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Volumn 275, Issue 33, 2000, Pages 25102-25108
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Conserved serine and histidine residues are critical for activity of the ER-type signal peptidase SipW of Bacillus subtilis
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Author keywords
[No Author keywords available]
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Indexed keywords
ASPARTIC ACID;
HISTIDINE;
SERINE;
SIGNAL PEPTIDASE;
SIGNAL PEPTIDASE I;
ARTICLE;
BACILLUS SUBTILIS;
BACTERIAL SPORE;
CONTROLLED STUDY;
ENDOPLASMIC RETICULUM;
ENZYME ACTIVE SITE;
ENZYME ACTIVITY;
ENZYME ANALYSIS;
ENZYME LOCALIZATION;
EUBACTERIUM;
GENETIC CONSERVATION;
NONHUMAN;
NUCLEOTIDE SEQUENCE;
PRIORITY JOURNAL;
PROTEIN PROCESSING;
PROTEIN SECRETION;
AMINO ACID SEQUENCE;
ARCHAEAL PROTEINS;
ASPARTIC ACID;
BACILLUS SUBTILIS;
BACTERIAL PROTEINS;
BINDING SITES;
BLOTTING, WESTERN;
CATALYSIS;
CELL FRACTIONATION;
CONSERVED SEQUENCE;
ELECTROPHORESIS, POLYACRYLAMIDE GEL;
ENDOPLASMIC RETICULUM;
HISTIDINE;
MEMBRANE PROTEINS;
MODELS, BIOLOGICAL;
MOLECULAR SEQUENCE DATA;
PEPTIDE HYDROLASES;
PLASMIDS;
PROTEIN STRUCTURE, TERTIARY;
SEQUENCE HOMOLOGY, AMINO ACID;
SERINE;
SERINE ENDOPEPTIDASES;
SPORES;
BACILLUS SUBTILIS;
BACTERIA (MICROORGANISMS);
POSIBACTERIA;
PROKARYOTA;
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EID: 0034682753
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: 10.1074/jbc.M002676200 Document Type: Article |
Times cited : (54)
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References (53)
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