GenomeNet

Database: Pfam
Entry: IncD
LinkDB: IncD
Original site: IncD 
#=GF ID   IncD
#=GF AC   PF17628.6
#=GF DE   Inclusion membrane protein D
#=GF AU   El-Gebali S;0000-0003-1378-5495
#=GF SE   PRODOM:PD175759
#=GF GA   27.00 27.00;
#=GF TC   36.90 280.20;
#=GF NC   23.00 21.80;
#=GF BM   hmmbuild HMM.ann SEED.ann
#=GF SM   hmmsearch -E 1000 -Z 75585367 --cpu 4 HMM pfamseq
#=GF TP   Family
#=GF RN   [1]
#=GF RM   23696825
#=GF RT   Role for chlamydial inclusion membrane proteins in inclusion
#=GF RT   membrane structure and biogenesis.
#=GF RA   Mital J, Miller NJ, Dorward DW, Dooley CA, Hackstadt T;
#=GF RL   PLoS One. 2013;8:e63426.
#=GF RN   [2]
#=GF RM   25717440
#=GF RT   Characterization of interactions between inclusion membrane
#=GF RT   proteins from Chlamydia trachomatis.
#=GF RA   Gauliard E, Ouellette SP, Rueden KJ, Ladant D;
#=GF RL   Front Cell Infect Microbiol. 2015;5:13.
#=GF RN   [3]
#=GF RM   25930206
#=GF RT   Chlamydiae interaction with the endoplasmic reticulum: contact,
#=GF RT   function and consequences.
#=GF RA   Derre I;
#=GF RL   Cell Microbiol. 2015;17:959-966.
#=GF DR   INTERPRO; IPR035117;
#=GF DR   SO; 0100021; polypeptide_conserved_region;
#=GF CC   The chlamydial inclusion membrane is extensively modified by the
#=GF CC   insertion of type III secreted effector proteins [1]. These
#=GF CC   inclusion membrane proteins (Incs) have two major
#=GF CC   characteristics: an N-terminal type III secretion signal that is
#=GF CC   necessary for their secretion out of the bacterium and a
#=GF CC   hydrophobic region consisting of at least two trans-membrane
#=GF CC   helices that allows insertion into the inclusion membrane.
#=GF CC   Generally, both the N- and C-terminal regions of the Inc are
#=GF CC   exposed to the host cell cytosol [2]. This family has members
#=GF CC   such as the IncD proteins found in Chlamydia trachomatis. This
#=GF CC   C. trachomatis effector protein IncD has been shown to recruit
#=GF CC   the lipid transfer protein CERT to the inclusion membrane by
#=GF CC   directly interacting with CERT PH domain, which mediates the
#=GF CC   FFAT motif-dependent recruitment of the ER-resident protein VAPB
#=GF CC   (vesicle-associated membrane protein-associated protein) to the
#=GF CC   inclusion [3].
#=GF SQ   2
#=GS A0A655MW98_CHLTH/1-127  AC A0A655MW98.1
#=GS INCD_CHLTR/1-141        AC P0DJI3.1
A0A655MW98_CHLTH/1-127             --------------MDRIALLERCLDPSNSLPTAKRLVAVAVATILAVALLVVAGLLFSGVLCSPVSVLAASLFFGVGAFLLGGALVGGVLTTEAVTRERLHRSQTLMWNNLCCKTAEVEQKISTASANAKSNDKTRKLGE
INCD_CHLTR/1-141                   MTKVYANSIQQERVVDRIALLERCLDPSNSLPTAKRLVAVAVATILAVALLVVAGLLFSGVLCSPVSVLAASLFFGVGAFLLGGALVGGVLTTEAVTRERLHRSQTLMWNNLCCKTAEVEQKISTASANAKSNDKTRKLGE
#=GC seq_cons                      ..............hDRIALLERCLDPSNSLPTAKRLVAVAVATILAVALLVVAGLLFSGVLCSPVSVLAASLFFGVGAFLLGGALVGGVLTTEAVTRERLHRSQTLMWNNLCCKTAEVEQKISTASANAKSNDKTRKLGE
//
DBGET integrated database retrieval system