Cfrench:multidomhem

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Analysis of multi-domain proteins with putative hemerythrin-like domains

Our analysis showed a variety of large multi-domain proteins with a hemerythrin-like domain, usually at the C-terminus or N-terminus. Other domains present were generally identified by sequence comparison as being involved in signalling: mainly methyl-accepting chemotaxis proteins (MCPs), diguanylate cyclases (GGDEF domains), histidine kinase domains, CheY-like response receiver domains, and cAMP-binding domains, and in one case an apparent phosphatase domain. The most obvious interpretation is that the hemerythrin domains act as oxygen sensors, and the auxiliary domains function in signal transduction to alter the cell's state. Sequence comparisons allowed the majority of the putative multi-domain hemerythrins to be assigned to a few well defined families.

MCP-hemerythrins

These proteins contain a large N-terminal MCP-like region and a C-terminal hemerythrin-like region. The most obvious interpretation is that they function in aerotaxis. Sequence analysis shows that they fall into three groups.

Magnetospirillum/Rhodospirillum MCP-hemerythrins
Magms807 Magnetospirillum magnetotacticum MS1 Magn03010970
Magms699 Magnetospirillum magnetotacticum MS1 Magn03011185
Magam807 Magnetospirillum magneticum AMB1 amb0220
Magam665 Magnetospirillum magneticum AMB1 amb3267
Magam810 Magnetospirillum magneticum AMB1 amb3793
Magam795 Magnetospirillum magneticum AMB1 amb4156
Rhoru736 Rhodospirillum rubrum ATCC 11170 Rru_A0632

Sequence comparisons show that Magms807 and Magma807 are specific homologs, as are Magms699 and Magam810. Rhoru736 is least closely related to the others.

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