PROSITE documentation PDOC50936EngC GTPase domain profile
GTPases function as crucial molecular switches in a broad variety of biochemical processes. The majority of GTPases form a vast class of evolutionarily related proteins within the superclass of P-loop-containing ATPases (see <PDOC00017>). The P-loop GTPases share a conserved amino acid sequence G1-G3-G4 motif pattern (G2 is a less conserved motif found only in some GTPases) present in the GTPase domain. The Escherichia coli protein engC represents a protein family whose members are broadly conserved in bacteria and have been shown to be indispensable to the growth of E. coli and Bacillus subtilis. The engC protein is an unusual, circularly permuted GTPase that catalyzes rapid hydrolysis of GTP with comparatively slow catalytic turnover. The GTPase domain of engC is highly similar to several P-loop GTPases, but has an altered connectivity of the structural elements and associated conserved motifs relative to the typical P-loop-containing GTPase domain. Specifically, engC and its orthologs have a circular permutation of the GTPase structure described by a G4-G1-G3 pattern [1]. The engC type GTPase domain is predominantly bacterial, with probable acquisition by plants from chloroplasts [2].
The profile we developed covers the entire engC type GTPase domain.
Last update:October 2003 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Daigle D.M. Rossi L. Berghuis A.M. Aravind L. Koonin E.V. Brown E.D. |
| Title | YjeQ, an essential, conserved, uncharacterized protein from Escherichia coli, is an unusual GTPase with circularly permuted G-motifs and marked burst kinetics. | |
| Source | Biochemistry 41:11109-11117(2002). | |
| PubMed ID | 12220175 | |
| DOI | 10.1021/bi020355q |
| 2 | Authors | Leipe D.D. Wolf Y.I. Koonin E.V. Aravind L. |
| Title | Classification and evolution of P-loop GTPases and related ATPases. | |
| Source | J. Mol. Biol. 317:41-72(2002). | |
| PubMed ID | 11916378 | |
| DOI | 10.1006/jmbi.2001.5378 |
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