BPAC_BURMA
ID BPAC_BURMA Reviewed; 1012 AA.
AC A0A0H2WHF1;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 30.
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:24731253};
GN OrderedLocusNames=BMA1027 {ECO:0000312|EMBL:AAU48866.1};
OS Burkholderia mallei (strain ATCC 23344).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=243160;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23344;
RX PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C.,
RA Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S.,
RA Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y.,
RA Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C.,
RA Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
RT "Structural flexibility in the Burkholderia mallei genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
RN [2]
RP FUNCTION IN ADHERENCE, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 23344;
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. Mediates adherence to human
CC respiratory epithelial cells. {ECO:0000269|PubMed:24731253}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P0C2W0}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000250|UniProtKB:A0A0H3HIJ5}.
CC Cell 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:0000250|UniProtKB:A0A0H3HIJ5}.
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: Inactivation of the gene substantially reduces
CC adherence to monolayers of HEp-2 laryngeal cells and A549 type II
CC pneumocytes, as well as to cultures of normal human bronchial
CC epithelium (NHBE). Mutation does not affect the virulence in a mouse
CC model of aerosol infection. {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; CP000010; AAU48866.1; -; Genomic_DNA.
DR RefSeq; WP_004197781.1; NC_006348.1.
DR RefSeq; YP_102734.1; NC_006348.1.
DR AlphaFoldDB; A0A0H2WHF1; -.
DR SMR; A0A0H2WHF1; -.
DR STRING; 243160.BMA1027; -.
DR EnsemblBacteria; AAU48866; AAU48866; BMA1027.
DR KEGG; bma:BMA1027; -.
DR PATRIC; fig|243160.12.peg.1065; -.
DR eggNOG; COG5295; Bacteria.
DR HOGENOM; CLU_309441_0_0_4; -.
DR OMA; FDGMWHS; -.
DR Proteomes; UP000006693; 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; -; 6.
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; 12.
DR Pfam; PF05662; YadA_stalk; 4.
DR SUPFAM; SSF101967; SSF101967; 4.
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"
FT CHAIN 72..1012
FT /note="Autotransporter adhesin BpaC"
FT /id="PRO_0000446521"
FT REGION 72..921
FT /note="Surface exposed passenger domain"
FT /evidence="ECO:0000250|UniProtKB:P0C2W0"
FT REGION 420..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..959
FT /note="Outer membrane translocation of the passenger
FT domain"
FT /evidence="ECO:0000250|UniProtKB:P0C2W0"
FT REGION 960..1012
FT /note="Translocator domain"
FT /evidence="ECO:0000250|UniProtKB:P0C2W0"
FT COMPBIAS 785..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1012 AA; 94759 MW; 53C27D16C62FBBDE CRC64;
MNRIFKSIWC EQTRTWVAAS EHAVARGGRA SSVVASAGGL EKVLKLSILG AASLIAMGVV
GPFAEEAMAA NNAGVCLTYN GSSNNTSGTG GWFADGCKSA GWVQGMVTNS KTDWVGLTAD
DTQIVLDGSA GSIYFRTGGI NGNVLTMSNA TGGVLLSGLA AGVNPTDAVN MSQLTSLSTS
TATGITSLST STATSIASLS TSMLSLGVGV VTQDASSGAI SVGANSPGLT VDFAGGQGPR
TLTGVAAGVN ATDAVNVGQL ASLSTSTAAG LSTAASGVAS LSTSLLGAAG DLASLSTSAS
TGLATADSGI ASLSTSLLGT ADNVTSLSTS LSTVNANLAG LQTSVDNVVS YDDPSKSAIT
LGGAGVATPV LLTNVAAGKI AATSTDAVNG SQLYTLQQEF SQQYDLLTSQ VSSLSTSVSG
LQGSVSANTG TASGDNSTAS GDNATASGTN STANGTNSTA SGDNSTASGT NASASGENST
ATGTDSTASG SNSTANGTNS TASGDNSTAS GTNASATGEN STATGTDSTA SGSNSTANGT
NSTASGDSST ASGTNASATG ENSTATGTDS TASGSNSTAN GTNSTASGDN STASGTNASA
TGENSTATGT DSTASGSNST ANGTNSTASG DNSTASGTNA SATGENSTAT GTDSTASGSN
STANGANSTA SGENSTATGT DSTASGSNST ANGTNSTASG DNSTASGTNA SATGENSTAT
GTASTASGSN STANGANSTA SGAGATATGE NAAATGAGAT ATGNNASASG TSSTAGGANA
IASGENSTAN GANSTASGNG SSAFGESAAA AGDGSTALGA NAVASGVGSV ATGAGSVASG
ANSSAYGTGS NATGAGSVAI GQGATASGSN SVALGTGSVA SEDNTVSVGS AGSERRITNV
AAGVNATDAV NVGQLNSAVS GIRNQMDGMQ GQIDTLARDA YSGIAAATAL TMIPDVDPGK
TLAVGIGTAN FKGYQASALG ATARITQNLK VKTGVSYSGS NYVWGAGMSY QW
