TY  - JOUR
AU  - Pastar, I
AU  - Tonić, I
AU  - Golić, Nataša
AU  - Kojić, Milan
AU  - van Kranenburg, R
AU  - Kleerebezem, M
AU  - Topisirović, Ljubiša
AU  - Jovanović, Goran
PY  - 2003
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/172
AB  - A novel proteinase, PrtR, produced by the human vaginal isolate Lactobacillus rhamnosus strain BGT10 was identified and genetically characterized. The prtR gene and flanking regions were cloned and sequenced. The deduced amino acid sequence of PrtR shares characteristics that are common for other cell envelope proteinases (CEPs) characterized to date, but in contrast to the other cell surface subtilisin-like serine proteinases, it has a smaller and somewhat different B domain and lacks the helix domain, and the anchor domain has a rare sorting signal sequence. Furthermore, PrtR lacks the insert domain, which otherwise is situated inside the catalytic serine protease domain of all CEPs, and has a different cell wall spacer (W) domain similar to that of the cell surface antigen I and II polypeptides expressed by oral and vaginal streptococci. Moreover, the PrtR W domain exhibits significant sequence homology to the consensus sequence that has been shown to be the hallmark of human intestinal mucin protein. According to its alpha(S1)- and beta-casein cleavage efficacy, PrtR is an efficient proteinase at pH 6.5 and is distributed throughout all L. rhamnosus strains tested. Proteinase extracts of the BGT10 strain obtained with Ca2+-free buffer at pH 6.5 were proteolytically active. The prtR promoter-like sequence was determined, and the minimal promoter region was defined by use of prtR-gusA operon fusions. The prtR expression is Casitone dependent, emphasizing that nitrogen depletion elevates its transcription. This is in correlation with the catalytic activity of the PrtR proteinase.
PB  - Amer Soc Microbiology, Washington
T2  - Applied and Environmental Microbiology
T1  - Identification and genetic characterization of a novel proteinase, PrtR, from the human isolate Lactobacillus rhamnosus BGT10
EP  - 5811
IS  - 10
SP  - 5802
VL  - 69
DO  - 10.1128/AEM.69.10.5802-5811.2003
ER  - 

@article{
author = "Pastar, I and Tonić, I and Golić, Nataša and Kojić, Milan and van Kranenburg, R and Kleerebezem, M and Topisirović, Ljubiša and Jovanović, Goran",
year = "2003",
abstract = "A novel proteinase, PrtR, produced by the human vaginal isolate Lactobacillus rhamnosus strain BGT10 was identified and genetically characterized. The prtR gene and flanking regions were cloned and sequenced. The deduced amino acid sequence of PrtR shares characteristics that are common for other cell envelope proteinases (CEPs) characterized to date, but in contrast to the other cell surface subtilisin-like serine proteinases, it has a smaller and somewhat different B domain and lacks the helix domain, and the anchor domain has a rare sorting signal sequence. Furthermore, PrtR lacks the insert domain, which otherwise is situated inside the catalytic serine protease domain of all CEPs, and has a different cell wall spacer (W) domain similar to that of the cell surface antigen I and II polypeptides expressed by oral and vaginal streptococci. Moreover, the PrtR W domain exhibits significant sequence homology to the consensus sequence that has been shown to be the hallmark of human intestinal mucin protein. According to its alpha(S1)- and beta-casein cleavage efficacy, PrtR is an efficient proteinase at pH 6.5 and is distributed throughout all L. rhamnosus strains tested. Proteinase extracts of the BGT10 strain obtained with Ca2+-free buffer at pH 6.5 were proteolytically active. The prtR promoter-like sequence was determined, and the minimal promoter region was defined by use of prtR-gusA operon fusions. The prtR expression is Casitone dependent, emphasizing that nitrogen depletion elevates its transcription. This is in correlation with the catalytic activity of the PrtR proteinase.",
publisher = "Amer Soc Microbiology, Washington",
journal = "Applied and Environmental Microbiology",
title = "Identification and genetic characterization of a novel proteinase, PrtR, from the human isolate Lactobacillus rhamnosus BGT10",
pages = "5811-5802",
number = "10",
volume = "69",
doi = "10.1128/AEM.69.10.5802-5811.2003"
}

Pastar, I., Tonić, I., Golić, N., Kojić, M., van Kranenburg, R., Kleerebezem, M., Topisirović, L.,& Jovanović, G.. (2003). Identification and genetic characterization of a novel proteinase, PrtR, from the human isolate Lactobacillus rhamnosus BGT10. in Applied and Environmental Microbiology
Amer Soc Microbiology, Washington., 69(10), 5802-5811.
https://doi.org/10.1128/AEM.69.10.5802-5811.2003

Pastar I, Tonić I, Golić N, Kojić M, van Kranenburg R, Kleerebezem M, Topisirović L, Jovanović G. Identification and genetic characterization of a novel proteinase, PrtR, from the human isolate Lactobacillus rhamnosus BGT10. in Applied and Environmental Microbiology. 2003;69(10):5802-5811.
doi:10.1128/AEM.69.10.5802-5811.2003 .

Pastar, I, Tonić, I, Golić, Nataša, Kojić, Milan, van Kranenburg, R, Kleerebezem, M, Topisirović, Ljubiša, Jovanović, Goran, "Identification and genetic characterization of a novel proteinase, PrtR, from the human isolate Lactobacillus rhamnosus BGT10" in Applied and Environmental Microbiology, 69, no. 10 (2003):5802-5811,
https://doi.org/10.1128/AEM.69.10.5802-5811.2003 . .