{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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