{PDOC00013}
{PS51257; PROKAR_LIPOPROTEIN}
{BEGIN}
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* Prokaryotic membrane lipoprotein lipid attachment site profile *
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In prokaryotes, membrane lipoproteins are synthesized  with a precursor signal
peptide, which is cleaved  by  a specific lipoprotein signal peptidase (signal
peptidase II). The peptidase recognizes a conserved sequence and cuts upstream
of a cysteine residue  to which a  glyceride-fatty acid lipid is attached [1].
Some of  the  proteins known to undergo such processing currently include (for
recent listings see [1,2,3]):

 - Major outer membrane lipoprotein (murein-lipoproteins) (gene lpp).
 - Escherichia coli lipoprotein-28 (gene nlpA).
 - Escherichia coli lipoprotein-34 (gene nlpB).
 - Escherichia coli lipoprotein nlpC.
 - Escherichia coli lipoprotein nlpD.
 - Escherichia coli osmotically inducible lipoprotein B (gene osmB).
 - Escherichia coli osmotically inducible lipoprotein E (gene osmE).
 - Escherichia coli peptidoglycan-associated lipoprotein (gene pal).
 - Escherichia coli rare lipoproteins A and B (genes rplA and rplB).
 - Escherichia coli copper homeostasis protein cutF (or nlpE).
 - Escherichia coli plasmids traT proteins.
 - Escherichia coli Col plasmids lysis proteins.
 - A number of Bacillus beta-lactamases.
 - Bacillus subtilis periplasmic oligopeptide-binding protein (gene oppA).
 - Borrelia burgdorferi outer surface proteins A and B (genes ospA and ospB).
 - Borrelia hermsii variable major protein 21 (gene vmp21) and 7 (gene vmp7).
 - Chlamydia trachomatis outer membrane protein 3 (gene omp3).
 - Fibrobacter succinogenes endoglucanase cel-3.
 - Haemophilus influenzae proteins Pal and Pcp.
 - Klebsiella pullulunase (gene pulA).
 - Klebsiella pullulunase secretion protein pulS.
 - Mycoplasma hyorhinis protein p37.
 - Mycoplasma hyorhinis variant surface antigens A, B, and C (genes vlpABC).
 - Neisseria outer membrane protein H.8.
 - Pseudomonas aeruginosa lipopeptide (gene lppL).
 - Pseudomonas solanacearum endoglucanase egl.
 - Rhodopseudomonas viridis reaction center cytochrome subunit (gene cytC).
 - Rickettsia 17 Kd antigen.
 - Shigella flexneri invasion plasmid proteins mxiJ and mxiM.
 - Streptococcus pneumoniae oligopeptide transport protein A (gene amiA).
 - Treponema pallidium 34 Kd antigen.
 - Treponema pallidium membrane protein A (gene tmpA).
 - Vibrio harveyi chitobiase (gene chb).
 - Yersinia virulence plasmid protein yscJ.

 - Halocyanin from Natrobacterium pharaonis [4], a membrane associated copper-
   binding protein.  This  is  the  first archaebacterial  protein known to be
   modified in such a fashion).

From  the precursor sequences of all these proteins, we derived a profile that
starts   at   the   beginning   of   the   sequence   and   ends   after   the
post-translationally modified cysteine.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: some 100 prokaryotic proteins. Some
 of them are not membrane lipoproteins, but at least half of them could be.

-Note:  This profile replace an obsolete rule. All the information in the rule
 has been encoded in the profile format.

-Last update: October 2006 / Text revised; profiles added; rule deleted.

[ 1] Hayashi S., Wu H.C.
     "Lipoproteins in bacteria."
     J. Bioenerg. Biomembr. 22:451-471(1990).
     PubMed=2202727
[ 2] Klein P., Somorjai R.L., Lau P.C.K.
     "Distinctive properties of signal sequences from bacterial
     lipoproteins."
     Protein Eng. 2:15-20(1988).
     PubMed=3253732
[ 3] von Heijne G.
     Protein Eng. 2:531-534(1989).
[ 4] Mattar S., Scharf B., Kent S.B.H., Rodewald K., Oesterhelt D.,
     Engelhard M.
     "The primary structure of halocyanin, an archaeal blue copper protein,
     predicts a lipid anchor for membrane fixation."
     J. Biol. Chem. 269:14939-14945(1994).
     PubMed=8195126
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