GenePage for the cobB gene of Escherichia coli K-12

Primary Gene Name: cobB
EcoGene Accession Number: EG13443
K-12 Gene Accession Number: ECK1106
MG1655 Gene Identifier: b1120
Gene Name Mnemonic: Cobalamin, coenzyme B12
Alternate Gene Symbols: npdA; ycfY
Description: Protein lysine deacetylase, NAD(+)-dependent; chemotaxis regulator; protein lysine desuccinylase; sirituin homolog
  # bp Upstream # bp Downstream
MW: 26716.38 ---------242 aa Pre-Run BlastP UniProt
Pre-Run BlastP NR+Env
Left End: 1179631
Left Intergenic Region

Name: nagK_cobB

Length: 126 bp gap

Orientation: Codirectional+

Left_end: 1179505

Right_end: 1179630

Centisome: 25.41

Genomic Address
Clockwise
Minute or Centisome (%) = 25.41
Right End: 1180359
Right Intergenic Region

Name: cobB_ycfZ

Length: 119 bp gap

Orientation: Convergent

Left_end: 1180360

Right_end: 1180478

Centisome: 25.43

In addition to its activity as a protein lysine deacetylase, CobB has protein lysine desuccinylase activity (Colak, 2013). NhoA is acetylated at Lys214 and at the C-terminal Lys281; NhoA is deacetylated by CobB, acetylation and deacytylation affects NhoA activity (Zhang, 2013). RcsB is acetylated at Lys180 by Pka(YfiQ) in vitro blocking its ability to bind to DNA, and Lys180 is deacetylated by CobB in vitro (Thao, 2010). Acetyl CoA synthase Acs is activated by CobB-mediated deacetylation of K609 in Salmonella (Starai, 2002). E. coli CobB deacetylates the Acs K609 peptide in vitro (Zhao, 2004). Protein acetyltransferase in Salmonella inhibits acetyl CoA synthase Acs by acetylating residue K609 (Starai, 2004). More than 100 proteins have acetylated lysines in E. coli (Yu, 2008; Zhang, 2008). CobB may have a limited role in general protein lysine deacetylation since only four protein bands were changed in an E. coli cobB mutant (Zhang, 2008). cobB is named after its Salmonella ortholog and has no known cobalamin function in E. coli. CobB can deacetylate CheY in vitro and in vivo, reducing FliM binding and chemotaxis (Li, 2010). cobB is a mutational phenotypic suppressor of a cheA cheZ double mutation (Li, 2010). CobB has been reported to have a weak protein ADP-ribosyltransferase activity, although this was subsequently refuted (Frye, 1999; Landry, 2000). CobB can catalyze an NAD-nicotinamide exchange reaction, which is dependent on the presence of acetyllysine, alone or in proteins, indicative of formation of an enzyme-ADP-ribose intermediate during the NAD-dependent deacetylation reaction (Landry, 2000). The CobB start has been moved up to Met-38, removing 37 aa that are not conserved, however verification is required because the upstream start has a good RBS and might be utilized in E. coli if transcribed (Maillet, 2007).

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BamHI EcoRI HindIII