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Protein

Translocator protein BipD

Gene

bipD

Organism
Burkholderia pseudomallei (strain K96243)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Required for invasion of epithelial cells, as well as for survival within host cells, escape from endocytic vesicles and subsequent actin-tail formation. Probably regulates the secretion of effectors BipB and BipC and their final integration into the target cell membrane.2 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Virulence

Enzyme and pathway databases

BioCyciBPSE272560:GJNI-5097-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Translocator protein BipD
Gene namesi
Name:bipD
Ordered Locus Names:BPSS1529
OrganismiBurkholderia pseudomallei (strain K96243)
Taxonomic identifieri272560 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
Proteomesi
  • UP000000605 Componenti: Chromosome 2

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 310310Translocator protein BipDPRO_0000344009Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi272560.BPSS1529.

Structurei

Secondary structure

1
310
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi37 – 426Combined sources
Helixi48 – 6316Combined sources
Beta strandi68 – 703Combined sources
Beta strandi73 – 753Combined sources
Helixi83 – 11028Combined sources
Beta strandi122 – 1254Combined sources
Helixi128 – 16740Combined sources
Helixi168 – 1714Combined sources
Beta strandi172 – 1754Combined sources
Turni176 – 1783Combined sources
Beta strandi179 – 1824Combined sources
Helixi184 – 19613Combined sources
Beta strandi200 – 2023Combined sources
Helixi209 – 2168Combined sources
Beta strandi220 – 2223Combined sources
Beta strandi227 – 2304Combined sources
Helixi233 – 2408Combined sources
Beta strandi247 – 2504Combined sources
Helixi251 – 30252Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IXRX-ray2.60A10-310[»]
2IZPX-ray2.10A/B8-310[»]
2J9TX-ray2.70A/B10-310[»]
3NFTX-ray1.51A10-310[»]
ProteinModelPortaliQ63K37.
SMRiQ63K37. Positions 30-301.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ63K37.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili127 – 17145Sequence analysisAdd
BLAST
Coiled coili250 – 29950Sequence analysisAdd
BLAST

Domaini

The N-terminal domain is an intra-molecular chaperone that prevents premature oligomerization of the residues on the coiled-coil region that are involved in interactions with the needle and/or itself. The residues in the C-terminal domain probably form oligomeric structures at the tip of the needle that are responsible for the regulation of secretion of other effectors.

Sequence similaritiesi

Belongs to the invasin protein D family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

HOGENOMiHOG000280678.
KOiK13287.
OMAiERWETEH.
OrthoDBiEOG6JQGZG.

Family and domain databases

InterProiIPR009483. Plasmid_invsIpaD.
IPR013386. T3SS_IpaD/SipD/SspD.
[Graphical view]
PfamiPF06511. IpaD. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02553. SipD_IpaD_SspD. 1 hit.

Sequencei

Sequence statusi: Complete.

Q63K37-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNMHVDMGRA LTVRDWPALE ALAKTMPADA GARAMTDDDL RAAGVDRRVP
60 70 80 90 100
EQKLGAAIDE FASLRLPDRI DGRFVDGRRA NLTVFDDARV AVRGHARAQR
110 120 130 140 150
NLLERLETEL LGGTLDTAGD EGGIQPDPIL QGLVDVIGQG KSDIDAYATI
160 170 180 190 200
VEGLTKYFQS VADVMSKLQD YISAKDDKNM KIDGGKIKAL IQQVIDHLPT
210 220 230 240 250
MQLPKGADIA RWRKELGDAV SISDSGVVTI NPDKLIKMRD SLPPDGTVWD
260 270 280 290 300
TARYQAWNTA FSGQKDNIQN DVQTLVEKYS HQNSNFDNLV KVLSGAISTL
310
TDTAKSYLQI
Length:310
Mass (Da):33,975
Last modified:October 25, 2004 - v1
Checksum:iD6C446F4D919069D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341A → E in ABL67521 (Ref. 1) Curated
Sequence conflicti292 – 2921V → M in ABL67521 (Ref. 1) Curated
Sequence conflicti303 – 3031T → A in ABL67521 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF120623 Genomic DNA. Translation: ABL67521.1.
BX571966 Genomic DNA. Translation: CAH39002.1.
RefSeqiWP_004188590.1. NZ_CP009537.1.
YP_111535.1. NC_006351.1.

Genome annotation databases

EnsemblBacteriaiCAH39002; CAH39002; BPSS1529.
GeneIDi3096115.
KEGGibps:BPSS1529.
PATRICi19271232. VBIBurPse99623_5786.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF120623 Genomic DNA. Translation: ABL67521.1.
BX571966 Genomic DNA. Translation: CAH39002.1.
RefSeqiWP_004188590.1. NZ_CP009537.1.
YP_111535.1. NC_006351.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IXRX-ray2.60A10-310[»]
2IZPX-ray2.10A/B8-310[»]
2J9TX-ray2.70A/B10-310[»]
3NFTX-ray1.51A10-310[»]
ProteinModelPortaliQ63K37.
SMRiQ63K37. Positions 30-301.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272560.BPSS1529.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAH39002; CAH39002; BPSS1529.
GeneIDi3096115.
KEGGibps:BPSS1529.
PATRICi19271232. VBIBurPse99623_5786.

Phylogenomic databases

HOGENOMiHOG000280678.
KOiK13287.
OMAiERWETEH.
OrthoDBiEOG6JQGZG.

Enzyme and pathway databases

BioCyciBPSE272560:GJNI-5097-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ63K37.

Family and domain databases

InterProiIPR009483. Plasmid_invsIpaD.
IPR013386. T3SS_IpaD/SipD/SspD.
[Graphical view]
PfamiPF06511. IpaD. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02553. SipD_IpaD_SspD. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Chotigeat W., Visutthi M., Jitsurong S.
    Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K96243.
  3. "An Inv/Mxi-Spa-like type III protein secretion system in Burkholderia pseudomallei modulates intracellular behaviour of the pathogen."
    Stevens M.P., Wood M.W., Taylor L.A., Monaghan P., Hawes P., Jones P.W., Wallis T.S., Galyov E.E.
    Mol. Microbiol. 46:649-659(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE IN LYSIS OF HOST VACUOLES.
    Strain: 10276.
  4. "Attenuated virulence and protective efficacy of a Burkholderia pseudomallei bsa type III secretion mutant in murine models of melioidosis."
    Stevens M.P., Haque A., Atkins T., Hill J., Wood M.W., Easton A., Nelson M., Underwood-Fowler C., Titball R.W., Bancroft G.J., Galyov E.E.
    Microbiology 150:2669-2676(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE IN VIRULENCE, SUBCELLULAR LOCATION.
    Strain: 576.
  5. "A live experimental vaccine against Burkholderia pseudomallei elicits CD4+ T cell-mediated immunity, priming T cells specific for 2 type III secretion system proteins."
    Haque A., Chu K., Easton A., Stevens M.P., Galyov E.E., Atkins T., Titball R., Bancroft G.J.
    J. Infect. Dis. 194:1241-1248(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IMMUNOGENICITY.
    Strain: 576.
  6. Cited for: IMMUNOGENICITY.
  7. "High resolution structure of BipD: an invasion protein associated with the type III secretion system of Burkholderia pseudomallei."
    Erskine P.T., Knight M.J., Ruaux A., Mikolajek H., Wong Fat Sang N., Withers J., Gill R., Wood S.P., Wood M., Fox G.C., Cooper J.B.
    J. Mol. Biol. 363:125-136(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 8-310.
  8. Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 8-310, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiBIPD_BURPS
AccessioniPrimary (citable) accession number: Q63K37
Secondary accession number(s): A1EC20
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: October 25, 2004
Last modified: November 11, 2015
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Human meliodoisis patients have detectable antibody response to BipD. However, BipD does not act as a protective antigen.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.