FIBD_BPBPP
ID FIBD_BPBPP Reviewed; 381 AA.
AC Q775D6;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 02-JUN-2021, entry version 66.
DE RecName: Full=Tail fiber receptor-binding protein {ECO:0000305};
DE AltName: Full=Major tropism determinant protein {ECO:0000303|PubMed:20160083};
GN Name=mtd {ECO:0000312|EMBL:AAR97674.1};
OS Bordetella phage BPP-1.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Podoviridae; Rauchvirus.
OX NCBI_TaxID=194699 {ECO:0000312|Proteomes:UP000001765};
OH NCBI_TaxID=518; Bordetella bronchiseptica (Alcaligenes bronchisepticus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=14973019; DOI=10.1128/jb.186.5.1503-1517.2004;
RA Liu M., Gingery M., Doulatov S.R., Liu Y., Hodes A., Baker S., Davis P.,
RA Simmonds M., Churcher C., Mungall K., Quail M.A., Preston A., Harvill E.T.,
RA Maskell D.J., Eiserling F.A., Parkhill J., Miller J.F.;
RT "Genomic and genetic analysis of Bordetella bacteriophages encoding reverse
RT transcriptase-mediated tropism-switching cassettes.";
RL J. Bacteriol. 186:1503-1517(2004).
RN [2]
RP FUNCTION, AND DOMAIN.
RX PubMed=15386016; DOI=10.1038/nature02833;
RA Doulatov S., Hodes A., Dai L., Mandhana N., Liu M., Deora R., Simons R.W.,
RA Zimmerly S., Miller J.F.;
RT "Tropism switching in Bordetella bacteriophage defines a family of
RT diversity-generating retroelements.";
RL Nature 431:476-481(2004).
RN [3]
RP STRUCTURE BY ELECTRON MICROSCOPY OF THE VIRAL PARTICLE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=20160083; DOI=10.1073/pnas.0915008107;
RA Dai W., Hodes A., Hui W.H., Gingery M., Miller J.F., Zhou Z.H.;
RT "Three-dimensional structure of tropism-switching Bordetella
RT bacteriophage.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:4347-4352(2010).
RN [4] {ECO:0007744|PDB:1YU0, ECO:0007744|PDB:1YU1, ECO:0007744|PDB:1YU2, ECO:0007744|PDB:1YU3, ECO:0007744|PDB:1YU4}
RP X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS), AND SUBUNIT.
RX PubMed=16170324; DOI=10.1038/nsmb992;
RA McMahon S.A., Miller J.L., Lawton J.A., Kerkow D.E., Hodes A.,
RA Marti-Renom M.A., Doulatov S., Narayanan E., Sali A., Miller J.F.,
RA Ghosh P.;
RT "The C-type lectin fold as an evolutionary solution for massive sequence
RT variation.";
RL Nat. Struct. Mol. Biol. 12:886-892(2005).
RN [5] {ECO:0000312|PDB:2IOU}
RP X-RAY CRYSTALLOGRAPHY (3.16 ANGSTROMS) OF 5-380.
RX PubMed=18532877; DOI=10.1371/journal.pbio.0060131;
RA Miller J.L., Le Coq J., Hodes A., Barbalat R., Miller J.F., Ghosh P.;
RT "Selective ligand recognition by a diversity-generating retroelement
RT variable protein.";
RL PLoS Biol. 6:E131-E131(2008).
CC -!- FUNCTION: Tail fiber protein located at the distal ends of the fibers
CC that binds to the adhesion receptors on the host surface, thereby
CC determining the host range. The phage can alter its tropism by
CC modifying this protein. Variants are expressed through a diversity-
CC generating retroelement (DGR) that creates mutant copies of a template
CC repeat and replaces the end of the tail fiber receptor-binding protein
CC with these sequences, thus changing the host range. Milliards of
CC variants of the fiber receptor-binding protein can be created with this
CC system. {ECO:0000269|PubMed:15386016}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:16170324}.
CC -!- INTERACTION:
CC Q775D6; Q03035: prn; Xeno; NbExp=8; IntAct=EBI-15556799, EBI-15556835;
CC -!- SUBCELLULAR LOCATION: Virion. Note=Part of the tail fibers.
CC {ECO:0000269|PubMed:20160083}.
CC -!- DOMAIN: The C-terminus contains a variable sequence in which nucleotide
CC subtitutions can be introduced at 23 sites by the DGR.
CC {ECO:0000269|PubMed:15386016}.
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DR EMBL; AY029185; AAR97674.1; -; Genomic_DNA.
DR RefSeq; NP_958677.1; NC_005357.1.
DR PDB; 1YU0; X-ray; 1.56 A; A=1-381.
DR PDB; 1YU1; X-ray; 2.07 A; A=1-381.
DR PDB; 1YU2; X-ray; 1.86 A; A=1-381.
DR PDB; 1YU3; X-ray; 2.52 A; A=1-381.
DR PDB; 1YU4; X-ray; 1.87 A; A/B/C=1-381.
DR PDB; 2IOU; X-ray; 3.16 A; A/B/C/D/E/F=5-380.
DR PDBsum; 1YU0; -.
DR PDBsum; 1YU1; -.
DR PDBsum; 1YU2; -.
DR PDBsum; 1YU3; -.
DR PDBsum; 1YU4; -.
DR PDBsum; 2IOU; -.
DR SMR; Q775D6; -.
DR DIP; DIP-46043N; -.
DR IntAct; Q775D6; 1.
DR GeneID; 2717224; -.
DR KEGG; vg:2717224; -.
DR EvolutionaryTrace; Q775D6; -.
DR Proteomes; UP000001765; Genome.
DR GO; GO:0098024; C:virus tail, fiber; IEA:UniProtKB-KW.
DR GO; GO:0098671; P:adhesion receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0098678; P:viral tropism switching; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1580.10; -; 1.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR041352; Mtd_N.
DR InterPro; IPR042095; SUMF_sf.
DR Pfam; PF18454; Mtd_N; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Host-virus interaction; Late protein; Reference proteome;
KW Viral attachment to host adhesion receptor; Viral attachment to host cell;
KW Viral receptor tropism switching; Viral tail fiber protein;
KW Viral tail protein; Virion; Virus entry into host cell.
FT CHAIN 1..381
FT /note="Tail fiber receptor-binding protein"
FT /id="PRO_0000432958"
FT HELIX 12..16
FT /evidence="ECO:0007829|PDB:1YU0"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:1YU0"
FT TURN 29..32
FT /evidence="ECO:0007829|PDB:1YU0"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:1YU0"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:1YU0"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:1YU4"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:1YU0"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:1YU0"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:1YU0"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:1YU0"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:1YU0"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:1YU0"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:1YU0"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:1YU0"
FT STRAND 136..147
FT /evidence="ECO:0007829|PDB:1YU0"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:1YU0"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:1YU0"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:1YU0"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:1YU0"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:1YU0"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:1YU0"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:1YU0"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:2IOU"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:1YU2"
FT TURN 223..226
FT /evidence="ECO:0007829|PDB:1YU0"
FT HELIX 238..247
FT /evidence="ECO:0007829|PDB:1YU0"
FT HELIX 255..262
FT /evidence="ECO:0007829|PDB:1YU0"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:1YU0"
FT HELIX 290..293
FT /evidence="ECO:0007829|PDB:1YU0"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:1YU0"
FT STRAND 307..317
FT /evidence="ECO:0007829|PDB:1YU0"
FT STRAND 326..329
FT /evidence="ECO:0007829|PDB:1YU0"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:1YU0"
FT STRAND 336..342
FT /evidence="ECO:0007829|PDB:1YU0"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:1YU0"
FT STRAND 374..379
FT /evidence="ECO:0007829|PDB:1YU0"
SQ SEQUENCE 381 AA; 39524 MW; D40DC9AE0133206D CRC64;
MSTAVQFRGG TTAQHATFTG AAREITVDTD KNTVVVHDGA TAGGFPLARH DLVKTAFIKA
DKSAVAFTRT GNATASIKAG TIVEVNGKLV QFTADTAITM PALTAGTDYA IYVCDDGTVR
ADSNFSAPTG YTSTTARKVG GFHYAPGSNA AAQAGGNTTA QINEYSLWDI KFRPAALDPR
GMTLVAGAFW ADIYLLGVNH LTDGTSKYNV TIADGSASPK KSTKFGGDGS AAYSDGAWYN
FAEVMTHHGK RLPNYNEFQA LAFGTTEATS SGGTDVPTTG VNGTGATSAW NIFTSKWGVV
QASGCLWTWG NEFGGVNGAS EYTANTGGRG SVYAQPAAAL FGGAWNGTSL SGSRAALWYS
GPSFSFAFFG ARGVCDHLIL E
