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Review
. 2007 Nov;75(11):5079-84.
doi: 10.1128/IAI.00525-07. Epub 2007 Jul 23.

MARTX, multifunctional autoprocessing repeats-in-toxin toxins

Karla J Fullner Satchell  1
Affiliations
Review

MARTX, multifunctional autoprocessing repeats-in-toxin toxins

Karla J Fullner Satchell. Infect Immun. 2007 Nov.
No abstract available

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Figures

FIG. 1.
FIG. 1.
A and C repeats of MARTXVc. Repeats were aligned using MacVector 7.0 (Oxford Molecular Group). Residues that align with the consensus are dark gray, while conserved residues are light gray. The consensus sequence is shown below the repeats, where x is any amino acid. The 9-aa RTX repeat is in the consensus sequence of the C repeat as indicated. Residues that form the core motif G-7X-GXXN are underlined in the consensus sequence.
FIG. 2.
FIG. 2.
Representative MARTXVc toxin is similar to MARTXVv and 10 other putative MARTX toxins. The red regions are highly conserved among the nine MARTX toxins shown; this includes but is not limited to the repeat regions (indicated by vertical lines) labeled at the top as A1, A2, B repeats, and C repeats as described in the text. The central activity domains for each toxin are color coded as indicated at the bottom, where abbreviations for genes with known or proposed functions as defined in text and domains with unknown functions (DUF) are also indicated. Genes were identified using PSI-BLAST (1), followed by analysis of independent protein sequences downloaded from the National Center for Biotechnology Information database, with the following accession numbers: V. cholerae N16961 (Vc), AAD21057.1 (16b); V. cholerae RC385 (VR), NP_937086.1; V. vulnificus YJ016 (Vv), NP_937086.1 (6a); V. splendidus 12B01 (Vs), ZP_00989505; A. hydrophila subsp. hydrophila ATCC 7966 (Ah), YP_855898 (29a); Y. enterocolitica type 0:3 (Ye), CAJ90394; and P. luminescens subsp. laumondii TT (Pl1 and Pl2-4), NP_928648, NP_928647, NP_930444, and NP_930545 (12). The sequences of Xenorhabdus bovienii (Xb) and Xenorhabdus nematophila ATCC 19061 (Xn) were downloaded from www.xenorhabdus.org (16a), and a comparative analysis was performed using BLAST2 (33a). Diagrams were drawn to scale using MacVector 7.0 (Oxford Molecular Group).
FIG. 3.
FIG. 3.
Generalized organization of rtx gene clusters, except for Y. enterocolitica and P. luminescens as noted in the text. The operon structure as drawn is modified from reference , with the gene designations for the left-oriented rtxHCA operon based on the annotation of Y. enterocolitica rtx genes (NCBI, accession number CAJ90394) and the gene designations for the right-oriented rtxBDE operon previously proposed for V. cholerae and V. vulnificus rtx genes (modified from reference 5; 21).
FIG. 4.
FIG. 4.
Comprehensive model for delivery of MARTX toxin activity domains as detailed in the text.
See this image and copyright information in PMC

References

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