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BrkA autotransporter [Cleaved into: Serum resistance protein BrkA; BrkA translocator]

 BRKA_BORPE              Reviewed;        1010 AA.
Q45340;
05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
10-OCT-2018, entry version 105.
RecName: Full=BrkA autotransporter;
Contains:
RecName: Full=Serum resistance protein BrkA;
Contains:
RecName: Full=BrkA translocator;
Flags: Precursor;
Name=brkA {ECO:0000303|PubMed:7927748}; OrderedLocusNames=BP3494;
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
Alcaligenaceae; Bordetella.
NCBI_TaxID=257313;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Tohama I / BP338;
PubMed=7927748;
Fernandez R.C., Weiss A.A.;
"Cloning and sequencing of a Bordetella pertussis serum resistance
locus.";
Infect. Immun. 62:4727-4738(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
PubMed=12910271; DOI=10.1038/ng1227;
Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
Chillingworth T., Collins M., Cronin A., Davis P., Doggett J.,
Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K.,
Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C.,
Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K.,
Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K.,
Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
"Comparative analysis of the genome sequences of Bordetella pertussis,
Bordetella parapertussis and Bordetella bronchiseptica.";
Nat. Genet. 35:32-40(2003).
[3]
PROTEIN SEQUENCE OF 43-47, SUBCELLULAR LOCATION, AND DOMAIN.
STRAIN=Tohama I / BP338;
PubMed=12511495; DOI=10.1128/JB.185.2.489-495.2003;
Oliver D.C., Huang G., Fernandez R.C.;
"Identification of secretion determinants of the Bordetella pertussis
BrkA autotransporter.";
J. Bacteriol. 185:489-495(2003).
[4]
PROTEIN SEQUENCE OF 732-743, AND CLEAVAGE SITE.
STRAIN=Tohama I / BP338;
PubMed=10079522; DOI=10.1111/j.1574-6968.1999.tb13442.x;
Passerini de Rossi B.N., Friedman L.E., Gonzalez Flecha F.L.,
Castello P.R., Franco M.A., Rossi J.P.F.C.;
"Identification of Bordetella pertussis virulence-associated outer
membrane proteins.";
FEMS Microbiol. Lett. 172:9-13(1999).
[5]
PORE FORMATION, DOMAIN, AND SUBCELLULAR LOCATION.
PubMed=10482528;
Shannon J.L., Fernandez R.C.;
"The C-terminal domain of the Bordetella pertussis autotransporter
BrkA forms a pore in lipid bilayer membranes.";
J. Bacteriol. 181:5838-5842(1999).
[6]
FUNCTION.
STRAIN=Tohama I / BP338;
PubMed=11292725; DOI=10.1128/IAI.69.5.3067-3072.2001;
Barnes M.G., Weiss A.A.;
"BrkA protein of Bordetella pertussis inhibits the classical pathway
of complement after C1 deposition.";
Infect. Immun. 69:3067-3072(2001).
[7]
CRYSTALLIZATION.
PubMed=19478443; DOI=10.1107/S174430910901642X;
Zhao L., Nguyen N.T., Fernandez R.C., Murphy M.E.;
"Crystallographic characterization of the passenger domain of the
Bordetella autotransporter BrkA.";
Acta Crystallogr. F 65:608-611(2009).
-!- FUNCTION: Inhibits the classical pathway of complement activation
and prevents accumulation of deposited C4.
{ECO:0000269|PubMed:11292725}.
-!- SUBCELLULAR LOCATION: BrkA autotransporter: Periplasm
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Serum resistance protein BrkA: Secreted
{ECO:0000269|PubMed:12511495}. Cell surface
{ECO:0000269|PubMed:12511495}.
-!- SUBCELLULAR LOCATION: BrkA translocator: Cell outer membrane
{ECO:0000269|PubMed:10482528}; Multi-pass membrane protein
{ECO:0000305}. Note=The cleaved C-terminal fragment
(autotransporter domain) is localized in the outer membrane.
{ECO:0000269|PubMed:10482528}.
-!- DOMAIN: The signal peptide, cleaved at the inner membrane, guides
the autotransporter protein to the periplasmic space. Then,
insertion of the C-terminal translocator domain in the outer
membrane forms a hydrophilic pore for the translocation of the
passenger domain to the bacterial cell surface, with subsequent
cleavage. Finally, the mature protein remains tightly associated
with the bacterium. {ECO:0000269|PubMed:10482528,
ECO:0000269|PubMed:12511495}.
-!- DOMAIN: A 31- to 39-amino-acid region found immediately upstream
of the translocator domain is essential for surface expression.
{ECO:0000269|PubMed:12511495}.
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EMBL; U12276; AAA51646.1; -; Genomic_DNA.
EMBL; BX640421; CAE43755.1; -; Genomic_DNA.
PIR; I40329; I40329.
RefSeq; NP_882013.1; NC_002929.2.
RefSeq; WP_010931506.1; NC_002929.2.
PDB; 3QQ2; X-ray; 3.00 A; A/B/C=727-1010.
PDBsum; 3QQ2; -.
ProteinModelPortal; Q45340; -.
SMR; Q45340; -.
STRING; 257313.BP3494; -.
TCDB; 1.B.12.2.3; the autotransporter-1 (at-1) family.
PRIDE; Q45340; -.
EnsemblBacteria; CAE43755; CAE43755; BP3494.
GeneID; 2664892; -.
KEGG; bpe:BP3494; -.
PATRIC; fig|257313.5.peg.3783; -.
eggNOG; ENOG4108P8G; Bacteria.
eggNOG; COG3468; LUCA.
KO; K12683; -.
OMA; NFEAGRF; -.
BioCyc; BPER257313:BP3494-MONOMER; -.
Proteomes; UP000002676; Chromosome.
GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
GO; GO:0007155; P:cell adhesion; IEA:InterPro.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
Gene3D; 2.160.20.20; -; 2.
Gene3D; 2.40.128.130; -; 1.
InterPro; IPR005546; Autotransporte_beta.
InterPro; IPR036709; Autotransporte_beta_dom_sf.
InterPro; IPR006315; OM_autotransptr_brl.
InterPro; IPR012332; P22_tailspike-like_C_sf.
InterPro; IPR011050; Pectin_lyase_fold/virulence.
InterPro; IPR004899; Pertactin_central.
InterPro; IPR003991; Pertactin_virulence_factor.
Pfam; PF03797; Autotransporter; 1.
Pfam; PF03212; Pertactin; 1.
PRINTS; PR01484; PRTACTNFAMLY.
SMART; SM00869; Autotransporter; 1.
SUPFAM; SSF103515; SSF103515; 1.
SUPFAM; SSF51126; SSF51126; 3.
TIGRFAMs; TIGR01414; autotrans_barl; 1.
PROSITE; PS51208; AUTOTRANSPORTER; 1.
1: Evidence at protein level;
3D-structure; Cell outer membrane; Complete proteome;
Direct protein sequencing; Membrane; Periplasm; Reference proteome;
Secreted; Signal; Transmembrane; Transmembrane beta strand; Virulence.
SIGNAL 1 42 {ECO:0000269|PubMed:12511495}.
CHAIN 43 1010 BrkA autotransporter.
/FTId=PRO_0000399092.
CHAIN 43 731 Serum resistance protein BrkA.
/FTId=PRO_0000399093.
CHAIN 732 1010 BrkA translocator.
/FTId=PRO_0000399094.
DOMAIN 742 1010 Autotransporter. {ECO:0000255|PROSITE-
ProRule:PRU00556}.
SITE 731 732 Cleavage. {ECO:0000269|PubMed:10079522}.
CONFLICT 47 47 P -> A (in Ref. 3; AA sequence).
{ECO:0000305}.
STRAND 747 760 {ECO:0000244|PDB:3QQ2}.
STRAND 768 783 {ECO:0000244|PDB:3QQ2}.
STRAND 788 804 {ECO:0000244|PDB:3QQ2}.
STRAND 806 808 {ECO:0000244|PDB:3QQ2}.
STRAND 812 846 {ECO:0000244|PDB:3QQ2}.
STRAND 850 852 {ECO:0000244|PDB:3QQ2}.
STRAND 856 872 {ECO:0000244|PDB:3QQ2}.
HELIX 877 879 {ECO:0000244|PDB:3QQ2}.
STRAND 880 893 {ECO:0000244|PDB:3QQ2}.
STRAND 896 899 {ECO:0000244|PDB:3QQ2}.
STRAND 905 908 {ECO:0000244|PDB:3QQ2}.
STRAND 912 924 {ECO:0000244|PDB:3QQ2}.
STRAND 929 931 {ECO:0000244|PDB:3QQ2}.
STRAND 933 947 {ECO:0000244|PDB:3QQ2}.
STRAND 967 978 {ECO:0000244|PDB:3QQ2}.
TURN 979 981 {ECO:0000244|PDB:3QQ2}.
STRAND 982 995 {ECO:0000244|PDB:3QQ2}.
STRAND 997 1008 {ECO:0000244|PDB:3QQ2}.
SEQUENCE 1010 AA; 103377 MW; 608A006EC3087B52 CRC64;
MYLDRFRQCP SSLQIPRSAW RLHALAAALA LAGMARLAPA AAQAPQPPVA GAPHAQDAGQ
EGEFDHRDNT LIAVFDDGVG INLDDDPDEL GETAPPTLKD IHISVEHKNP MSKPAIGVRV
SGAGRALTLA GSTIDATEGG IPAVVRRGGT LELDGVTVAG GEGMEPMTVS DAGSRLSVRG
GVLGGEAPGV GLVRAAQGGQ ASIIDATLQS ILGPALIADG GSISVAGGSI DMDMGPGFPP
PPPPLPGAPL AAHPPLDRVA AVHAGQDGKV TLREVALRAH GPQATGVYAY MPGSEITLQG
GTVSVQGDDG AGVVAGAGLL DALPPGGTVR LDGTTVSTDG ANTDAVLVRG DAARAEVVNT
VLRTAKSLAA GVSAQHGGRV TLRQTRIETA GAGAEGISVL GFEPQSGSGP ASVDMQGGSI
TTTGNRAAGI ALTHGSARLE GVAVRAEGSG SSAAQLANGT LVVSAGSLAS AQSGAISVTD
TPLKLMPGAL ASSTVSVRLT DGATAQGGNG VFLQQHSTIP VAVALESGAL ARGDIVADGN
KPLDAGISLS VASGAAWHGA TQVLQSATLG KGGTWVVNAD SRVQDMSMRG GRVEFQAPAP
EASYKTLTLQ TLDGNGVFVL NTNVAAGQND QLRVTGRADG QHRVLVRNAG GEADSRGARL
GLVHTQGQGN ATFRLANVGK AVDLGTWRYS LAEDPKTHVW SLQRAGQALS GAANAAVNAA
DLSSIALAES NALDKRLGEL RLRADAGGPW ARTFSERQQI SNRHARAYDQ TVSGLEIGLD
RGWSASGGRW YAGGLLGYTY ADRTYPGDGG GKVKGLHVGG YAAYVGDGGY YLDTVLRLGR
YDQQYNIAGT DGGRVTADYR TSGAAWSLEG GRRFELPNDW FAEPQAEVML WRTSGKRYRA
SNGLRVKVDA NTATLGRLGL RFGRRIALAG GNIVQPYARL GWTQEFKSTG DVRTNGIGHA
GAGRHGRVEL GAGVDAALGK GHNLYASYEY AAGDRINIPW SFHAGYRYSF


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