{PDOC51712}
{PS51712; G_ENGA}
{BEGIN}
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* EngA-type guanine nucleotide-binding (G) domain profile *
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The P-loop  (see  <PDOC00017>)  guanosine  triphosphatases (GTPases) control a
multitude of  biological  processes, ranging from cell division, cell cycling,
and signal  transduction,  to ribosome assembly and protein synthesis. GTPases
exert their  control  by interchanging between an inactive GDP-bound state and
an active  GTP-bound  state,  thereby acting as molecular switches. The common
denominator of  GTPases is the highly conserved guanine nucleotide-binding (G)
domain that is responsible for binding and hydrolysis of guanine nucleotides.

EngA (Essential  neisserial  GTPase  A) proteins belong to TrmE-Era-EngA-YihA-
Septin like  superfamily of TRAFAC class and form a unique family of bacterial
GTPases with  two  G  domains  in tandem, namely GD1 and GD2, followed by a C-
terminal KH-like  domain.  They have been shown to interact with the bacterial
ribosome and to be involved in its biogenesis [1,2,3,4,5].

The EngA-type  G  domains  consist  of  ~159-170  amino acid residues and show
sequence homology  to  the  Era-type G domain. The EngA-type G domain has thus
also been  termed Der, because it has double Era-like G domains [2]. The EngA-
type G  domain  is  composed  of  5  alpha helices and 6 beta sheets linked by
characteristic loops constituting switch I and II (see <PDB:2HJG>). Each EngA-
type G  domain  contains  conserved residues organized in five distinct motifs
numbered G1-G5.  In  the  G1/Walker A motifs of EngA (Gx(4)GKS) or P-loop, the
two invariant  lysine  residues  are  known  to  coordinate  the  phosphate of
nucleotide. G2  (DxxG) belongs to the loop forming switch I and interacts with
a Mg(2+)  ion as well as the G3/Walker B motif (DxxG). G4 has a characteristic
NKxD sequence  that  is unique to GTPases and provides specificity to GTP. The
G5 motif (SA) is less obvious.

The profile we developed covers the entire EngA-type G domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: March 2014 / First entry.

[ 1] Leipe D.D., Wolf Y.I., Koonin E.V., Aravind L.
     "Classification and evolution of P-loop GTPases and related ATPases."
     J. Mol. Biol. 317:41-72(2002).
     PubMed=11916378; DOI=10.1006/jmbi.2001.5378
[ 2] Hwang J., Inouye M.
     "An essential GTPase, der, containing double GTP-binding domains from
     Escherichia  coli and Thermotoga maritima."
     J. Biol. Chem. 276:31415-31421(2001).
     PubMed=11387344; DOI=10.1074/jbc.M104455200
[ 3] Muench S.P., Xu L., Sedelnikova S.E., Rice D.W.
     "The essential GTPase YphC displays a major domain rearrangement
     associated with nucleotide binding."
     Proc. Natl. Acad. Sci. U.S.A. 103:12359-12364(2006).
     PubMed=16894162; DOI=10.1073/pnas.0602585103
[ 4] Agarwal N., Pareek M., Thakur P., Pathak V.
     "Functional characterization of EngA(MS), a P-loop GTPase of
     Mycobacterium smegmatis."
     PLoS ONE 7:E34571-E34571(2012).
     PubMed=22506030; DOI=10.1371/journal.pone.0034571
[ 5] Foucher A.-E., Reiser J.-B., Ebel C., Housset D., Jault J.-M.
     "Potassium acts as a GTPase-activating element on each
     nucleotide-binding domain of the essential Bacillus subtilis EngA."
     PLoS ONE 7:E46795-E46795(2012).
     PubMed=23056455; DOI=10.1371/journal.pone.0046795

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