ID   BIPD_BURTA              Reviewed;         310 AA.
AC   Q2T708;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Translocator protein BipD;
GN   Name=bipD; OrderedLocusNames=BTH_II0844;
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS   E264).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX   PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA   Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA   DeShazer D.;
RT   "Bacterial genome adaptation to niches: divergence of the potential
RT   virulence genes in three Burkholderia species of different survival
RT   strategies.";
RL   BMC Genomics 6:174-174(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABC34619.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000085; ABC34619.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_025404166.1; NZ_CP008786.1.
DR   AlphaFoldDB; Q2T708; -.
DR   SMR; Q2T708; -.
DR   PRIDE; Q2T708; -.
DR   EnsemblBacteria; ABC34619; ABC34619; BTH_II0844.
DR   KEGG; bte:BTH_II0844; -.
DR   HOGENOM; CLU_893331_0_0_4; -.
DR   OrthoDB; 866539at2; -.
DR   Proteomes; UP000001930; 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_0000344010"
FT   COILED          127..171
FT                   /evidence="ECO:0000255"
FT   COILED          250..299
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   310 AA;  33727 MW;  2598042444F6B769 CRC64;
     MNVQVDMGRA LAARDWRAVA ALAVAMPAHA GAGTITDDDL RAAGVDRRVP EQKLGATIDE
     FASVRLPEQI DGEFVEGRRA NLAVFDDARV AVRSHALAQR NLLERWETEH LGGTLDAAGS
     GGGIQPDPIL QQLVDVIAQG KSDVDAYATI VEGLTKYFQS VADVMSKLQD YISAKDDKNM
     KIDGGKIKAL IQQVIDNLPK MQLPKGADIA RWRKELGDAV SISDSGVVTI NPDKLIKMRD
     SLPPDGTVWD TARYQAWNTA FSGQKDNIQN DVQTLVEKYS HQNSNFDNLV KVLSGAISTL
     TDTAKSYLQI