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PDOC00013
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1995-07-26
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* Prokaryotic membrane lipoprotein lipid attachment site *
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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].
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 osmotically inducible lipoprotein (gene osmB).
- Escherichia coli peptidoglycan-associated lipoprotein (gene pal).
- Escherichia coli rare lipoproteins A and B (genes rplA and rplB).
- 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).
- 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).
- Neisseiria 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 archebacterial protein known to be
modified in such a fashion).
From the precursor sequences of all these proteins, we derived a consensus
pattern and a set of rules to identify this type of post-translational
modification.
-Consensus pattern: {DERK}(6)-[LIVMFSTAG](2)-[IVMSTAGQ]-[AGS]-C
[C is the lipid attachment site]
Additional rules: 1) The cysteine must be between positions 15 and 35 of the
sequence in consideration.
2) There must be at least one Lys or one Arg in the first
seven positions of the sequence.
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in SWISS-PROT: some 60 prokaryotic proteins. A few
of them are not membrane lipoproteins, but at least half of them could be,
some of which have been proposed to bind lipid (for example the endoglucanase
cel-3 from Fibrobacter succinogenes, or a neuraminidase from Clostridium
sordellii).
-Last update: June 1994 / Text revised.
[ 1] Hayashi S., Wu H.C.
J. Bioenerg. Biomembr. 22:451-471(1990).
[ 2] Klein P., Somorjai R.L., Lau P.C.K.
Protein Eng. 2:15-20(1988).
[ 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.
J. Biol. Chem. 269:14939-14945(1994).