BIPB_BURPS
ID BIPB_BURPS Reviewed; 620 AA.
AC Q63K34;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Translocator protein BipB;
GN Name=bipB; OrderedLocusNames=BPSS1532;
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], AND IMMUNOGENICITY.
RC STRAIN=K96243, PHLS 40, PHLS 79, PHLS 91, and S13;
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 [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 FUNCTION IN THE INDUCTION OF HOST MEMBRANE FUSION.
RC STRAIN=K96243;
RX PubMed=16159789; DOI=10.1128/jb.187.18.6556-6560.2005;
RA Suparak S., Kespichayawattana W., Haque A., Easton A., Damnin S.,
RA Lertmemongkolchai G., Bancroft G.J., Korbsrisate S.;
RT "Multinucleated giant cell formation and apoptosis in infected host cells
RT is mediated by Burkholderia pseudomallei type III secretion protein BipB.";
RL J. Bacteriol. 187:6556-6560(2005).
CC -!- FUNCTION: Plays a role in the bacterium-induced formation of
CC multinucleated giant cell (MNGC), which is formed after host cell
CC fusion, as well as in the intercellular spreading of bacteria and in
CC the induction of apoptosis in macrophages. May act in concert with
CC other effector proteins to induce fusion of host cell membranes.
CC {ECO:0000269|PubMed:16159789}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Host membrane
CC {ECO:0000305}. Note=Secreted via the bsa type III secretion system, and
CC probably inserted into host membranes.
CC -!- MISCELLANEOUS: Human meliodoisis patients have detectable antibody
CC response to BipB. However, BipB does not act as a protective antigen.
CC -!- SIMILARITY: Belongs to the invasin protein B family. {ECO:0000305}.
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DR EMBL; EF428328; ABO26346.1; -; Genomic_DNA.
DR EMBL; EF428329; ABO26348.1; -; Genomic_DNA.
DR EMBL; EF428332; ABO26354.1; -; Genomic_DNA.
DR EMBL; EF436253; ABO28812.1; -; Genomic_DNA.
DR EMBL; EF436254; ABO28814.1; -; Genomic_DNA.
DR EMBL; BX571966; CAH39005.1; -; Genomic_DNA.
DR RefSeq; WP_004533397.1; NZ_CP009537.1.
DR RefSeq; YP_111538.1; NC_006351.1.
DR AlphaFoldDB; Q63K34; -.
DR SMR; Q63K34; -.
DR STRING; 272560.BPSS1532; -.
DR EnsemblBacteria; CAH39005; CAH39005; BPSS1532.
DR GeneID; 56597877; -.
DR KEGG; bps:BPSS1532; -.
DR PATRIC; fig|272560.51.peg.4887; -.
DR eggNOG; ENOG502ZBCB; Bacteria.
DR OMA; KFASHSI; -.
DR PHI-base; PHI:5322; -.
DR Proteomes; UP000000605; Chromosome 2.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR032391; SipB_N.
DR InterPro; IPR006972; SseC.
DR InterPro; IPR003895; T3SS_invasion_prot_B.
DR Pfam; PF04888; SseC; 1.
DR Pfam; PF16535; T3SSipB; 1.
DR PRINTS; PR01375; BACINVASINB.
PE 1: Evidence at protein level;
KW Coiled coil; Host membrane; Membrane; Reference proteome; Secreted;
KW Transmembrane; Transmembrane helix; Virulence.
FT CHAIN 1..620
FT /note="Translocator protein BipB"
FT /id="PRO_0000343993"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 58..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 309..339
FT /evidence="ECO:0000255"
FT COMPBIAS 64..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 620 AA; 64680 MW; DCAFE3579309EFAC CRC64;
MSSGVQGGPA ANANAYQTHP LRDAASALGT LSPQAYVDVV SAAQRNFLER MSQLASEQCD
AQPAAHDARL DDRPALRAPQ ERDAPPLGAS DTGSRASGAA KLTELLGVLM SVISASSLDE
LKQRSDIWNQ MSKAAQDNLS RLSDAFQRAT DEAKAAADAA EQAAAAAKQA GADAKAADAA
VDAAQKRYDD AVKQGLPDDR LQSLKAALEQ ARQQAGDAHG RADALQADAT KKLDAASALA
TQARACEQQV DDAVNQATQQ YGASASLRTP QSPRLSGAAE LTAVLGKLQE LISSGNVKEL
ESKQKLFTEM QAKREAELQK KSDEYQAQVK KAEEMQKTMG CIGKIVGWVI TAVSFAAAAF
TGGASLALAA VGLALAVGDE ISRATTGVSF MDKLMQPVMD AILKPLMEMI SSLITKALVA
CGVDQQKAEL AGAILGAVVT GVALVAAAFV GASAVKAVAS KVIDAMAGQL TKLMDSAIGK
MLVQLIEKFS EKSGLQALGS RTATAMTRMR RAIGVEAKED GMLLANRFEK AGTVMNVGNQ
VSQAAGGIVV GVERAKAMGL LADVKEAMYD IKLLGDLLKQ AVDAFAEHNR VLAQLMQQMS
DAGEMQTSTG KLILRNARAV
