RegulonDB RegulonDB 10.8: Gene Form
   

pbpG gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

dld pbpG yohC terminator pbpGp5 pbpGp5 pbpGp7 pbpGp7 TSS_2451 TSS_2451

Gene      
Name: pbpG    Texpresso search in the literature
Synonym(s): ECK2127, EG12015, b2134, yohB
Genome position(nucleotides): 2223938 <-- 2224870 Genome Browser
Strand: reverse
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
50.7
External database links:  
ASAP:
ABE-0007050
CGSC:
36349
ECHOBASE:
EB1952
OU-MICROARRAY:
b2134
PortEco:
pbpG
STRING:
511145.b2134
COLOMBOS: pbpG


Product      
Name: peptidoglycan DD-endopeptidase PbpG
Synonym(s): PBP7, PBP8, PbpG, YohB, penicillin-binding protein 7
Sequence: Get amino acid sequence Fasta Format
Cellular location: periplasmic space
Molecular weight: 33.887
Isoelectric point: 10.526
Motif(s):
 
Type Positions Sequence
26 -> 310 KTAAATTASQPEIASGSAMIVDLNTNKVIYSNHPDLVRPIASISKLMTAMVVLDARLPLDEKLKVDISQTPEMKGVYSRVRLNSEISRKDMLLLALMSSENRAAASLAHHYPGGYKAFIKAMNAKAKSLGMNNTRFVEPTGLSVHNVSTARDLTKLLIASKQYPLIGQLSTTREDMATFSNPTYTLPFRNTNHLVYRDNWNIQLTKTGFTNAAGHCLVMRTVINNKPVALVVMDAFGKYTHFADASRLRTWIETGKVMPVPAAALSYKKQKAAQMAAAGQTAQND
30 -> 261 ATTASQPEIASGSAMIVDLNTNKVIYSNHPDLVRPIASISKLMTAMVVLDARLPLDEKLKVDISQTPEMKGVYSRVRLNSEISRKDMLLLALMSSENRAAASLAHHYPGGYKAFIKAMNAKAKSLGMNNTRFVEPTGLSVHNVSTARDLTKLLIASKQYPLIGQLSTTREDMATFSNPTYTLPFRNTNHLVYRDNWNIQLTKTGFTNAAGHCLVMRTVINNKPVALVVMDAF
1 -> 25 MPKFRVSLFSLALMLAVPFAPQAVA

 

Classification:
Multifun Terms (GenProtEC)  
  1 - metabolism --> 1.6 - biosynthesis of macromolecules (cellular constituents) --> 1.6.7 - murein (peptidoglycan)
  5 - cell processes --> 5.1 - cell division
  5 - cell processes --> 5.6 - protection --> 5.6.4 - drug resistance/sensitivity
  6 - cell structure --> 6.2 - murein
Gene Ontology Terms (GO)  
cellular_component GO:0030288 - outer membrane-bounded periplasmic space
GO:0042597 - periplasmic space
molecular_function GO:0005515 - protein binding
GO:0016787 - hydrolase activity
GO:0004175 - endopeptidase activity
GO:0009002 - serine-type D-Ala-D-Ala carboxypeptidase activity
biological_process GO:0000270 - peptidoglycan metabolic process
GO:0006508 - proteolysis
GO:0009252 - peptidoglycan biosynthetic process
GO:0042493 - response to drug
GO:0043093 - FtsZ-dependent cytokinesis
GO:0008360 - regulation of cell shape
GO:0071555 - cell wall organization
Note(s): Note(s): ...[more].
Evidence: [APPH] Assay of protein purified to homogeneity
Reference(s): [1] Denome SA., et al., 1999
[2] Fischer E. 1989
[3] Henderson TA., et al., 1997
[4] Jacoby GH., et al., 1988
[5] Leidenix MJ., et al., 1989
[6] Romeis T., et al., 1994
[7] Satta G., et al., 1995
External database links:  
DIP:
DIP-48108N
ECOCYC:
EG12015-MONOMER
ECOLIWIKI:
b2134
INTERPRO:
IPR018044
INTERPRO:
IPR012338
INTERPRO:
IPR001967
MODBASE:
P0AFI5
PFAM:
PF00768
PRIDE:
P0AFI5
PRINTS:
PR00725
PRODB:
PRO_000023497
REFSEQ:
NP_416638
SMR:
P0AFI5
UNIPROT:
P0AFI5


Operon      
Name: pbpG         
Operon arrangement:
Transcription unit        Promoter
 


RNA cis-regulatory element    
Attenuation: Translational


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_2451 2223795 forward nd [RS-EPT-CBR] [8]
  promoter pbpGp7 2224941 reverse Similarity to the consensus
Read more >
[ICWHO] [9]
  promoter pbpGp5 2225066 reverse Similarity to the consensus
Read more >
[ICWHO] [9]


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] Denome SA., Elf PK., Henderson TA., Nelson DE., Young KD., 1999, Escherichia coli mutants lacking all possible combinations of eight penicillin binding proteins: viability, characteristics, and implications for peptidoglycan synthesis., J Bacteriol 181(13):3981-93

 [2] Fischer E., 1989, Osmolability of Escherichia coli and modification of [125I]ampicillin-binding by competence induction for uptake of transforming DNA., Arch Microbiol 153(1):43-6

 [3] Henderson TA., Young KD., Denome SA., Elf PK., 1997, AmpC and AmpH, proteins related to the class C beta-lactamases, bind penicillin and contribute to the normal morphology of Escherichia coli., J Bacteriol 179(19):6112-21

 [4] Jacoby GH., Young KD., 1988, Unequal distribution of penicillin-binding proteins among inner membrane vesicles of Escherichia coli., J Bacteriol 170(8):3660-7

 [5] Leidenix MJ., Jacoby GH., Henderson TA., Young KD., 1989, Separation of Escherichia coli penicillin-binding proteins into different membrane vesicles by agarose electrophoresis and sizing chromatography., J Bacteriol 171(10):5680-6

 [6] Romeis T., Holtje JV., 1994, Specific interaction of penicillin-binding proteins 3 and 7/8 with soluble lytic transglycosylase in Escherichia coli., J Biol Chem 269(34):21603-7

 [7] Satta G., Cornaglia G., Mazzariol A., Golini G., Valisena S., Fontana R., 1995, Target for bacteriostatic and bactericidal activities of beta-lactam antibiotics against Escherichia coli resides in different penicillin-binding proteins., Antimicrob Agents Chemother 39(4):812-8

 [8] 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.

 [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


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