BIPB_BURTA
ID BIPB_BURTA Reviewed; 624 AA.
AC Q2T711;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Translocator protein BipB;
GN Name=bipB; OrderedLocusNames=BTH_II0841;
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: 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; CP000085; ABC34967.1; -; Genomic_DNA.
DR RefSeq; WP_011401047.1; NZ_CP008786.1.
DR AlphaFoldDB; Q2T711; -.
DR SMR; Q2T711; -.
DR PRIDE; Q2T711; -.
DR EnsemblBacteria; ABC34967; ABC34967; BTH_II0841.
DR KEGG; bte:BTH_II0841; -.
DR HOGENOM; CLU_027418_0_0_4; -.
DR OMA; KFASHSI; -.
DR OrthoDB; 483748at2; -.
DR Proteomes; UP000001930; 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..624
FT /note="Translocator protein BipB"
FT /id="PRO_0000343994"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 54..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 313..343
FT /evidence="ECO:0000255"
FT COMPBIAS 64..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 624 AA; 65044 MW; EF362C3A437D47E4 CRC64;
MSSGVQGGSA ANANAYQTHP LRDAASALGT LSPQAYVDVV SAAQRNFLER MSRLASEQCD
AQPVTDDARL DRLDDKPALR APRSDAAHAA DGNARGNGGA SGAAKLTELL GVLMSVISAS
SLDELRQRSD IWNQMSKAAQ DNLTSLSDKF QCATDDAKAA TDAAERAAAA AKQAAADAKA
ADAAADAAQK RYDDAMKQGL PDDQLKTLQA ALEQAKQQAG DAHARADALQ ADAAGKLDAA
TALATQAREW EQQIDDAVNQ ASRQYGASAS LRTPPSPKLS GAAELTAVLG KLQELISSGN
VKELESKQKL FTEMQAKREA ELQKKSDEYQ EQVKKAEEMQ KTMGCIGKIV GWVITAVSFA
AAAFTGGASL ALAAVGLALA VGDEISRATT GVSFMDKLMQ PVMDAILKPL MEVISSLITK
ALVACGVDQQ KAELAGAILG AVVTGVALVA AAFVGASAVK AVASKVIDAV AGQLTKLMDS
AIGKMLVQLI EKFSEKSGLQ ALGSRTATAM TRMRRAIGVE AKEDGMLLAN RFEKAGTVMN
VGNQVSQAAG GIVVGVERAK AMGLLADVKE AMYDIKLLGD LLKQAVESFA EHNRALAQLM
QQMSDAGEMQ TATGKLILRN ARAV