ID   BIPD_BURM7              Reviewed;         310 AA.
AC   A3MCH1;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Translocator protein BipD;
GN   Name=bipD; OrderedLocusNames=BMA10247_A0757;
OS   Burkholderia mallei (strain NCTC 10247).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320389;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 10247;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
CC   -!- FUNCTION: Required for invasion of epithelial cells, as well as for
CC       survival within host cells, escape from endocytic vesicles and
CC       subsequent actin-tail formation. Probably regulates the secretion of
CC       effectors BipB and BipC and their final integration into the target
CC       cell membrane (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Secreted via the bsa
CC       type III secretion system. Localizes to the tip of the external
CC       secretion needle that is part of the secretion apparatus (By
CC       similarity). {ECO:0000250}.
CC   -!- DOMAIN: The N-terminal domain is an intra-molecular chaperone that
CC       prevents premature oligomerization of the residues on the coiled-coil
CC       region that are involved in interactions with the needle and/or itself.
CC       The residues in the C-terminal domain probably form oligomeric
CC       structures at the tip of the needle that are responsible for the
CC       regulation of secretion of other effectors (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the invasin protein D family. {ECO:0000305}.
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DR   EMBL; CP000547; ABO02884.1; -; Genomic_DNA.
DR   RefSeq; WP_004188590.1; NZ_CP007801.1.
DR   AlphaFoldDB; A3MCH1; -.
DR   SMR; A3MCH1; -.
DR   GeneID; 56597874; -.
DR   KEGG; bmaz:BM44_4989; -.
DR   KEGG; bmn:BMA10247_A0757; -.
DR   PATRIC; fig|320389.8.peg.5725; -.
DR   OMA; ERWETEH; -.
DR   Proteomes; UP000002284; Chromosome II.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   Gene3D; 1.20.1710.10; -; 1.
DR   InterPro; IPR036708; BipD-like_sf.
DR   InterPro; IPR009483; IpaD.
DR   Pfam; PF06511; T3SS_TC; 1.
DR   SUPFAM; SSF140693; SSF140693; 1.
DR   TIGRFAMs; TIGR02553; SipD_IpaD_SspD; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Secreted; Virulence.
FT   CHAIN           1..310
FT                   /note="Translocator protein BipD"
FT                   /id="PRO_0000344003"
FT   COILED          127..171
FT                   /evidence="ECO:0000255"
FT   COILED          250..299
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   310 AA;  33975 MW;  D6C446F4D919069D CRC64;
     MNMHVDMGRA LTVRDWPALE ALAKTMPADA GARAMTDDDL RAAGVDRRVP EQKLGAAIDE
     FASLRLPDRI DGRFVDGRRA NLTVFDDARV AVRGHARAQR NLLERLETEL LGGTLDTAGD
     EGGIQPDPIL QGLVDVIGQG KSDIDAYATI VEGLTKYFQS VADVMSKLQD YISAKDDKNM
     KIDGGKIKAL IQQVIDHLPT MQLPKGADIA RWRKELGDAV SISDSGVVTI NPDKLIKMRD
     SLPPDGTVWD TARYQAWNTA FSGQKDNIQN DVQTLVEKYS HQNSNFDNLV KVLSGAISTL
     TDTAKSYLQI