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1.
Fig. 5

Fig. 5. From: Comparative genomics and evolution of the amylase-binding proteins of oral streptococci.

RAxML tree of AbpA subgroups using CLUSTAL W functional regions alignment

Elaine M. Haase, et al. BMC Microbiol. 2017;17:94.
2.
Fig. 3

Fig. 3. From: Comparative genomics and evolution of the amylase-binding proteins of oral streptococci.

Schematic of AbpA-like proteins. a Signal sequence; b N-terminal regions for subgroups 1–5; c variable region; d sortase B-binding motif; and (e) termination codon

Elaine M. Haase, et al. BMC Microbiol. 2017;17:94.
3.
Fig. 2

Fig. 2. From: Comparative genomics and evolution of the amylase-binding proteins of oral streptococci.

CLUSTAL Omega alignment of functional regions from AbpA-like protein sequences. Similarity in signal sequence (blue), sortase-binding motif (violet) and termination codon (orange). Subgroup (1 to 5) differentiation is based on the N-terminal sequence (red)

Elaine M. Haase, et al. BMC Microbiol. 2017;17:94.
4.
Fig. 1

Fig. 1. From: Comparative genomics and evolution of the amylase-binding proteins of oral streptococci.

Composite of (a) Coomassie-stained gels and (b) blots from the amylase-ligand overlay assay. a Boxes represent protein bands cut out from the Coomassie-stained blot for N-terminal sequencing. b AbpA-like, red boxes; AbpB-like, blue boxes; Novel ABPs, green boxes; Indeterminant, black boxes. Summary of ABPs are listed in Table

Elaine M. Haase, et al. BMC Microbiol. 2017;17:94.
5.
Fig. 4

Fig. 4. From: Comparative genomics and evolution of the amylase-binding proteins of oral streptococci.

Sequence similarity network of all ABPs. a At low stringency, amylase-binding proteins cluster into six families: AbpA (red), AbpB (yellow) and Abp Novel (blue). At high stringency, AbpA separates into two interrelated subfamilies. b Sequence similarity network of AbpA subgroups at high stringency. Each AbpA is color-coded according to its classification into one of the five subgroups defined by the N-terminal sequence, a putative amylase-binding motif

Elaine M. Haase, et al. BMC Microbiol. 2017;17:94.
6.
Fig. 7

Fig. 7. From: Comparative genomics and evolution of the amylase-binding proteins of oral streptococci.

Tertiary protein structure of representative AbpA sequences. N-terminal half of AbpA is predominated by helical spatial arrangement and the C-terminal half is largely coiled. NMR structure of S. gordonii CH1 is in red and the predicted structures for representative sequences are coded in various colors (Green-Subgroup1-WP_008810020.1; Yellow-Subgroup2-WP_005591359.1; Purple-Subgroup3-WP_002886387.1; Blue-Subgroup4-WP_033629133.1; Orange-Subgroup5-WP_003092326.1)

Elaine M. Haase, et al. BMC Microbiol. 2017;17:94.
7.
Fig. 6

Fig. 6. From: Comparative genomics and evolution of the amylase-binding proteins of oral streptococci.

Synteny mapping of abpA-srtB. S. cristatus AS1.3089 did not carry the abpA-srtB locus. ORFs flanking the abpA-srtB locus were deduced from genome sequences available at NCBI. All strains except S. cristatus AS1.3089, S. vestibularis F0396, and G. haemolysans M341 have been tested in vitro for the ability to bind amylase. Flanking genes include: (1) ribose-phosphate pyrophosphokinase; (2) aminotransferase; (3) haloacid dehalogenase; (4) MFS transporter; (5) peptidase M42; (6) peptidase; (7) DNA-binding transcriptional regulator, XRE-family; (8) metallophosphatase; (9) CoA-binding protein; and (10) IS200/IS605 family transposase. A in silico evidence only

Elaine M. Haase, et al. BMC Microbiol. 2017;17:94.

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