BRKA_BORPE
ID BRKA_BORPE Reviewed; 1010 AA.
AC Q45340;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=BrkA autotransporter;
DE Contains:
DE RecName: Full=Serum resistance protein BrkA;
DE Contains:
DE RecName: Full=BrkA translocator;
DE Flags: Precursor;
GN Name=brkA {ECO:0000303|PubMed:7927748}; OrderedLocusNames=BP3494;
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Tohama I / BP338;
RX PubMed=7927748; DOI=10.1128/iai.62.11.4727-4738.1994;
RA Fernandez R.C., Weiss A.A.;
RT "Cloning and sequencing of a Bordetella pertussis serum resistance locus.";
RL Infect. Immun. 62:4727-4738(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
RN [3]
RP PROTEIN SEQUENCE OF 43-47, SUBCELLULAR LOCATION, AND DOMAIN.
RC STRAIN=Tohama I / BP338;
RX PubMed=12511495; DOI=10.1128/jb.185.2.489-495.2003;
RA Oliver D.C., Huang G., Fernandez R.C.;
RT "Identification of secretion determinants of the Bordetella pertussis BrkA
RT autotransporter.";
RL J. Bacteriol. 185:489-495(2003).
RN [4]
RP PROTEIN SEQUENCE OF 732-743, AND CLEAVAGE SITE.
RC STRAIN=Tohama I / BP338;
RX PubMed=10079522; DOI=10.1111/j.1574-6968.1999.tb13442.x;
RA Passerini de Rossi B.N., Friedman L.E., Gonzalez Flecha F.L.,
RA Castello P.R., Franco M.A., Rossi J.P.F.C.;
RT "Identification of Bordetella pertussis virulence-associated outer membrane
RT proteins.";
RL FEMS Microbiol. Lett. 172:9-13(1999).
RN [5]
RP PORE FORMATION, DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=10482528; DOI=10.1128/jb.181.18.5838-5842.1999;
RA Shannon J.L., Fernandez R.C.;
RT "The C-terminal domain of the Bordetella pertussis autotransporter BrkA
RT forms a pore in lipid bilayer membranes.";
RL J. Bacteriol. 181:5838-5842(1999).
RN [6]
RP FUNCTION.
RC STRAIN=Tohama I / BP338;
RX PubMed=11292725; DOI=10.1128/iai.69.5.3067-3072.2001;
RA Barnes M.G., Weiss A.A.;
RT "BrkA protein of Bordetella pertussis inhibits the classical pathway of
RT complement after C1 deposition.";
RL Infect. Immun. 69:3067-3072(2001).
RN [7]
RP CRYSTALLIZATION.
RX PubMed=19478443; DOI=10.1107/s174430910901642x;
RA Zhao L., Nguyen N.T., Fernandez R.C., Murphy M.E.;
RT "Crystallographic characterization of the passenger domain of the
RT Bordetella autotransporter BrkA.";
RL Acta Crystallogr. F 65:608-611(2009).
CC -!- FUNCTION: Inhibits the classical pathway of complement activation and
CC prevents accumulation of deposited C4. {ECO:0000269|PubMed:11292725}.
CC -!- SUBCELLULAR LOCATION: [BrkA autotransporter]: Periplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Serum resistance protein BrkA]: Secreted
CC {ECO:0000269|PubMed:12511495}. Cell surface
CC {ECO:0000269|PubMed:12511495}.
CC -!- SUBCELLULAR LOCATION: [BrkA translocator]: Cell outer membrane
CC {ECO:0000269|PubMed:10482528}; Multi-pass membrane protein
CC {ECO:0000305}. Note=The cleaved C-terminal fragment (autotransporter
CC domain) is localized in the outer membrane.
CC {ECO:0000269|PubMed:10482528}.
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, with subsequent cleavage. Finally, the mature
CC protein remains tightly associated with the bacterium.
CC {ECO:0000269|PubMed:10482528, ECO:0000269|PubMed:12511495}.
CC -!- DOMAIN: A 31- to 39-amino-acid region found immediately upstream of the
CC translocator domain is essential for surface expression.
CC {ECO:0000269|PubMed:12511495}.
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DR EMBL; U12276; AAA51646.1; -; Genomic_DNA.
DR EMBL; BX640421; CAE43755.1; -; Genomic_DNA.
DR PIR; I40329; I40329.
DR RefSeq; NP_882013.1; NC_002929.2.
DR RefSeq; WP_010931506.1; NZ_CP039022.1.
DR PDB; 3QQ2; X-ray; 3.00 A; A/B/C=727-1010.
DR PDBsum; 3QQ2; -.
DR AlphaFoldDB; Q45340; -.
DR SMR; Q45340; -.
DR STRING; 257313.BP3494; -.
DR TCDB; 1.B.12.2.3; the autotransporter-1 (at-1) family.
DR GeneID; 45388226; -.
DR KEGG; bpe:BP3494; -.
DR PATRIC; fig|257313.5.peg.3783; -.
DR eggNOG; COG3468; Bacteria.
DR HOGENOM; CLU_297135_0_0_4; -.
DR OMA; NFEAGRF; -.
DR Proteomes; UP000002676; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR Gene3D; 2.160.20.20; -; 2.
DR Gene3D; 2.40.128.130; -; 1.
DR InterPro; IPR005546; Autotransporte_beta.
DR InterPro; IPR036709; Autotransporte_beta_dom_sf.
DR InterPro; IPR012332; Autotransporter_pectin_lyase_C.
DR InterPro; IPR006315; OM_autotransptr_brl.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR004899; Pertactin_central.
DR InterPro; IPR003991; Pertactin_virulence_factor.
DR Pfam; PF03797; Autotransporter; 1.
DR Pfam; PF03212; Pertactin; 1.
DR PRINTS; PR01484; PRTACTNFAMLY.
DR SMART; SM00869; Autotransporter; 1.
DR SUPFAM; SSF103515; SSF103515; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR TIGRFAMs; TIGR01414; autotrans_barl; 1.
DR PROSITE; PS51208; AUTOTRANSPORTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Direct protein sequencing; Membrane;
KW Periplasm; Reference proteome; Secreted; Signal; Transmembrane;
KW Transmembrane beta strand; Virulence.
FT SIGNAL 1..42
FT /evidence="ECO:0000269|PubMed:12511495"
FT CHAIN 43..1010
FT /note="BrkA autotransporter"
FT /id="PRO_0000399092"
FT CHAIN 43..731
FT /note="Serum resistance protein BrkA"
FT /id="PRO_0000399093"
FT CHAIN 732..1010
FT /note="BrkA translocator"
FT /id="PRO_0000399094"
FT DOMAIN 742..1010
FT /note="Autotransporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
FT SITE 731..732
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:10079522"
FT CONFLICT 47
FT /note="P -> A (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 747..760
FT /evidence="ECO:0007829|PDB:3QQ2"
FT STRAND 768..783
FT /evidence="ECO:0007829|PDB:3QQ2"
FT STRAND 788..804
FT /evidence="ECO:0007829|PDB:3QQ2"
FT STRAND 806..808
FT /evidence="ECO:0007829|PDB:3QQ2"
FT STRAND 812..846
FT /evidence="ECO:0007829|PDB:3QQ2"
FT STRAND 850..852
FT /evidence="ECO:0007829|PDB:3QQ2"
FT STRAND 856..872
FT /evidence="ECO:0007829|PDB:3QQ2"
FT HELIX 877..879
FT /evidence="ECO:0007829|PDB:3QQ2"
FT STRAND 880..893
FT /evidence="ECO:0007829|PDB:3QQ2"
FT STRAND 896..899
FT /evidence="ECO:0007829|PDB:3QQ2"
FT STRAND 905..908
FT /evidence="ECO:0007829|PDB:3QQ2"
FT STRAND 912..924
FT /evidence="ECO:0007829|PDB:3QQ2"
FT STRAND 929..931
FT /evidence="ECO:0007829|PDB:3QQ2"
FT STRAND 933..947
FT /evidence="ECO:0007829|PDB:3QQ2"
FT STRAND 967..978
FT /evidence="ECO:0007829|PDB:3QQ2"
FT TURN 979..981
FT /evidence="ECO:0007829|PDB:3QQ2"
FT STRAND 982..995
FT /evidence="ECO:0007829|PDB:3QQ2"
FT STRAND 997..1008
FT /evidence="ECO:0007829|PDB:3QQ2"
SQ 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
