5AYW
PDB:
 5D0O
PDB:
 5D0Q
PDB:
 5EKQ
PDB:
 5LJO
PDB:
 6LYQ
PDB:
 6LYR
PDB:
 6LYS
PDB:
 6LYU
PDB:
 6SN9
PDB:
 6V05
PDB:
 2YH9
PDB:
 2KXX
PDB:
 2KM7
PFAM:
 PF04355
PRIDE:
 P0A937
PROSITE:
 PS51257
REFSEQ:
 NP_417107
SMR:
 P0A937
UNIPROT:
 P0A937


Operon      
Name: bamE         
Operon arrangement:
Transcription unit        Promoter
bamE


Transcriptional Regulation      
Display Regulation             
Repressed by: NsrR, CpxR


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_2964 2752658 reverse nd [RS-EPT-CBR] [9]
  promoter TSS_2965 2753488 forward nd [RS-EPT-CBR] [9]
  promoter TSS_2966 2753555 forward nd [RS-EPT-CBR] [9]
  promoter TSS_2967 2753588 forward nd [RS-EPT-CBR] [9]
  promoter TSS_2968 2753594 forward nd [RS-EPT-CBR] [9]
  promoter TSS_2969 2753599 forward nd [RS-EPT-CBR] [9]
  promoter TSS_2970 2753605 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] Han L., Zheng J., Wang Y., Yang X., Liu Y., Sun C., Cao B., Zhou H., Ni D., Lou J., Zhao Y., Huang Y., 2016, Structure of the BAM complex and its implications for biogenesis of outer-membrane proteins., Nat Struct Mol Biol 23(3):192-6

 [2] Hart EM., Gupta M., Wuhr M., Silhavy TJ., 2019, The Synthetic Phenotype of Δ bamB Δ bamE Double Mutants Results from a Lethal Jamming of the Bam Complex by the Lipoprotein RcsF., MBio 10(3)

 [3] Miczak A., Chauhan AK., Apirion D., 1991, Two new genes located between 2758 and 2761 kilobase pairs on the Escherichia coli genome., J Bacteriol 173(11):3271-2

 [4] Rao S., Bates GT., Matthews CR., Newport TD., Vickery ON., Stansfeld PJ., 2020, Characterizing Membrane Association and Periplasmic Transfer of Bacterial Lipoproteins through Molecular Dynamics Simulations., Structure 28(4):475-487.e3

 [5] Sabina J., Dover N., Templeton LJ., Smulski DR., Soll D., LaRossa RA., 2003, Interfering with different steps of protein synthesis explored by transcriptional profiling of Escherichia coli K-12., J Bacteriol 185(20):6158-70

 [6] Sklar JG., Wu T., Gronenberg LS., Malinverni JC., Kahne D., Silhavy TJ., 2007, Lipoprotein SmpA is a component of the YaeT complex that assembles outer membrane proteins in Escherichia coli., Proc Natl Acad Sci U S A 104(15):6400-5

 [7] Tata M., Konovalova A., 2019, Improper Coordination of BamA and BamD Results in Bam Complex Jamming by a Lipoprotein Substrate., MBio 10(3)

 [8] Wei Y., Lee JM., Richmond C., Blattner FR., Rafalski JA., LaRossa RA., 2001, High-density microarray-mediated gene expression profiling of Escherichia coli., J Bacteriol 183(2):545-56

 [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.

RegulonDB