BIPD_BURPS
ID BIPD_BURPS Reviewed; 310 AA.
AC Q63K37; A1EC20;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Translocator protein BipD;
GN Name=bipD; OrderedLocusNames=BPSS1529;
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Chotigeat W., Visutthi M., Jitsurong S.;
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243;
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
RN [3]
RP ROLE IN LYSIS OF HOST VACUOLES.
RC STRAIN=10276;
RX PubMed=12410823; DOI=10.1046/j.1365-2958.2002.03190.x;
RA Stevens M.P., Wood M.W., Taylor L.A., Monaghan P., Hawes P., Jones P.W.,
RA Wallis T.S., Galyov E.E.;
RT "An Inv/Mxi-Spa-like type III protein secretion system in Burkholderia
RT pseudomallei modulates intracellular behaviour of the pathogen.";
RL Mol. Microbiol. 46:649-659(2002).
RN [4]
RP ROLE IN VIRULENCE, AND SUBCELLULAR LOCATION.
RC STRAIN=576;
RX PubMed=15289563; DOI=10.1099/mic.0.27146-0;
RA Stevens M.P., Haque A., Atkins T., Hill J., Wood M.W., Easton A.,
RA Nelson M., Underwood-Fowler C., Titball R.W., Bancroft G.J., Galyov E.E.;
RT "Attenuated virulence and protective efficacy of a Burkholderia
RT pseudomallei bsa type III secretion mutant in murine models of
RT melioidosis.";
RL Microbiology 150:2669-2676(2004).
RN [5]
RP IMMUNOGENICITY.
RC STRAIN=576;
RX PubMed=17041850; DOI=10.1086/508217;
RA Haque A., Chu K., Easton A., Stevens M.P., Galyov E.E., Atkins T.,
RA Titball R., Bancroft G.J.;
RT "A live experimental vaccine against Burkholderia pseudomallei elicits CD4+
RT T cell-mediated immunity, priming T cells specific for 2 type III secretion
RT system proteins.";
RL J. Infect. Dis. 194:1241-1248(2006).
RN [6]
RP IMMUNOGENICITY.
RX PubMed=17995960; DOI=10.1111/j.1574-695x.2007.00345.x;
RA Druar C., Yu F., Barnes J.L., Okinaka R.T., Chantratita N., Beg S.,
RA Stratilo C.W., Olive A.J., Soltes G., Russell M.L., Limmathurotsakul D.,
RA Norton R.E., Ni S.X., Picking W.D., Jackson P.J., Stewart D.I.H.,
RA Tsvetnitsky V., Picking W.L., Cherwonogrodzky J.W., Ketheesan N.,
RA Peacock S.J., Wiersma E.J.;
RT "Evaluating Burkholderia pseudomallei Bip proteins as vaccines and Bip
RT antibodies as detection agents.";
RL FEMS Immunol. Med. Microbiol. 52:78-87(2008).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 8-310.
RX PubMed=16950399; DOI=10.1016/j.jmb.2006.07.069;
RA Erskine P.T., Knight M.J., Ruaux A., Mikolajek H., Wong Fat Sang N.,
RA Withers J., Gill R., Wood S.P., Wood M., Fox G.C., Cooper J.B.;
RT "High resolution structure of BipD: an invasion protein associated with the
RT type III secretion system of Burkholderia pseudomallei.";
RL J. Mol. Biol. 363:125-136(2006).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 8-310, AND SUBCELLULAR LOCATION.
RX PubMed=17077085; DOI=10.1074/jbc.m607945200;
RA Johnson S., Roversi P., Espina M., Olive A., Deane J.E., Birket S.,
RA Field T., Picking W.D., Blocker A.J., Galyov E.E., Picking W.L., Lea S.M.;
RT "Self-chaperoning of the type III secretion system needle tip proteins IpaD
RT and BipD.";
RL J. Biol. Chem. 282:4035-4044(2007).
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. {ECO:0000269|PubMed:12410823,
CC ECO:0000269|PubMed:15289563}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15289563,
CC ECO:0000269|PubMed:17077085}. Note=Secreted via the bsa type III
CC secretion system. Localizes to the tip of the external secretion needle
CC that is part of the secretion apparatus.
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.
CC -!- MISCELLANEOUS: Human meliodoisis patients have detectable antibody
CC response to BipD. However, BipD does not act as a protective antigen.
CC -!- SIMILARITY: Belongs to the invasin protein D family. {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; EF120623; ABL67521.1; -; Genomic_DNA.
DR EMBL; BX571966; CAH39002.1; -; Genomic_DNA.
DR RefSeq; WP_004188590.1; NZ_CP009537.1.
DR RefSeq; YP_111535.1; NC_006351.1.
DR PDB; 2IXR; X-ray; 2.60 A; A=10-310.
DR PDB; 2IZP; X-ray; 2.10 A; A/B=8-310.
DR PDB; 2J9T; X-ray; 2.70 A; A/B=10-310.
DR PDB; 3NFT; X-ray; 1.51 A; A=10-310.
DR PDBsum; 2IXR; -.
DR PDBsum; 2IZP; -.
DR PDBsum; 2J9T; -.
DR PDBsum; 3NFT; -.
DR AlphaFoldDB; Q63K37; -.
DR SMR; Q63K37; -.
DR STRING; 272560.BPSS1529; -.
DR EnsemblBacteria; CAH39002; CAH39002; BPSS1529.
DR GeneID; 56597874; -.
DR KEGG; bps:BPSS1529; -.
DR PATRIC; fig|272560.51.peg.4884; -.
DR eggNOG; ENOG5032RHE; Bacteria.
DR OMA; ERWETEH; -.
DR EvolutionaryTrace; Q63K37; -.
DR Proteomes; UP000000605; Chromosome 2.
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 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Reference proteome; Secreted; Virulence.
FT CHAIN 1..310
FT /note="Translocator protein BipD"
FT /id="PRO_0000344009"
FT COILED 127..171
FT /evidence="ECO:0000255"
FT COILED 250..299
FT /evidence="ECO:0000255"
FT CONFLICT 34
FT /note="A -> E (in Ref. 1; ABL67521)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="V -> M (in Ref. 1; ABL67521)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="T -> A (in Ref. 1; ABL67521)"
FT /evidence="ECO:0000305"
FT HELIX 37..42
FT /evidence="ECO:0007829|PDB:3NFT"
FT HELIX 48..63
FT /evidence="ECO:0007829|PDB:3NFT"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:3NFT"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:3NFT"
FT HELIX 83..110
FT /evidence="ECO:0007829|PDB:3NFT"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:2IZP"
FT HELIX 128..167
FT /evidence="ECO:0007829|PDB:3NFT"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:3NFT"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:3NFT"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:3NFT"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:3NFT"
FT HELIX 184..196
FT /evidence="ECO:0007829|PDB:3NFT"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:3NFT"
FT HELIX 209..216
FT /evidence="ECO:0007829|PDB:3NFT"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:3NFT"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:3NFT"
FT HELIX 233..240
FT /evidence="ECO:0007829|PDB:3NFT"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:3NFT"
FT HELIX 251..302
FT /evidence="ECO:0007829|PDB:3NFT"
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
