Alignment and domains of M. tuberculosis H37Rv PG remodelling enzymes. Domain architecture is based on output from InterScanPro. All enzymes depicted are the M. tuberculosis H37Rv homologues. Amino acid sequences are grouped according to their common domains, as indicated by their colors: Rpf domains [yellow], PBPs [orange], endopeptidases [pink], LD-transpeptidases [green] and amidases [blue]. PonA proteins are grouped with PBPs. PFAM domains are annotated as follows: PF06737 Transglycosylase-like domain, PF00905 PBP transpeptidases domain, PF00912 Transglycosylase domain, PF00768 D-alanyl-D-alanine Carboxypeptidase domain, PF02113 D-Ala-D-Ala carboxypeptidase 3 (S13) family domain, PF00877 NlpC/P60 family domain, PF03734 L,D-transpeptidase catalytic domain, PF01520 N-acetylmuramoyl-L-alanine amidase amidase_3 domain, PF01510 N-acetylmuramoyl-L-alanine amidase amidase_2 domain. N-terminal signal sequence or transmembrane domains are displayed as purple and pink, respectively. Additional domains annotated at PFAM are as follows (in grey): PonA2, PF03793, PASTA domain; PbpB, PF03717, PBP dimerization domain; PBP-lipo, PF05223, NTF2-like N-terminal transpeptidase; Ami2, PF01471, Peptidoglycan-binding like; RpfB, PF03990, Domain of unknown function DUF348; RpfB, PF07501, G5 domain. Rv3627c retains two tandem copies of the PF02113 D-Ala-D-Ala carboxypeptidase 3 (S13) family domain, one of which is contracted. Figure not to scale.
Machowski et al. BMC Microbiology 2014 14:75 doi:10.1186/1471-2180-14-75