Microbiology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Abstract
Right arrow Full Text
Services
Right arrow Email this article to a friend
Right arrow Alert me to new issues of the journal
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via CrossRef

The predicted secretome of Lactobacillus plantarum WCFS1 sheds light on interactions with its environment, by J. Boekhorst, M. Wels, M. Kleerebezem and R. J. Siezen

Microbiology vol. 152, part 11, pp. 3175 - 3183

Fig. S1. Multiple sequence alignment of Repeat_5. Residues were coloured using the default ClustalX colouring scheme: conserved A, C, F, H, I, L, M, V, W,Y or P residues are coloured blue, while conserved S or T residues are in green. Conserved positively charged residues and negatively charged residues are coloured red and magenta, respectively. Exact details can be found in the ClustalX manual (Thompson et al., 1997; see main paper for reference details). The number following the locus tags indicate the start position of the domain in the complete protein sequence.

Alignment of Repeat_5

Fig. S2. Multiple sequence alignment of the WY domain and the transglycosylase-like domain from the PFAM database (PF06737). Residues were coloured using the default ClustalX colouring scheme: conserved A, C, F, H, I, L, M, V, W, Y or P residues are coloured blue, while columns with conserved S or T residues are in green. Conserved positively charged residues and negatively charged residues are coloured red and magenta, respectively. Exact details can be found in the ClustalX manual (Thompson et al., 1997). An asterisk indicates the conserved Glu residue.

Alignment of WY domain and PF06737

Fig. S3. Multiple sequence alignment of the CSH domain. Residues were coloured using the default ClustalX colouring scheme: conserved A, C, F, H, I, L, M,V,W,Y or P residues are coloured blue, while columns with conserved S or T residues are in green. Conserved positively charged residues and negatively charged residues are coloured red and magenta, respectively. Exact details can be found in the ClustalX manual (Thompson et al., 1997).The numbers following the locus tags indicate the start position of the domain in the complete protein sequence. Asterisks indicate the conserved catalytic residues Ser, Asp and His of these alpha/beta hydrolases.

Alignment of CSH domain

Supplementary tables. Table S1 lists all proteins predicted to be extracellular, Tables S2-S13 list proteins classified by function and anchor type, Tables S14-S17 list identified PFAM domains, and Table S18 lists groups of genes with similar phylogenetic distributions. [Excel file] (102 kb)


REFERENCE
Thompson, J. D., Gibson, T. J., Plewniak, F., Jeanmougin, F. & Higgins, D. G. (1997). The CLUSTAL_X Windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 25, 4876-4882.







This Article
Right arrow Abstract
Right arrow Full Text
Services
Right arrow Email this article to a friend
Right arrow Alert me to new issues of the journal
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via CrossRef


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 2009 Society for General Microbiology.