The peptidyl-prolyl isomerase motif is lacking in PmpA, the PrsA-like protein involved in the secretion machinery of Lactococcus lactis

The peptidyl-prolyl isomerase motif is lacking in PmpA, the PrsA-like protein involved in the secretion machinery of Lactococcus lactis

Item
http://www.wikidata.org/entity/Q34057292
PpiA, a surface PPIase of the cyclophilin family in Lactococcus lactisHow Listeria monocytogenes organizes its surface for virulenceMicrobial peptidyl-prolyl cis/trans isomerases (PPIases): virulence factors and potential alternative drug targets.Antimicrobial peptides targeting Gram-negative pathogens, produced and delivered by lactic acid bacteria.Functional analysis of the Listeria monocytogenes secretion chaperone PrsA2 and its multiple contributions to bacterial virulence.Dimeric Structure of the Bacterial Extracellular Foldase PrsA.Mutation of the maturase lipoprotein attenuates the virulence of Streptococcus equi to a greater extent than does loss of general lipoprotein lipidationType I signal peptidase and protein secretion in Staphylococcus aureus.Identification of Conserved and Species-Specific Functions of the Listeria monocytogenes PrsA2 Secretion Chaperone.The Staphylococcus aureus Chaperone PrsA Is a New Auxiliary Factor of Oxacillin Resistance Affecting Penicillin-Binding Protein 2AThe posttranslocation chaperone PrsA2 contributes to multiple facets of Listeria monocytogenes pathogenesisPhenotypic characterization of the foldase homologue PrsA in Streptococcus mutans.Listeria monocytogenes virulence factor secretion: don't leave the cell without a chaperoneDetermination of the domain of the Lactobacillus delbrueckii subsp. bulgaricus cell surface proteinase PrtB involved in attachment to the cell wall after heterologous expression of the prtB gene in Lactococcus lactis.The streptococcal lipoprotein rotamase A (SlrA) is a functional peptidyl-prolyl isomerase involved in pneumococcal colonization.Characterisation of SEQ0694 (PrsA/PrtM) of Streptococcus equi as a functional peptidyl-prolyl isomerase affecting multiple secreted protein substrates.Structure-function analysis of PrsA reveals roles for the parvulin-like and flanking N- and C-terminal domains in protein folding and secretion in Bacillus subtilis.
P2860

The peptidyl-prolyl isomerase motif is lacking in PmpA, the PrsA-like protein involved in the secretion machinery of Lactococcus lactis

Item
http://www.wikidata.org/entity/Q34057292
description
2002 nî lūn-bûn
@nan
2002 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
The peptidyl-prolyl isomerase ...... achinery of Lactococcus lactis
@ast
The peptidyl-prolyl isomerase ...... achinery of Lactococcus lactis
@en
The peptidyl-prolyl isomerase ...... achinery of Lactococcus lactis
@nl
type
label
The peptidyl-prolyl isomerase ...... achinery of Lactococcus lactis
@ast
The peptidyl-prolyl isomerase ...... achinery of Lactococcus lactis
@en
The peptidyl-prolyl isomerase ...... achinery of Lactococcus lactis
@nl
prefLabel
The peptidyl-prolyl isomerase ...... achinery of Lactococcus lactis
@ast
The peptidyl-prolyl isomerase ...... achinery of Lactococcus lactis
@en
The peptidyl-prolyl isomerase ...... achinery of Lactococcus lactis
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698
P932
P356
P1433
P1476
The peptidyl-prolyl isomerase ...... achinery of Lactococcus lactis
@en
P2093
P2860
P304
P31
P356
10.1128/AEM.68.8.3932-3942.2002
P407
P433
P478
P577
P698
P932