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{PDOC00799}
{PS01040; SBP_BACTERIAL_5}
{BEGIN}
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* Bacterial extracellular solute-binding proteins, family 5 signature *
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Bacterial high affinity transport systems are involved in active  transport of
solutes across  the  cytoplasmic  membrane.  The  protein  components of these
traffic systems  include  one  or two transmembrane protein components, one or
two membrane-associated    ATP-binding   proteins   (ABC   transporters;   see
<PDOC00185>) and a high affinity periplasmic solute-binding protein. The later
are thought  to  bind the substrate in the vicinity of the inner membrane, and
to transfer  it to a complex of inner membrane proteins for concentration into
the cytoplasm.

In gram-positive  bacteria  which are surrounded by a single membrane and have
therefore no  periplasmic  region  the  equivalent  proteins  are bound to the
membrane via an N-terminal lipid anchor. These homolog proteins do not play an
integral role in the transport process per se, but probably serve as receptors
to trigger  or  initiate  translocation of the solute throught the membrane by
binding to  external  sites  of  the  integral membrane proteins of the efflux
system.

In addition  at  least some solute-binding proteins function in the initiation
of sensory transduction pathways.

On the  basis  of  sequence  similarities,  the vast majority of these solute-
binding proteins  can  be  grouped  [1] into eight families of clusters, which
generally correlate with the nature of the solute bound.

Family 5 currently includes the following proteins:

 - Periplasmic  oligopeptide-binding  proteins  (gene  oppA)  of Gram-negative
   bacteria and homologous lipoproteins in Gram-positive bacteria (genes oppA,
   amiA or appA).
 - Periplasmic  dipeptide-binding proteins of Escherichia coli (gene dppA) and
   of Bacillus subtilis (gene dppE).
 - Periplasmic murein peptide-binding protein of Escherichia coli (gene mppA).
 - Periplasmic  peptide-binding  proteins sapA of Escherichia coli, Salmonella
   typhimurium and Haemophilus influenzae.
 - Periplasmic nickel-binding protein (gene nikA) of Escherichia coli.
 - Heme-binding lipoprotein (gene hbpA or dppA) from Haemophilus influenzae.
 - Lipoprotein xP55 from Streptomyces lividans.
 - Haemophilus influenzae hypothetical protein HI0213.
 - Hypothethical protein y4tO from Rhizobium strain NGR234 symbiotic plasmid.
 - Hypothethical protein y4wM from Rhizobium strain NGR234 symbiotic plasmid.

The signature pattern is located near the N-terminus of the mature proteins.

-Consensus pattern: [AG]-x(6,7)-[DNEG]-x(2)-[STAIVE]-[LIVMFYWA]-x-[LIVMFY]-x-
                    [LIVM]-[KR]-[KRHDE]-[GDN]-[LIVMA]-[KNGSP]-[FW]
-Sequences known to belong to this class detected by the pattern: ALL,  except
 y4wM.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: July 1999 / Pattern and text revised.

[ 1] Tam R., Saier M.H. Jr.
     "Structural, functional, and evolutionary relationships among
     extracellular solute-binding receptors of bacteria."
     Microbiol. Rev. 57:320-346(1993).
     PubMed=8336670

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