{PDOC51713}
{PS51713; G_ERA}
{BEGIN}
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* Era-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.

Era is a small G-protein widely conserved in eubacteria and eukaryotes. It is
essential for bacterial cell viability and is required for the maturation of
16S rRNA and assembly of the 30S ribosomal subunit. Era contains an N-terminal
GTPase domain and a C-terminal distinct derivative of the type-II RNA-binding
KH domain (see <PDOC50084>) [1,2,3,4].

The Era-type  GTPase  domain  consists  of  a  central six-stranded beta-sheet
flanked by  five  alpha-helices, in which the GTP-binding site is located (see
<PDB:3IEU>). Guanine  nucleotide  molecules  interact  with highly conserved G
protein regions G1-G5 [3].

The profile we developed covers the entire Era-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: April 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] Sullivan S.M., Mishra R., Neubig R.R., Maddock J.R.
     "Analysis of guanine nucleotide binding and exchange kinetics of the
     Escherichia coli GTPase Era."
     J. Bacteriol. 182:3460-3466(2000).
     PubMed=10852878
[ 3] Tu C., Zhou X., Tropea J.E., Austin B.P., Waugh D.S., Court D.L.,
     Ji X.
     "Structure of ERA in complex with the 3' end of 16S rRNA: implications
     for ribosome biogenesis."
     Proc. Natl. Acad. Sci. U.S.A. 106:14843-14848(2009).
     PubMed=19706445; DOI=10.1073/pnas.0904032106
[ 4] Tu C., Zhou X., Tarasov S.G., Tropea J.E., Austin B.P., Waugh D.S.,
     Court D.L., Ji X.
     "The Era GTPase recognizes the GAUCACCUCC sequence and binds helix 45
     near the 3'  end of 16S rRNA."
     Proc. Natl. Acad. Sci. U.S.A. 108:10156-10161(2011).
     PubMed=21646538; DOI=10.1073/pnas.1017679108

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