BIPB_BURP6
ID BIPB_BURP6 Reviewed; 620 AA.
AC A3NLD5;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Translocator protein BipB;
GN Name=bipB; OrderedLocusNames=BURPS668_A2162;
OS Burkholderia pseudomallei (strain 668).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=320373;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=668;
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: 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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Host membrane
CC {ECO:0000250}. Note=Secreted via the bsa type III secretion system, and
CC probably inserted into host membranes. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the invasin protein B 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; CP000571; ABN86659.1; -; Genomic_DNA.
DR RefSeq; WP_011853456.1; NC_009075.1.
DR AlphaFoldDB; A3NLD5; -.
DR SMR; A3NLD5; -.
DR EnsemblBacteria; ABN86659; ABN86659; BURPS668_A2162.
DR KEGG; bpd:BURPS668_A2162; -.
DR HOGENOM; CLU_027418_0_0_4; -.
DR OMA; KFASHSI; -.
DR Proteomes; UP000002153; Chromosome II.
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 3: Inferred from homology;
KW Coiled coil; Host membrane; Membrane; Secreted; Transmembrane;
KW Transmembrane helix; Virulence.
FT CHAIN 1..620
FT /note="Translocator protein BipB"
FT /id="PRO_0000343992"
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; 64675 MW; 9C85629E3C24EC84 CRC64;
MSSGVQGGPA AHANAYQTHP LRDAASALGT LSPQAYVDVV SAAQRNFLER MSQLASEQCD
AQPAAHDARL DDRPALRAPQ ERDAPPLGAS DTGSRASGAA KLTELLGVLM SVISASSLDE
LKQRSDIWNQ MSKAAQDNLS RLSDAFQRAT DEAKAAADAA EQAAAAAKQA GADAKAADAA
VDAAQKRYDD AVKQGLPDDQ 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