BSAZ_BURP2
ID BSAZ_BURP2 Reviewed; 411 AA.
AC I1WUC2;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Secretion apparatus protein BsaZ;
GN Name=bsaZ; OrderedLocusNames=BP1026B_II1630;
OS Burkholderia pseudomallei (strain 1026b).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=884204;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1026b;
RX PubMed=22615773; DOI=10.1371/journal.pone.0036507;
RA Hayden H.S., Lim R., Brittnacher M.J., Sims E.H., Ramage E.R., Fong C.,
RA Wu Z., Crist E., Chang J., Zhou Y., Radey M., Rohmer L., Haugen E.,
RA Gillett W., Wuthiekanun V., Peacock S.J., Kaul R., Miller S.I., Manoil C.,
RA Jacobs M.A.;
RT "Evolution of Burkholderia pseudomallei in recurrent melioidosis.";
RL PLoS ONE 7:E36507-E36507(2012).
RN [2]
RP ROLE IN ESCAPE FROM VACUOLES.
RC STRAIN=1026b;
RX PubMed=18443088; DOI=10.1128/iai.00263-08;
RA Burtnick M.N., Brett P.J., Nair V., Warawa J.M., Woods D.E.,
RA Gherardini F.C.;
RT "Burkholderia pseudomallei type III secretion system mutants exhibit
RT delayed vacuolar escape phenotypes in RAW 264.7 murine macrophages.";
RL Infect. Immun. 76:2991-3000(2008).
CC -!- FUNCTION: Part of the bsa type III secretion system, is involved in the
CC intracellular replication of invading bacteria inside the host cell.
CC Probably necessary for the lysis of the vacuole membrane and escape
CC into the host cell cytoplasm. {ECO:0000269|PubMed:18443088}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the type III secretion exporter family.
CC {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; CP002834; AFI69866.1; -; Genomic_DNA.
DR RefSeq; WP_004530588.1; NZ_CP004380.1.
DR AlphaFoldDB; I1WUC2; -.
DR SMR; I1WUC2; -.
DR EnsemblBacteria; AFI69866; AFI69866; BP1026B_II1630.
DR KEGG; bpz:BP1026B_II1630; -.
DR PATRIC; fig|884204.3.peg.6016; -.
DR Proteomes; UP000010087; Chromosome 2.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009306; P:protein secretion; IEA:InterPro.
DR Gene3D; 3.40.1690.10; -; 1.
DR InterPro; IPR006307; BsaZ.
DR InterPro; IPR006135; T3SS_substrate_exporter.
DR InterPro; IPR029025; T3SS_substrate_exporter_C.
DR PANTHER; PTHR30531; PTHR30531; 1.
DR Pfam; PF01312; Bac_export_2; 1.
DR PRINTS; PR00950; TYPE3IMSPROT.
DR SUPFAM; SSF160544; SSF160544; 1.
DR TIGRFAMs; TIGR01404; FlhB_rel_III; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Transmembrane; Transmembrane helix; Virulence.
FT CHAIN 1..411
FT /note="Secretion apparatus protein BsaZ"
FT /id="PRO_0000429785"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 341..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 411 AA; 44400 MW; 3E2EDCFA2830C92F CRC64;
MAEKTEKPTA KKLRDAAKKG QTFKARDIVA LIVIATGALA APALVDLTRI AAEFVRIAST
GAQPNPGAYA FAWAKLFLRI AAPFVLLCAA AGALPSLVQS RFTLAVESIR FDLTALDPVK
GMKRLFSWRS AKDAVKALLY VGVFALTVRV FAGLYHADVF GLFRARPALL GHMWIVLTVR
LVLLFLLCAL PVLILDAAVE YFLYHRELKM DKHEVKQEYK ESEGNHEIKS KRREIHQELL
SEEIKANVEQ SDFIVANPTH IAIGVYVNPD IVPIPFVSVR ETNARALAVI RHAEACGVPV
VRNVALARSI YRNSPRRYSF VSHDDIDGVM RVLIWLGEVE AANRGGPPPE TRAPTSAEPQ
ARDGVAPPGD ACADNAFPDD APPGAAAPNA GSPDGPAPDG GAPARTGDQN A