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Fig. 1 | BMC Microbiology

Fig. 1

From: Enterococcus hirae LcpA (Psr), a new peptidoglycan-binding protein localized at the division site

Fig. 1

a Genetic organization of the 3 lcp gene loci in the genome of E. hirae ATCC 9790. Dark shaded arrows represent the lcp genes. The psr gene is here renamed lcpA and takes place between ftsW and pbp5 genes. Other genes are annotated as: nitrilotriacetate monooxygenase component B (EHR_11435); major facilitator superfamily permease (EHR_11455); hypothetical protein (EHR_11985); topoisomerase IA (EHR_11990); shikimate 5-dehydrogenase (EHR_12010); ABC transporter ATP-binding protein (EHR_12015); chitinase B (EHR_14355); tspO protein (EHR_14360); UDP-N-acetylmuramyl pentapeptide synthase (EHR_14370); hypothetical protein (EHR_14375). Annotation follows NCBI available sequence data for E. hirae ATCC 9790. b Predicted domains of E. hirae LCP proteins. The membrane topology was predicted for each LCP proteins with the TMHMM Server v.2.0. The LCP domains were predicted using the pfam03816 consensus sequence. c Phylogenetic tree, based on the multiple alignment of LCP proteins from E. hirae, B. subtilis and S. aureus, showing the relatedness of LCP proteins from these firmicutes bacteria. The tree was calculated with Clustal W. d Alignment of the LytR-CpsA-Psr domains of LCP proteins from E. hirae, B. subtilis and S. aureus. Full length sequences were aligned using Clustal W and formatted with ESPript, only the LCP domain as defined in the PFAM database (pfam03816) is shown. The red color is depending on the identity of residues. The white color on a red background denotes strictly conserved residues. A consensus sequence based on the aligned sequences is shown in the lower row. From the consensus sequence, the following pattern has beed deduced R-X-D-X(20)-R-D-X(91,103)-R-X-R-X(4,7)-D-X(2)-R-X(2)-R-Q (Prosite syntax). These residues are highly conserved in LCP proteins and, in known LCP 3D-structures, their side-chains are spatially close, most of them being involved in the binding of the pyro-phosphate lipid [28] (for more details see Additional file 1: S2)

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