SepL resembles an aberrant effector in binding to a class 1 type III secretion chaperone and carrying an N-terminal secretion signal

Journal of Bacteriology

Volumn 192, Issue 22, 2010, Pages 6093-6098

  Younis, Rasha ^a   Bingle, Lewis E H ^a   Rollauer, Sarah ^b   Munera, Diana ^c   Busby, Stephen J ^a   Johnson, Steven ^b   Deane, Janet E ^b,d   Lea, Susan M ^b   Frankel, Gad ^c   Pallen, Mark J ^a  

^a UNIVERSITY OF BIRMINGHAM   (United Kingdom)

^b UNIVERSITY OF OXFORD   (United Kingdom)

^c IMPERIAL COLLEGE LONDON   (United Kingdom)

^d UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; PROTEIN CESL; PROTEIN SEPL; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; GENE TRANSLOCATION; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN SECRETION; TYPE III SECRETION SYSTEM;

AMINO ACID SEQUENCE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN SORTING SIGNALS; PROTEIN TRANSPORT; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID;

PYRONIA TITHONUS;

EID: 78049445421     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00760-10     Document Type: Article

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