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Database: Pfam
Entry: T3SchapCesA
LinkDB: T3SchapCesA
Original site: T3SchapCesA 
#=GF ID   T3SchapCesA
#=GF AC   PF11439.8
#=GF DE   Type III secretion system filament chaperone CesA
#=GF PI   DUF3200; CesA;
#=GF AU   Pollington J;0000-0002-8158-8998
#=GF SE   pdb_1xou
#=GF GA   29.10 29.10;
#=GF TC   29.70 196.70;
#=GF NC   28.10 29.00;
#=GF BM   hmmbuild HMM.ann SEED.ann
#=GF SM   hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
#=GF TP   Family
#=GF RN   [1]
#=GF RM   15619638
#=GF RT   Structural characterization of a type III secretion system
#=GF RT   filament protein in complex with its chaperone.
#=GF RA   Yip CK, Finlay BB, Strynadka NC;
#=GF RL   Nat Struct Mol Biol. 2005;12:75-81.
#=GF DR   INTERPRO; IPR021545;
#=GF DR   SO; 0100021; polypeptide_conserved_region;
#=GF CC   This family represents a chaperone protein for the type III
#=GF CC   secretion system - TTSS - translocon protein EspA, to prevent
#=GF CC   the latter's self-polymerisation. The TTSS is a highly
#=GF CC   specialised bacterial protein secretory pathway, similar in many
#=GF CC   ways to the flagellar system, that is essential for the
#=GF CC   pathogenesis of many Gram-negative bacteria. The twenty or so
#=GF CC   proteins making up the TTSS apparatus, referred to as the needle
#=GF CC   complex, allow the injection of virulence proteins (known as
#=GF CC   effectors) directly into the cytoplasm of the eukaryotic host
#=GF CC   cells they infect; however, the injection process itself is
#=GF CC   mediated by a subset of extracellular proteins that are secreted
#=GF CC   by the needle complex to the bacterial surface and assembled
#=GF CC   into the type III translocon - EspA. EspB and EspD. EspA
#=GF CC   polymerises into an extracellular filament, and, as with other
#=GF CC   fibrous proteins, is apt to undergo massive polymerisation when
#=GF CC   overexpressed. CesA is the secretion chaperone protein that
#=GF CC   binds to EspA. CesA is dimeric and helical, and it traps EspA in
#=GF CC   a monomeric state and inhibits its polymerisation.
#=GF SQ   2
#=GS Q7DB53_ECO57/1-95  AC Q7DB53.1
#=GS D2TKH3_CITRI/1-95  AC D2TKH3.1
Q7DB53_ECO57/1-95             MSIVSQTRNKELLDKKIRSEIEAIKKIIAEFDVVKESVNELSEKAKTDPQAAEKLNKLIEGYTYGEERKLYDSALSKIEKLIETLSPARSKSQST
D2TKH3_CITRI/1-95             MNIVKQTKNKELLDKKIRSEIETIKKIIAEFDVIKENVNILSEKAKTSPQAAETLNKLIEGYTYGEERRLYDSALSKIEKLIETMKPTRSGSQLT
#=GC seq_cons                 MsIVpQT+NKELLDKKIRSEIEsIKKIIAEFDVlKEsVN.LSEKAKTsPQAAEpLNKLIEGYTYGEER+LYDSALSKIEKLIEThpPsRStSQ.T
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