PROSITE documentation PDOC00013

Prokaryotic membrane lipoprotein lipid attachment site profile




Description

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.

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.

Technical section

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

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


References

1AuthorsHayashi S., Wu H.C.
TitleLipoproteins in bacteria.
SourceJ. Bioenerg. Biomembr. 22:451-471(1990).
PubMed ID2202727

2AuthorsKlein P., Somorjai R.L., Lau P.C.K.
TitleDistinctive properties of signal sequences from bacterial lipoproteins.
SourceProtein Eng. 2:15-20(1988).
PubMed ID3253732

3Authorsvon Heijne G.
SourceProtein Eng. 2:531-534(1989).

4AuthorsMattar S., Scharf B., Kent S.B.H., Rodewald K., Oesterhelt D., Engelhard M.
TitleThe primary structure of halocyanin, an archaeal blue copper protein, predicts a lipid anchor for membrane fixation.
SourceJ. Biol. Chem. 269:14939-14945(1994).
PubMed ID8195126



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