About: A single bifunctional enzyme, PilD, catalyzes cleavage and N-methylation of proteins belonging to the type IV pilin family

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About: A single bifunctional enzyme, PilD, catalyzes cleavage and N-methylation of proteins belonging to the type IV pilin family Goto Sponge NotDistinct Permalink

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description	artículu científicu espublizáu en 1993 (ast) vědecký článek publikovaný v roce 1993 (cs) vedecký článok (publikovaný 1993/03/15) (sk) 1993 թուականի Մարտին հրատարակուած գիտական յօդուած (hyw) наукова стаття, опублікована в березні 1993 (uk) 1993 թվականի մարտին հրատարակված գիտական հոդված (hy) مقالة علمية (نشرت في 15-3-1993) (ar) 1993年學術文章 (zh) wetenschappelijk artikel (gepubliceerd op 1993/03/15) (nl) article publié dans les Proceedings of the National Academy of Sciences of the United States of America (fr) scientific journal article (en) im März 1993 veröffentlichter wissenschaftlicher Artikel (de)
publication date	wds:Q28492973-8FF0A18C-BA05-49CB-928F-8FE6B725C54F
publication date	1993-03-15 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28492973-B03302C0-F195-480E-83D9-1E4880293F2A
language of work or name	English
cites work	wds:Q28492973-097947CD-C474-446F-B5DB-CB267778DA1A wds:Q28492973-1AC5E66C-8B89-492B-8D61-5D6BC9271F5F wds:Q28492973-3067D3E8-4265-4264-8096-C099663E0824 wds:Q28492973-319474C5-5784-439B-A5C7-863362900C14 wds:Q28492973-35A7E535-DC75-4167-A7CF-BF2839404D6E wds:Q28492973-3A77DEBE-91CA-4573-8F62-C4BAE82A37A7 wds:Q28492973-49BCBB7B-F067-4328-A8BA-31DD3B3FB9CB wds:Q28492973-4C28CA1C-5F06-4E4D-BAA7-37EC584AB62B wds:Q28492973-54D2189D-AC6E-4BC7-8BC3-42977C13BFB2 wds:Q28492973-5592CEC0-23FF-49D3-BD94-BC5ED3139414 wds:Q28492973-56BFE332-6FF5-4007-9EF3-F211AF9F114B wds:Q28492973-5C5D3619-BED3-43BD-9D7C-C8227D6F6658 wds:Q28492973-60234F1F-0A20-40CB-94A6-5A8D02B6ED3B wds:Q28492973-6096A8B5-8D02-4DB2-BCB6-8060E9D50938 wds:Q28492973-64D55591-A018-4625-9D14-1AA37D4F4ECD wds:Q28492973-77631E14-21A7-415F-9BAC-B9AFB48DABBC wds:Q28492973-7E5268E2-E971-466C-9BCB-B62FE3CB4C8E wds:Q28492973-7E815F70-5BA5-4392-B77D-3E39A6A737F9 wds:Q28492973-7F356740-DF8A-4A3A-904A-13B1B851F461 wds:Q28492973-85116F5D-43DD-4422-BCAE-45EDAD94D69C wds:Q28492973-8708B815-4B7F-443C-B45C-B30EF5D980C6 wds:Q28492973-9429BB2C-67E2-44E0-82B2-782991E4E89D wds:Q28492973-976B2B54-4900-4EF8-B78B-F9E868F88160 wds:Q28492973-9FF4AECD-55C4-4B35-AE04-737B771642A6 wds:Q28492973-A8CF7E22-779D-4CA0-9374-14FD26D55A17 wds:Q28492973-BA61E5AD-51FB-4A1A-96D3-3A19FD98CC12 wds:Q28492973-BEB648AC-9507-4B9C-B880-B8E1AF389DF3 wds:Q28492973-C02CEA61-B08D-4B17-8A13-E594EDEDA6F8 wds:Q28492973-D6CD41D5-E2CF-45EE-B960-2E370292883C wds:Q28492973-EE32426C-2B3A-4E75-BBFC-018C96F20A92 wds:Q28492973-F210F79E-69C0-4F35-B319-76E78E7EF939 wds:Q28492973-F35883BE-A560-4D52-9CB8-0EBE870E3C22 wds:Q28492973-F71DCB51-C12E-4E84-B77D-60448AA7A913
cites work	Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa Multiple roles of the pilus biogenesis protein pilD: involvement of pilD in excretion of enzymes from Pseudomonas aeruginosa Products of three accessory genes, pilB, pilC, and pilD, are required for biogenesis of Pseudomonas aeruginosa pili Product of the Pseudomonas aeruginosa gene pilD is a prepilin leader peptidase Amino acid substitutions in pilin of Pseudomonas aeruginosa. Effect on leader peptide cleavage, amino-terminal methylation, and pilus assembly N-terminal methylation of proteins: structure, function and specificity The protein carboxylmethyltransferase involved in Escherichia coli and Salmonella typhimurium chemotaxis. Protein secretion in Pseudomonas aeruginosa: characterization of seven xcp genes and processing of secretory apparatus components by prepilin peptidase Cloning and sequencing of a Moraxella bovis pilin gene Cloned Erwinia chrysanthemi out genes enable Escherichia coli to selectively secrete a diverse family of heterologous proteins to its milieu Pilus genes of Neisseria gonorrheae: chromosomal organization and DNA sequence Structural characterization of protein secretion genes of the bacterial phytopathogen Xanthomonas campestris pathovar campestris: relatedness to secretion systems of other gram-negative bacteria Amino acid sequence of pilin from Bacteroides nodosus (strain 198), the causative organism of ovine footrot Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes Molecular cloning and characterization of comC, a late competence gene of Bacillus subtilis Five additional genes in the pulC-O operon of the gram-negative bacterium Klebsiella oxytoca UNF5023 which are required for pullulanase secretion. Protein carboxyl methyltransferases: two distinct classes of enzymes The primary structure of protein L16 located at the peptidyltransferase center of Escherichia coli ribosomes An enzyme with type IV prepilin peptidase activity is required to process components of the general extracellular protein secretion pathway of Klebsiella oxytoca Components of the protein-excretion apparatus of Pseudomonas aeruginosa are processed by the type IV prepilin peptidase Five genes at the 3' end of the Klebsiella pneumoniae pulC operon are required for pullulanase secretion. Vibrio cholerae O395 tcpA pilin gene sequence and comparison of predicted protein structural features to those of type 4 pilins Protein secretion in Pseudomonas aeruginosa: the xcpA gene encodes an integral inner membrane protein homologous to Klebsiella pneumoniae secretion function protein PulO Nucleotide sequence and genetic organization of the Bacillus subtilis comG operon Characterization of Pseudomonas aeruginosa mutants with altered piliation The type 4 pilin of Moraxella nonliquefaciens exhibits unique similarities with the pilins of Neisseria gonorrhoeae and Dichelobacter (Bacteroides) nodosus. Kinetics and sequence specificity of processing of prepilin by PilD, the type IV leader peptidase of Pseudomonas aeruginosa Occurrence of methylated amino acids as N-termini of proteins from Escherichia coli ribosomes The primary structure of the initiation factor IF-3 from Escherichia coli The primary structure of L11, the most heavily methylated protein fromEscherichia coliribosomes Genetic and biochemical analysis of protein export from Xanthomonas campestris A second type of protein methylation reaction in bacterial chemotaxis. N-Methylmethionine at the Amino Terminus of a Protein Required for Bacterial Chemotaxis
author name string	wds:Q28492973-0547CD29-0F2C-4C51-ADB2-D269A20D2512 wds:Q28492973-F7683A99-EF55-42CC-B22B-08733574597F wds:Q28492973-FDDBBCCF-7B02-4D27-8E8F-8816BF7FD2C2
OpenCitations bibliographic resource ID	wds:Q28492973-C5888C8D-3686-40D4-890C-DBCD440FC5B8
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/1799415
author name string	M. S. Strom S. Lory D. N. Nunn
OpenCitations bibliographic resource ID	1799415
rdfs:label	A single bifunctional enzyme, PilD, catalyzes cleavage and N-methylation of proteins belonging to the type IV pilin family (en) A single bifunctional enzyme, PilD, catalyzes cleavage and N-methylation of proteins belonging to the type IV pilin family (nl) A single bifunctional enzyme, PilD, catalyzes cleavage and N-methylation of proteins belonging to the type IV pilin family (ast)
skos:prefLabel	A single bifunctional enzyme, PilD, catalyzes cleavage and N-methylation of proteins belonging to the type IV pilin family (en) A single bifunctional enzyme, PilD, catalyzes cleavage and N-methylation of proteins belonging to the type IV pilin family (nl) A single bifunctional enzyme, PilD, catalyzes cleavage and N-methylation of proteins belonging to the type IV pilin family (ast)
name	A single bifunctional enzyme, PilD, catalyzes cleavage and N-methylation of proteins belonging to the type IV pilin family (en) A single bifunctional enzyme, PilD, catalyzes cleavage and N-methylation of proteins belonging to the type IV pilin family (nl)

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