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Fig. 2 | BMC Microbiology

Fig. 2

From: Purification and partial characterization of LdtP, a cell envelope modifying enzyme in Liberibacter asiaticus

Fig. 2

Conserved domains, sequence alignment, and structure of LdtP. a The domain arrangement of LdtP according to the NCBI Conserved Domain Database. b A partial sequence alignment covering the L,D-transpeptidase catalytic domain (pfam03734) of LdtP and homologous L,D-transpeptidase proteins identified by PSI-Blast. Identical residues are colored white with a red background; columns with higher than 70% equivalent residues considering physico-chemical properties are boxed and colored red with a white background; catalytic residues are denoted by blue arrows; the conserved motif, HXX14–17[S/T]HGChN, is boxed in purple. Abbreviations (accession numbers): L.a._LdtP, Liberibacter asiaticus, (ACT56823); L.s._CKC_02390, Liberibacter solancearum (ADR52227); L.c._B488_10900, Liberibacter crescens (AGA65082); S.m._SMc01769, Sinorhizobium meliloti (NP_385313); C.s._Ga0061061_11165, Chelatococcus sambhunathii (CUA90119); P.i._Ga0061067_11813, Pannonibacter indicus (CUB00332); L.a._LA5094_04658, Labrenzia alba (CTQ61876); M.s._MSIL_RS10785, Methylocella silvestris (ACK51051); E.c._YcbB, Escherichia coli (NP_415445). The figure was made using the web server ESPript [47]. c A three-dimensional model of LdtP (residues 98–356) predicted by PHYRE2 based on LdtMt1 from Mycobacterium tuberculosis (PDB:4JMX) as the template. Yellow, imipenem; blue, binding pocket; red, catalytic residues (labeled)

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