BPAC_BURP2
ID BPAC_BURP2 Reviewed; 1152 AA.
AC A0A0H3HIJ5;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 25-MAY-2022, entry version 23.
DE RecName: Full=Autotransporter adhesin BpaC {ECO:0000305};
DE AltName: Full=Type 5 secretion system autotransporter BpaC {ECO:0000305};
DE Flags: Precursor;
GN Name=bpaC {ECO:0000303|PubMed:23716608};
GN OrderedLocusNames=BP1026B_I1575 {ECO:0000312|EMBL:AFI66204.1};
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 FUNCTION IN VIRULENCE, DOMAIN, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bp340 / 1026b;
RX PubMed=23716608; DOI=10.1128/iai.00526-13;
RA Campos C.G., Byrd M.S., Cotter P.A.;
RT "Functional characterization of Burkholderia pseudomallei trimeric
RT autotransporters.";
RL Infect. Immun. 81:2788-2799(2013).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DD503 / 1026b;
RX PubMed=24731253; DOI=10.1186/1471-2180-14-92;
RA Lafontaine E.R., Balder R., Michel F., Hogan R.J.;
RT "Characterization of an autotransporter adhesin protein shared by
RT Burkholderia mallei and Burkholderia pseudomallei.";
RL BMC Microbiol. 14:92-92(2014).
CC -!- FUNCTION: Involved in virulence (PubMed:23716608, PubMed:24731253).
CC Mediates adherence to human respiratory epithelial cells
CC (PubMed:24731253). {ECO:0000269|PubMed:23716608,
CC ECO:0000269|PubMed:24731253}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P0C2W0}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:24731253}. Cell
CC outer membrane {ECO:0000250|UniProtKB:P0C2W0}. Note=The C-terminal
CC translocator domain is localized in the outer membrane and the
CC passenger domain is at the cell surface.
CC {ECO:0000250|UniProtKB:P0C2W0}.
CC -!- INDUCTION: Expressed in vivo during the course of aerosol infection.
CC Expressed at very low levels under routine laboratory growth
CC conditions. {ECO:0000269|PubMed:24731253}.
CC -!- DOMAIN: Contains a well-conserved 23 amino acid extended signal peptide
CC region (ESPR) preceding a typical N-terminal signal sequence. ESPR
CC region may be involved in regulating the translocation of the
CC autotransporter across the inner membrane into the periplasm.
CC {ECO:0000305|PubMed:23716608}.
CC -!- DOMAIN: The signal peptide, cleaved at the inner membrane, guides the
CC autotransporter protein to the periplasmic space. Then, insertion of
CC the C-terminal translocator domain in the outer membrane forms a
CC hydrophilic pore for the translocation of the passenger domain to the
CC bacterial cell surface. {ECO:0000250|UniProtKB:P0C2W0}.
CC -!- DISRUPTION PHENOTYPE: Lafontaine et al. show that disruption of the
CC gene reduces adherence to cultures of normal human bronchial epithelium
CC (NHBE) but does not impair binding to HEp-2 laryngeal cells and A549
CC type II pneumocytes (PubMed:24731253). In contrast, Campos et al. show
CC that disruption of the gene decreases adherence to A549 cells and
CC attenuates the ability of the bacteria to invade A549 cells
CC (PubMed:23716608). Mutant does not show a plaque formation defect
CC (PubMed:23716608). Mutation reduces the ability to disseminate and/or
CC survive within the liver in a mouse model of infection
CC (PubMed:23716608). Mutation does not affect the virulence in a mouse
CC model of aerosol infection (PubMed:24731253).
CC {ECO:0000269|PubMed:23716608, ECO:0000269|PubMed:24731253}.
CC -!- SIMILARITY: Belongs to the autotransporter-2 (AT-2) (TC 1.B.40) family.
CC {ECO:0000305}.
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DR EMBL; CP002833; AFI66204.1; -; Genomic_DNA.
DR RefSeq; WP_014696818.1; NZ_CP004379.1.
DR AlphaFoldDB; A0A0H3HIJ5; -.
DR SMR; A0A0H3HIJ5; -.
DR EnsemblBacteria; AFI66204; AFI66204; BP1026B_I1575.
DR KEGG; bpz:BP1026B_I1575; -.
DR PATRIC; fig|884204.3.peg.1749; -.
DR Proteomes; UP000010087; Chromosome 1.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.150.10.10; -; 8.
DR InterPro; IPR008640; Adhesin_Head_dom.
DR InterPro; IPR008635; Coiled_stalk_dom.
DR InterPro; IPR024973; ESPR.
DR InterPro; IPR045584; Pilin-like.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR InterPro; IPR005594; YadA_C.
DR Pfam; PF13018; ESPR; 1.
DR Pfam; PF03895; YadA_anchor; 1.
DR Pfam; PF05658; YadA_head; 14.
DR Pfam; PF05662; YadA_stalk; 4.
DR SUPFAM; SSF101967; SSF101967; 5.
DR SUPFAM; SSF54523; SSF54523; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell outer membrane; Membrane; Protein transport; Signal;
KW Transmembrane; Transmembrane beta strand; Transport; Virulence.
FT SIGNAL 1..71
FT /evidence="ECO:0000305|PubMed:23716608"
FT CHAIN 72..1152
FT /note="Autotransporter adhesin BpaC"
FT /id="PRO_0000446522"
FT REGION 72..1061
FT /note="Surface exposed passenger domain"
FT /evidence="ECO:0000250|UniProtKB:P0C2W0"
FT REGION 420..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 900..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1062..1099
FT /note="Outer membrane translocation of the passenger
FT domain"
FT /evidence="ECO:0000250|UniProtKB:P0C2W0"
FT REGION 1100..1152
FT /note="Translocator domain"
FT /evidence="ECO:0000250|UniProtKB:P0C2W0"
FT COMPBIAS 900..944
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1152 AA; 107389 MW; 51A091BB054638CF CRC64;
MNRIFKSIWC EQTRTWVAAS EHAVARGGRA SSVVASAGGL EKVLKLSILG AASLIAMGVV
GPFAEEAMAA NNAGVCLTYN GSSNNTSGTG GWFADGCKSA GWVQGMVTNS KTDWVGLTAD
DTQIVLDGSA GSIYFRTGGI NGNVLTMSNA TGGVLLSGLA AGVNPTDAVN MSQLTSLSTS
TATGITSLST STATSIASLS TSMLSLGVGV VTQDASTGAI SVGANSPGLT VDFAGGQGPR
TLTGVAAGVN ATDAVNVGQL ASLSTSTAAG LSTAASGVAS LSTSLLGAVG DLASLSTSAS
TGLATADSGI ASLSTSLLGT ADNVTSLSTS LSTVNANLAG LQTSVDNVVS YDDPSKSAIT
LGGAGVTTPV LLTNVAAGKI AATSTDAVNG SQLYTLQQEF SQQYDLLTSQ VSSLSTSVSG
LQGSVSANTG TASGDNSTAS GDNATASGTN STANGTNSTA SGDNSTASGT NASASGENST
ATGTDSTASG SNSTANGTNS TASGDNSTAS GTNASATGEN STATGTDSTA SGSNSTANGT
NSTASGDNST ASGTNASASG ENSTATGTDS TASGSNSTAN GTNSTASGDN STASGTNASA
TGENSTATGT DSTASGSNST ANGTNSTASG DNSTASGTNA SATGENSTAT GTDSTASGSN
STANGTNSTA SGDNSTASGT NASATGENST ATGTDSTASG SNSTANGTNS TASGDNSTAS
GTNASATGEN STATGTDSTA SGSNSTANGA NSTASGDNST ASGTNASATG ENSTATGTDS
TASGSNSTAN GTNSTASGNN STASGTNASA TGENSTATGT DSAASGTNST ANGTNSTASG
DNSTASGTNA SATGENSTAT GTASTASGSN STANGANSTA SGAGATATGE NAAATGAGAT
ATGNNASASG TSSTAGGANA IASGENSTTN GANSTASGNG SSAFGESAAA AGDGSTALGA
NAVASGVGSV ATGAGSVASG ANSSAYGTGS NATGAGSVAI GQGATASGSN SVALGTGSVA
SEDNTVSVGS AGSERRITNV AAGVNATDAV NVGQLNSAVS GIRNQMDGMQ GQIDTLARDA
YSGIAAATAL TMIPDVDPGK TLAVGIGTAN FKGYQASALG ATARITQNLK VKTGVSYSGS
NYVWGAGMSY QW
