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. 2002 Apr;68(4):1837–1845. doi: 10.1128/AEM.68.4.1837-1845.2002

FIG. 2.

FIG. 2.

(A) Partial sequence alignment of the P21 protein of A. ferrooxidans with those of representative sulfurtransferases. The active site and two conserved structural motifs, designated CH2A and CH2B, are labeled. A consensus is indicated in which the active site presents a cysteine conserved in all of the sequences shown. Rhod-Bt, bovine liver rhodanese; MPST-Rn, rat mercaptopyruvate sulfurtransferase; Sud-Ws, sulfide dehydrogenase from W. succinogenes; GlpE-Ec, E. coli rhodanese-like protein; P21-Atf, putative periplasmic rhodanese-like protein P21 from A. ferrooxidans. (B) Sequence alignment of A. ferrooxidans proteins with similarity to rhodaneses. The P21 protein sequence contains a 28-amino-acid leader peptide. Within this leader peptide, indicated by the numbered lines above, are the following: the positively charged residues at the N terminus (line 1), a stretch of hydrophobic residues (line 2), a glycyl residue at the end of this stretch (line 3), and a consensus cleavage sequence (Ala/Gly/Ser)-X-(Ala/Gly/Ser) (line 4). The arrow indicates the site where the cleavage of the leader peptide would occur. P14-Atf, putative cytoplasmic rhodanese-like from A. ferrooxidans; P16-Atf, putative cytoplasmic rhodanase-like from A. ferrooxidans. The underlined sequence in P21-Atf indicates a putative cysteine motif known to bind iron-sulfur clusters. Accession numbers: Sud, X81642; Rhod-Bt, M58561; MPST-Rn, D50564; GlpE-Ec, M96795; P21-Atf, AJ312238; and P14-Atf and P16-Atf, derived from the genome sequence of A. ferrooxidans 23270.