Amidase domains from bacterial and phage autolysins define a family of gamma-D,L-glutamate-specific amidohydrolases.
about
One for all or all for one: heterogeneous expression and host cell lysis are key to gene transfer agent activity in Rhodobacter capsulatusFratricide is essential for efficient gene transfer between pneumococci in biofilmsDissecting the essentiality of the bifunctional trypanothione synthetase-amidase in Trypanosoma brucei using chemical and genetic methodsLeishmania trypanothione synthetase-amidase structure reveals a basis for regulation of conflicting synthetic and hydrolytic activitiesThe PECACE domain: a new family of enzymes with potential peptidoglycan cleavage activity in Gram-positive bacteriaSystematic association of genes to phenotypes by genome and literature miningStructure of the γ- D -glutamyl- L -diamino acid endopeptidase YkfC from Bacillus cereus in complex with L -Ala-γ- D -Glu: insights into substrate recognition by NlpC/P60 cysteine peptidasesStructural elucidation of the Cys-His-Glu-Asn proteolytic relay in the secreted CHAP domain enzyme from the human pathogenStaphylococcus saprophyticusStructural Basis of Murein Peptide Specificity of a γ-D-Glutamyl-L-Diamino Acid EndopeptidaseStructure and mechanism ofEscherichia coliglutathionylspermidine amidase belonging to the family of cysteine; histidine-dependent amidohydrolases/peptidasesStructural Insights into the Effector – Immunity System Tse1/Tsi1 from Pseudomonas aeruginosaStructure of the Type VI Effector-Immunity Complex (Tae4-Tai4) Provides Novel Insights into the Inhibition Mechanism of the Effector by Its Immunity ProteinCrystal structure of type VI effector Tse1 from Pseudomonas aeruginosaStructural insights into the inhibition of type VI effector Tae3 by its immunity protein Tai3Functional and structural characterization of a novel putative cysteine protease cell wall-modifying multi-domain enzyme selected from a microbial metagenome.Biochemical and biophysical characterization of PlyGRCS, a bacteriophage endolysin active against methicillin-resistant Staphylococcus aureus.Peptidoglycan hydrolase fusions maintain their parental specificitiesExtensive genomic plasticity in Pseudomonas aeruginosa revealed by identification and distribution studies of novel genes among clinical isolates.How Listeria monocytogenes organizes its surface for virulencecse, a Chimeric and variable gene, encodes an extracellular protein involved in cellular segregation in Streptococcus thermophilusStaphylococcus haemolyticus prophage ΦSH2 endolysin relies on cysteine, histidine-dependent amidohydrolases/peptidases activity for lysis 'from without'Peptidoglycan crosslinking relaxation plays an important role in Staphylococcus aureus WalKR-dependent cell viability.Competence-programmed predation of noncompetent cells in the human pathogen Streptococcus pneumoniae: genetic requirementsComparative genomics of four closely related Clostridium perfringens bacteriophages reveals variable evolution among core genes with therapeutic potential.Lytic activity of the virion-associated peptidoglycan hydrolase HydH5 of Staphylococcus aureus bacteriophage vB_SauS-phiIPLA88.Immunoproteomic assay of secreted proteins of Streptococcus suis serotype 9 with convalescent sera from pigs.TgaA, a VirB1-like component belonging to a putative type IV secretion system of Bifidobacterium bifidum MIMBb75Streptococcus pyogenes Ser/Thr kinase-regulated cell wall hydrolase is a cell division plane-recognizing and chain-forming virulence factor.Characterization of the modular design of the autolysin/adhesin Aaa from Staphylococcus aureusEngineered bacteriophage lysins as novel anti-infectivesThe genome of the novel phage Rtp, with a rosette-like tail tip, is homologous to the genome of phage T1Potential of the virion-associated peptidoglycan hydrolase HydH5 and its derivative fusion proteins in milk biopreservation.Differential proteomic analysis of the Bacillus anthracis secretome: distinct plasmid and chromosome CO2-dependent cross talk mechanisms modulate extracellular proteolytic activitiesPlyC: a multimeric bacteriophage lysin.Endopeptidase and glycosidase activities of the bacteriophage B30 lysinCharacterization of mutants deficient in the L,D-carboxypeptidase (DacB) and WalRK (VicRK) regulon, involved in peptidoglycan maturation of Streptococcus pneumoniae serotype 2 strain D39.A functional peptidoglycan hydrolase characterized from T4SS in 89K pathogenicity island of epidemic Streptococcus suis serotype 2Characterization of the fibrinogen binding domain of bacteriophage lysin from Streptococcus mitis.LytN, a murein hydrolase in the cross-wall compartment of Staphylococcus aureus, is involved in proper bacterial growth and envelope assembly.Serine/threonine protein kinase Stk is required for virulence, stress response, and penicillin tolerance in Streptococcus pyogenes.
P2860
Q21560770-5DFF0E25-C58B-4E7C-A5CC-A7653E8C3619Q24629356-A69F8B75-9606-4E92-B9E7-7B4367FE8E35Q24649110-2ACA2B3B-1E8A-453F-B28B-5045F040E4D6Q24655332-59EB7ECC-016B-4F5D-A760-BEA70E771A2BQ24795323-4F03A842-89E2-41E4-AA28-21FEC546CA7CQ24806114-E4BE48E6-152B-429E-81E1-94E5F92C2A53Q27644469-EAB4986E-CB6D-4DE9-818E-6A6457071B62Q27652649-74C4B6A8-6053-4045-ABF6-B31761D9B50BQ27653800-CDA45D33-6E1F-4F52-8DC8-B0925E22689DQ27666555-CFD400E9-7E6B-4BBD-AF47-3B33411442BDQ27670727-5D88B228-A1EC-4514-8850-8B099AF50AFFQ27675748-A9FFE40B-1695-4E94-AC90-9147B431689BQ27681661-9FDB1CC6-6516-45B9-904B-5EE9722B5127Q27684739-A6CAD24F-805A-4AA1-BBD0-42D033775E76Q30008807-7329FCD6-823F-417A-A692-79F51EA9C12BQ30009348-B22ED00E-DC68-4A09-8765-A15635D5407CQ30446323-27029683-C5A1-4C39-821A-85B71A33563CQ33254871-AD1B16B7-EEE4-4F6D-92AA-D3172C37160FQ33569229-2174A407-3119-4A7E-8677-586AE0E0B729Q33726785-08E53032-CAA5-4ED5-ABCA-649683D89B7BQ33775374-78CBE21E-BB29-428A-9298-7C88EE009EDFQ33840892-528DFCAE-65A0-4B12-9A71-A492CBFE0DB3Q33853895-01ACD678-9BC8-475D-8F3D-7CF4620F2865Q33919231-13AE5CD9-0722-4CFF-B561-B662031E4145Q33935353-A14D446B-AFDF-4DA4-AB71-3657FBA71922Q34016797-BBD02C36-3CAF-401D-8042-8D74ECA470B6Q34058443-BCD70256-3F66-4AC4-8ADF-8D4C89232AC4Q34155390-14B3B25C-7F33-4C79-806C-4199D1EEEC4BQ34328881-784742A7-DCFE-4143-835D-C22A8B3D32B5Q34349552-817F0A54-D611-4FC3-870E-6158A2D21055Q34353966-122E1196-DF35-4236-8519-88DEE461A376Q34566563-06EAA7EE-E0F8-46C4-8443-293CD4A6BF10Q34696713-7593C6C9-FD93-4D04-93F7-B4EAE4C97F6AQ34708961-D62BC0CA-FFBF-420B-A33E-2F7922C034ACQ35091838-FB44E74C-5A9E-4F08-83AA-875D4121D895Q35095905-E49BC096-BE79-4A9D-8C42-61913FE8793EQ35127298-7DBBE30D-8116-4DD3-92F8-9AB44660A28CQ35191968-633749AF-C9AB-4052-BE89-5998ECBADC83Q35213392-625A0759-DA3B-4D9A-9BD2-18208CE69569Q35273191-EBE8BE00-70FF-4A67-AB06-31732EA6173D
P2860
Amidase domains from bacterial and phage autolysins define a family of gamma-D,L-glutamate-specific amidohydrolases.
description
2003 nî lūn-bûn
@nan
2003 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Amidase domains from bacterial ...... mate-specific amidohydrolases.
@ast
Amidase domains from bacterial ...... mate-specific amidohydrolases.
@en
type
label
Amidase domains from bacterial ...... mate-specific amidohydrolases.
@ast
Amidase domains from bacterial ...... mate-specific amidohydrolases.
@en
prefLabel
Amidase domains from bacterial ...... mate-specific amidohydrolases.
@ast
Amidase domains from bacterial ...... mate-specific amidohydrolases.
@en
P1476
Amidase domains from bacterial ...... mate-specific amidohydrolases.
@en
P2093
Mark J Jedrzejas
P304
P356
10.1016/S0968-0004(03)00062-8
P577
2003-05-01T00:00:00Z