A peptidoglycan binding domain in the porin-associated protein (PAP) of Rhodospirillum rubrum FR1

Uwe Neumann; Emile Schiltz; Bernd Stahl; Franz Hillenkamp; Jürgen Weckesser

doi:10.1016/0378-1097(96)00082-1

A peptidoglycan binding domain in the porin-associated protein (PAP) of Rhodospirillum rubrum FR1

Uwe Neumann^*
, Emile Schiltz
, Bernd Stahl
, Franz Hillenkamp
, Jürgen Weckesser

^*Corresponding author for this work

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

The porin-associated protein of Rhodospirillum rubrum FR1 was found to contain a peptidoglycan binding motif. A partial fragment of 179 amino, acids, obtained by cleavage of PAP with trypsin, Asp-N protease, and CNBr, was sequenced. Substantial sequence homology was found of the C-terminal part (residues 126-179) of porin-associated protein with OmpA, the peptidoglycan-associated lipoprotein of several bacteria, protein F of Pseudomonas aeruginosa, and PIII of Neisseria gonorrhoeae, the latter being also a porin-associated protein. The 179 amino acid fragment comprised about 67% of the mass spectrometrically determined total mass of PAP of 27,850 Da.

Original language	English
Pages (from-to)	55-58
Number of pages	4
Journal	FEMS Microbiology Letters
Volume	138
Issue number	1
DOIs	https://doi.org/10.1016/0378-1097(96)00082-1
Publication status	Published - 15 Apr 1996
Externally published	Yes

Bibliographical note

Funding Information:
The authors thank the Deutsche Forschungsge-meinschaft and the Fonds der Chemischen Industrie for financial support.

Funding

The authors thank the Deutsche Forschungsge-meinschaft and the Fonds der Chemischen Industrie for financial support.

Keywords

Bacterial cell wall
Membrane protein
OmpA
Outer membrane
Porin
Porin-assoeiated-protein
Rhodospirillum rubrum

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@article{e0f6869e72ca4506828140a9fcf5d8b1,

title = "A peptidoglycan binding domain in the porin-associated protein (PAP) of Rhodospirillum rubrum FR1",

abstract = "The porin-associated protein of Rhodospirillum rubrum FR1 was found to contain a peptidoglycan binding motif. A partial fragment of 179 amino, acids, obtained by cleavage of PAP with trypsin, Asp-N protease, and CNBr, was sequenced. Substantial sequence homology was found of the C-terminal part (residues 126-179) of porin-associated protein with OmpA, the peptidoglycan-associated lipoprotein of several bacteria, protein F of Pseudomonas aeruginosa, and PIII of Neisseria gonorrhoeae, the latter being also a porin-associated protein. The 179 amino acid fragment comprised about 67\% of the mass spectrometrically determined total mass of PAP of 27,850 Da.",

keywords = "Bacterial cell wall, Membrane protein, OmpA, Outer membrane, Porin, Porin-assoeiated-protein, Rhodospirillum rubrum",

author = "Uwe Neumann and Emile Schiltz and Bernd Stahl and Franz Hillenkamp and J{\"u}rgen Weckesser",

note = "Funding Information: The authors thank the Deutsche Forschungsge-meinschaft and the Fonds der Chemischen Industrie for financial support.",

year = "1996",

month = apr,

day = "15",

doi = "10.1016/0378-1097(96)00082-1",

language = "English",

volume = "138",

pages = "55--58",

journal = "FEMS Microbiology Letters",

issn = "0378-1097",

publisher = "Oxford University Press",

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TY - JOUR

T1 - A peptidoglycan binding domain in the porin-associated protein (PAP) of Rhodospirillum rubrum FR1

AU - Neumann, Uwe

AU - Schiltz, Emile

AU - Stahl, Bernd

AU - Hillenkamp, Franz

AU - Weckesser, Jürgen

N1 - Funding Information: The authors thank the Deutsche Forschungsge-meinschaft and the Fonds der Chemischen Industrie for financial support.

PY - 1996/4/15

Y1 - 1996/4/15

N2 - The porin-associated protein of Rhodospirillum rubrum FR1 was found to contain a peptidoglycan binding motif. A partial fragment of 179 amino, acids, obtained by cleavage of PAP with trypsin, Asp-N protease, and CNBr, was sequenced. Substantial sequence homology was found of the C-terminal part (residues 126-179) of porin-associated protein with OmpA, the peptidoglycan-associated lipoprotein of several bacteria, protein F of Pseudomonas aeruginosa, and PIII of Neisseria gonorrhoeae, the latter being also a porin-associated protein. The 179 amino acid fragment comprised about 67% of the mass spectrometrically determined total mass of PAP of 27,850 Da.

AB - The porin-associated protein of Rhodospirillum rubrum FR1 was found to contain a peptidoglycan binding motif. A partial fragment of 179 amino, acids, obtained by cleavage of PAP with trypsin, Asp-N protease, and CNBr, was sequenced. Substantial sequence homology was found of the C-terminal part (residues 126-179) of porin-associated protein with OmpA, the peptidoglycan-associated lipoprotein of several bacteria, protein F of Pseudomonas aeruginosa, and PIII of Neisseria gonorrhoeae, the latter being also a porin-associated protein. The 179 amino acid fragment comprised about 67% of the mass spectrometrically determined total mass of PAP of 27,850 Da.

KW - Bacterial cell wall

KW - Membrane protein

KW - OmpA

KW - Outer membrane

KW - Porin

KW - Porin-assoeiated-protein

KW - Rhodospirillum rubrum

UR - https://www.scopus.com/pages/publications/0029984887

U2 - 10.1016/0378-1097(96)00082-1

DO - 10.1016/0378-1097(96)00082-1

M3 - Article

C2 - 8674970

AN - SCOPUS:0029984887

SN - 0378-1097

VL - 138

SP - 55

EP - 58

JO - FEMS Microbiology Letters

JF - FEMS Microbiology Letters

IS - 1

ER -

A peptidoglycan binding domain in the porin-associated protein (PAP) of Rhodospirillum rubrum FR1

Abstract

Bibliographical note

Funding

Keywords

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