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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 β-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.

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

October 2006 / Text revised; profiles added; rule deleted.

PROSITE method (with tools and information) covered by this documentation:

PROKAR_LIPOPROTEIN, PS51257; Prokaryotic membrane lipoprotein lipid attachment site profile  (MATRIX)

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.

• Domain architecture view of Swiss-Prot proteins matching PS51257 • Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS51257 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS51257 • Scan Swiss-Prot/TrEMBL entries against PS51257 • view ligand binding statistics

1	Authors	Hayashi S., Wu H.C.
	Title	Lipoproteins in bacteria.
	Source	J. Bioenerg. Biomembr. 22:451-471(1990).
	PubMed ID	2202727

2	Authors	Klein P., Somorjai R.L., Lau P.C.K.
	Title	Distinctive properties of signal sequences from bacterial lipoproteins.
	Source	Protein Eng. 2:15-20(1988).
	PubMed ID	3253732

3	Authors	von Heijne G.
	Source	Protein Eng. 2:531-534(1989).

4	Authors	Mattar S., Scharf B., Kent S.B.H., Rodewald K., Oesterhelt D., Engelhard M.
	Title	The primary structure of halocyanin, an archaeal blue copper protein, predicts a lipid anchor for membrane fixation.
	Source	J. Biol. Chem. 269:14939-14945(1994).
	PubMed ID	8195126

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