RBP_BPLP2
ID RBP_BPLP2 Reviewed; 264 AA.
AC Q71AW2; Q1RNF7;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 02-JUN-2021, entry version 92.
DE RecName: Full=Receptor binding protein {ECO:0000303|PubMed:20351260};
DE Short=RBP {ECO:0000303|PubMed:20351260};
DE AltName: Full=Gene product 18 {ECO:0000305};
DE Short=Gp18 {ECO:0000305};
GN Name=rbp {ECO:0000312|EMBL:AAQ10938.1};
OS Lactococcus phage p2 (Lactococcus lactis bacteriophage p2).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae; Skunavirus.
OX NCBI_TaxID=254252;
OH NCBI_TaxID=1358; Lactococcus lactis.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15466519; DOI=10.1128/aem.70.10.5818-5824.2004;
RA Dupont K., Vogensen F.K., Neve H., Bresciani J., Josephsen J.;
RT "Identification of the receptor-binding protein in 936-species lactococcal
RT bacteriophages.";
RL Appl. Environ. Microbiol. 70:5818-5824(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15752347; DOI=10.1111/j.1365-2672.2005.02548.x;
RA Dupont K., Vogensen F.K., Josephsen J.;
RT "Detection of lactococcal 936-species bacteriophages in whey by magnetic
RT capture hybridization PCR targeting a variable region of receptor-binding
RT protein genes.";
RL J. Appl. Microbiol. 98:1001-1009(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tremblay D.M., Deveau H., Moineau S.;
RT "Complete genomic sequence of Lactococcus lactis phage p2.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0007744|PDB:1ZRU}
RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS), AND INTERACTION WITH HOST
RP PHOSPHOPOLYSACCHARIDES.
RX PubMed=16547026; DOI=10.1128/jb.188.7.2400-2410.2006;
RA Tremblay D.M., Tegoni M., Spinelli S., Campanacci V., Blangy S., Huyghe C.,
RA Desmyter A., Labrie S., Moineau S., Cambillau C.;
RT "Receptor-binding protein of Lactococcus lactis phages: identification and
RT characterization of the saccharide receptor-binding site.";
RL J. Bacteriol. 188:2400-2410(2006).
RN [5] {ECO:0007744|PDB:2BSD, ECO:0007744|PDB:2BSE}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS).
RX PubMed=16327804; DOI=10.1038/nsmb1029;
RA Spinelli S., Desmyter A., Verrips C.T., de Haard H.J., Moineau S.,
RA Cambillau C.;
RT "Lactococcal bacteriophage p2 receptor-binding protein structure suggests a
RT common ancestor gene with bacterial and mammalian viruses.";
RL Nat. Struct. Mol. Biol. 13:85-89(2006).
RN [6] {ECO:0007744|PDB:2WZP, ECO:0007744|PDB:2X53}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 2-264, SUBUNIT, SUBCELLULAR
RP LOCATION, INTERACTION WITH HOST PHOSPHOPOLYSACCHARIDES, AND FUNCTION.
RX PubMed=20351260; DOI=10.1073/pnas.1000232107;
RA Sciara G., Bebeacua C., Bron P., Tremblay D., Ortiz-Lombardia M.,
RA Lichiere J., van Heel M., Campanacci V., Moineau S., Cambillau C.;
RT "Structure of lactococcal phage p2 baseplate and its mechanism of
RT activation.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:6852-6857(2010).
RN [7]
RP STRUCTURE BY ELECTRON MICROSCOPY (22 ANGSTROMS) OF THE TAIL, FUNCTION,
RP SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH HOST
RP PHOSPHOPOLYSACCHARIDES, AND INTERACTION WITH THE DISTAL TAIL PROTEIN.
RX PubMed=24027307; DOI=10.1128/jvi.02033-13;
RA Bebeacua C., Tremblay D., Farenc C., Chapot-Chartier M.P., Sadovskaya I.,
RA van Heel M., Veesler D., Moineau S., Cambillau C.;
RT "Structure, adsorption to host, and infection mechanism of virulent
RT lactococcal phage p2.";
RL J. Virol. 87:12302-12312(2013).
CC -!- FUNCTION: Binds to the host phosphopolysaccharides at the onset of
CC infection. Upon activation by calcium, the receptor binding proteins
CC change their conformation, presenting their binding sites to the host,
CC and a channel opens at the bottom of the baseplate for DNA ejection.
CC {ECO:0000269|PubMed:20351260, ECO:0000269|PubMed:24027307}.
CC -!- SUBUNIT: Homotrimer; found as an assembly of 6 homotrimers
CC (PubMed:20351260, PubMed:24027307). Interacts with host
CC phosphopolysaccharides; this allows the virus to bind the external cell
CC wall layer (PubMed:16547026, PubMed:20351260, PubMed:24027307).
CC Interacts with the distal tail protein (PubMed:24027307).
CC {ECO:0000269|PubMed:20351260, ECO:0000269|PubMed:24027307}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:20351260,
CC ECO:0000269|PubMed:24027307}. Note=Part of the baseplate.
CC {ECO:0000269|PubMed:20351260, ECO:0000269|PubMed:24027307}.
CC -!- DOMAIN: The C-terminus is involved in host receptor binding. Host-
CC recognition domains point upwards, towards the capsid.
CC {ECO:0000269|PubMed:24027307}.
CC -!- SIMILARITY: Belongs to the skunalikevirus receptor binding protein
CC family. {ECO:0000305}.
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DR EMBL; AF539441; AAQ10938.1; -; Genomic_DNA.
DR EMBL; GQ979703; AAT81478.1; -; Genomic_DNA.
DR PDB; 1ZRU; X-ray; 1.73 A; A/B/C=1-264.
DR PDB; 2BSD; X-ray; 2.30 A; A/B/C=1-264.
DR PDB; 2BSE; X-ray; 2.70 A; A/B/C=1-264.
DR PDB; 2WZP; X-ray; 2.60 A; A/B/C/G/H/I=2-264.
DR PDB; 2X53; X-ray; 3.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=2-264.
DR PDB; 3DA0; X-ray; 1.65 A; A/B/C=163-264.
DR PDB; 4V5I; X-ray; 5.46 A; AA/AB/AC/AD/AE/AF/AG/AH/AI/AJ/AK/AL/AM/AN/AO/AP/AQ/AR/BA/BB/BC/BD/BE/BF/BG/BH/BI/BJ/BK/BL=2-264.
DR PDB; 6ZIG; EM; 42.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=1-264.
DR PDB; 6ZIH; EM; 28.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=1-264.
DR PDB; 6ZJJ; EM; 22.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=1-264.
DR PDBsum; 1ZRU; -.
DR PDBsum; 2BSD; -.
DR PDBsum; 2BSE; -.
DR PDBsum; 2WZP; -.
DR PDBsum; 2X53; -.
DR PDBsum; 3DA0; -.
DR PDBsum; 4V5I; -.
DR PDBsum; 6ZIG; -.
DR PDBsum; 6ZIH; -.
DR PDBsum; 6ZJJ; -.
DR SMR; Q71AW2; -.
DR DIP; DIP-59525N; -.
DR IntAct; Q71AW2; 1.
DR ABCD; Q71AW2; 1 sequenced antibody.
DR EvolutionaryTrace; Q71AW2; -.
DR Proteomes; UP000002348; Genome.
DR GO; GO:0098025; C:virus tail, baseplate; IDA:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0098670; P:entry 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:0019062; P:virion attachment to host cell; IDA:UniProtKB.
DR InterPro; IPR008982; Adenovirus_pIV-like_att.
DR InterPro; IPR015027; Caudo_bapla_RBP.
DR Pfam; PF08931; Caudo_bapla_RBP; 1.
DR SUPFAM; SSF49835; SSF49835; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Host-virus interaction; Reference proteome;
KW Viral attachment to host cell; Viral attachment to host entry receptor;
KW Viral baseplate protein; Viral tail protein; Virion;
KW Virus entry into host cell.
FT CHAIN 1..264
FT /note="Receptor binding protein"
FT /id="PRO_0000438236"
FT REGION 164..264
FT /note="Host receptor binding"
FT /evidence="ECO:0000269|PubMed:20351260"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:1ZRU"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:2WZP"
FT HELIX 20..31
FT /evidence="ECO:0007829|PDB:1ZRU"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:1ZRU"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:2BSD"
FT STRAND 50..62
FT /evidence="ECO:0007829|PDB:1ZRU"
FT STRAND 65..75
FT /evidence="ECO:0007829|PDB:1ZRU"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:1ZRU"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:1ZRU"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:1ZRU"
FT STRAND 119..128
FT /evidence="ECO:0007829|PDB:1ZRU"
FT STRAND 130..138
FT /evidence="ECO:0007829|PDB:1ZRU"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:1ZRU"
FT STRAND 146..157
FT /evidence="ECO:0007829|PDB:1ZRU"
FT STRAND 163..171
FT /evidence="ECO:0007829|PDB:3DA0"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:3DA0"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:3DA0"
FT STRAND 185..194
FT /evidence="ECO:0007829|PDB:3DA0"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:3DA0"
FT STRAND 218..224
FT /evidence="ECO:0007829|PDB:3DA0"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:3DA0"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:3DA0"
FT STRAND 253..262
FT /evidence="ECO:0007829|PDB:3DA0"
SQ SEQUENCE 264 AA; 28645 MW; 6D2F7356D7C34853 CRC64;
MTIKNFTFFS PNSTEFPVGS NNDGKLYMML TGMDYRTIRR KDWSSPLNTA LNVQYTNTSI
IAGGRYFELL NETVALKGDS VNYIHANIDL TQTANPVSLS AETANNSNGV DINNGSGVLK
VCFDIVTTSG TGVTSTKPIV QTSTLDSISV NDMTVSGSID VPVQTLTVEA GNGLQLQLTK
KNNDLVIVRF FGSVSNIQKG WNMSGTWVDR PFRPAAVQSL VGHFAGRDTS FHIDINPNGS
ITWWGANIDK TPIATRGNGS YFIK
