{PDOC51108}
{PS51108; PTS_EIID}
{BEGIN}
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* PTS EIID domain profile *
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The  phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS) [1,2]
is  a  major  carbohydrate transport system in bacteria. The PTS catalyzes the
phosphorylation   of   incoming   sugar   substrates  concomitant  with  their
translocation  across  the  cell membrane. The general mechanism of the PTS is
the   following:   a   phosphoryl  group  from  phosphoenolpyruvate  (PEP)  is
transferred to enzyme I (EI) of PTS which in turn transfers it to a phosphoryl
carrier  protein  (HPr)  (see  <PDOC00318>).  Phospho-HPr  then  transfers the
phosphoryl group to a sugar-specific permease which consists of at least three
structurally  distinct  domains  (IIA,  IIB, and IIC), [3] which can either be
fused  together  in  a  single  polypeptide  chain  or  exist  as two or three
interactive chains, formerly called enzymes II (EII) and III (EIII).

The  first domain (IIA) (see <PDOC00528>), carries the first permease-specific
phosphorylation site, an histidine which is phosphorylated by phospho-HPr. The
second  domain  (IIB)  (see <PDOC00795>) is phosphorylated by phospho-IIA on a
cysteinyl  or  histidyl  residue, depending on the sugar transported. Finally,
the phosphoryl group is transferred from the IIB domain to the sugar substrate
concomitantly  with  the sugar uptake processed  by  the  IIC domain.  The IIC
(see  <PDOC51103>)  domain  forms  the  translocation channel and the specific
substrate-binding  site. An additional transmembrane domain IID, homologous to
IIC, can be found in some PTSs, e.g. for mannose [1,3,4,5,6].

We  have  developed a profile for this domain, which cover the entire PTS EIID
domain.

-Sequences known to belong to this class detected by the fifth profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: April 2005 / First entry.

[ 1] Postma P.W., Lengeler J.W., Jacobson G.R.
     "Phosphoenolpyruvate:carbohydrate phosphotransferase systems of
     bacteria."
     Microbiol. Rev. 57:543-594(1993).
     PubMed=8246840
[ 2] Meadow N.D., Fox D.K., Roseman S.
     "The bacterial phosphoenolpyruvate: glycose phosphotransferase
     system."
     Annu. Rev. Biochem. 59:497-542(1990).
     PubMed=2197982; DOI=10.1146/annurev.bi.59.070190.002433
[ 3] Saier M.H. Jr., Reizer J.
     "Proposed uniform nomenclature for the proteins and protein domains of
     the bacterial phosphoenolpyruvate: sugar phosphotransferase system."
     J. Bacteriol. 174:1433-1438(1992).
     PubMed=1537788
[ 4] Saier M.H. Jr., Reizer J.
     "The bacterial phosphotransferase system: new frontiers 30 years
     later."
     Mol. Microbiol. 13:755-764(1994).
     PubMed=7815935
[ 5] Tchieu J.H., Norris V., Edwards J.S., Saier M.H. Jr.
     "The complete phosphotranferase system in Escherichia coli."
     J. Mol. Microbiol. Biotechnol. 3:329-346(2001).
     PubMed=11361063
[ 6] Saier M.H., Hvorup R.N., Barabote R.D.
     "Evolution of the bacterial phosphotransferase system: from carriers
     and enzymes to group translocators."
     Biochem. Soc. Trans. 33:220-224(2005).
     PubMed=15667312; DOI=10.1042/BST0330220

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