ID A4GV77_BURPE Unreviewed; 620 AA.
AC A4GV77;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Translocator protein BipB {ECO:0000256|ARBA:ARBA00018823};
GN Name=bipB {ECO:0000313|EMBL:ABO28808.1};
OS Burkholderia pseudomallei (Pseudomonas pseudomallei).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=28450 {ECO:0000313|EMBL:ABO28808.1};
RN [1] {ECO:0000313|EMBL:ABO28808.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=406e {ECO:0000313|EMBL:ABO28808.1};
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).
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:0000256|ARBA:ARBA00025490}.
CC -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000256|ARBA:ARBA00004551}.
CC Membrane {ECO:0000256|ARBA:ARBA00004370}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the SctE/SipB/YopB family.
CC {ECO:0000256|ARBA:ARBA00035640}.
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DR EMBL; EF436251; ABO28808.1; -; Genomic_DNA.
DR RefSeq; WP_004539442.1; NZ_UUXL01000086.1.
DR AlphaFoldDB; A4GV77; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 2.
DR InterPro; IPR006972; BipB-like_C.
DR InterPro; IPR032391; IpaB/BipB/SctE_N.
DR InterPro; IPR003895; T3SS_SctE/BipB.
DR Pfam; PF04888; SseC; 1.
DR Pfam; PF16535; T3SSipB; 1.
DR PRINTS; PR01375; BACINVASINB.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT TRANSMEM 345..377
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 430..452
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 99..261
FT /note="IpaB/BipB/SctE N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16535"
FT DOMAIN 286..616
FT /note="Translocator protein BipB-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04888"
FT REGION 58..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 118..228
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 64..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 620 AA; 64652 MW; F1AFE35120613C92 CRC64;
MSSGVQGGPA ANANAYQTHP LRDAASALGT LSPQAYVDVV SAAQRNFLER MSQLASEQCD
AQPAAHDARL DDKPALRAPQ 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
//
