P2_BPPRD
ID P2_BPPRD Reviewed; 591 AA.
AC P27378; Q3T4P2;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 29-SEP-2021, entry version 96.
DE RecName: Full=Adsorption protein P2;
DE AltName: Full=Protein P2;
GN Name=II;
OS Enterobacteria phage PRD1 (Bacteriophage PRD1).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Kalamavirales; Tectiviridae; Alphatectivirus.
OX NCBI_TaxID=10658;
OH NCBI_TaxID=471; Acinetobacter calcoaceticus.
OH NCBI_TaxID=562; Escherichia coli.
OH NCBI_TaxID=584; Proteus mirabilis.
OH NCBI_TaxID=287; Pseudomonas aeruginosa.
OH NCBI_TaxID=294; Pseudomonas fluorescens.
OH NCBI_TaxID=303; Pseudomonas putida (Arthrobacter siderocapsulatus).
OH NCBI_TaxID=90371; Salmonella typhimurium.
OH NCBI_TaxID=666; Vibrio cholerae.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-10.
RX PubMed=1853567; DOI=10.1016/0042-6822(91)90995-n;
RA Bamford J.K.H., Haenninen A.-L., Pakula T.M., Ojala P.M., Kalkkinen N.,
RA Frilander M., Bamford D.H.;
RT "Genome organization of membrane-containing bacteriophage PRD1.";
RL Virology 183:658-676(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15946683; DOI=10.1016/j.jmb.2005.04.059;
RA Saren A.M., Ravantti J.J., Benson S.D., Burnett R.M., Paulin L.,
RA Bamford D.H., Bamford J.K.H.;
RT "A snapshot of viral evolution from genome analysis of the tectiviridae
RT family.";
RL J. Mol. Biol. 350:427-440(2005).
RN [3]
RP FUNCTION.
RX PubMed=11577098; DOI=10.1074/jbc.m106848200;
RA Sokolova A., Malfois M., Caldentey J., Svergun D.I., Koch M.H.,
RA Bamford D.H., Tuma R.;
RT "Solution structure of bacteriophage PRD1 vertex complex.";
RL J. Biol. Chem. 276:46187-46195(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=11042087; DOI=10.1006/jsbi.2000.4275;
RA Xu L., Butcher S.J., Benson S.D., Bamford D.H., Burnett R.M.;
RT "Crystallization and preliminary X-ray analysis of receptor-binding protein
RT P2 of bacteriophage PRD1.";
RL J. Struct. Biol. 131:159-163(2000).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=12623018; DOI=10.1016/s0969-2126(03)00023-6;
RA Xu L., Benson S.D., Butcher S.J., Bamford D.H., Burnett R.M.;
RT "The receptor binding protein P2 of PRD1, a virus targeting antibiotic-
RT resistant bacteria, has a novel fold suggesting multiple functions.";
RL Structure 11:309-322(2003).
CC -!- FUNCTION: Adsorption protein. In association with P31 and trimeric P5,
CC forms the spike complexes located at the 5-fold vertices of the capsid.
CC Involved in recognition and attachment to the receptor on the surface
CC of the host. Likely triggers the processes of vertex disassembly,
CC membrane tube formation, and subsequent DNA injection. Essential for
CC viral infectivity. {ECO:0000269|PubMed:11577098}.
CC -!- SUBCELLULAR LOCATION: Virion.
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DR EMBL; AY848689; AAX45913.1; -; Genomic_DNA.
DR PIR; D40477; WMBPQ2.
DR RefSeq; NP_040684.1; NC_001421.2.
DR PDB; 1N7U; X-ray; 2.40 A; A=2-555.
DR PDB; 1N7V; X-ray; 2.20 A; A=2-556.
DR PDBsum; 1N7U; -.
DR PDBsum; 1N7V; -.
DR SMR; P27378; -.
DR PRIDE; P27378; -.
DR EvolutionaryTrace; P27378; -.
DR Proteomes; UP000002143; Genome.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR Gene3D; 2.105.10.10; -; 2.
DR Gene3D; 2.70.250.10; -; 1.
DR InterPro; IPR036325; P2_sf.
DR InterPro; IPR015297; Phage_PRD1_P2.
DR InterPro; IPR015948; Phage_PRD1_P2_C.
DR InterPro; IPR015949; Phage_PRD1_P2_N.
DR Pfam; PF09214; Prd1-P2; 1.
DR SUPFAM; SSF89428; SSF89428; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Host-virus interaction; Reference proteome; Viral attachment to host cell;
KW Virion; Virus entry into host cell.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000269|PubMed:1853567"
FT CHAIN 2..591
FT /note="Adsorption protein P2"
FT /id="PRO_0000165349"
FT DISULFID 254..277
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:1N7V"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:1N7V"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:1N7V"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:1N7V"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1N7V"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:1N7V"
FT STRAND 48..57
FT /evidence="ECO:0007829|PDB:1N7V"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:1N7V"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:1N7V"
FT HELIX 93..103
FT /evidence="ECO:0007829|PDB:1N7V"
FT HELIX 118..122
FT /evidence="ECO:0007829|PDB:1N7V"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:1N7V"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:1N7V"
FT STRAND 141..154
FT /evidence="ECO:0007829|PDB:1N7V"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:1N7V"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:1N7V"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:1N7V"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:1N7V"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:1N7V"
FT TURN 202..206
FT /evidence="ECO:0007829|PDB:1N7V"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:1N7V"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:1N7V"
FT STRAND 223..239
FT /evidence="ECO:0007829|PDB:1N7V"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:1N7U"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:1N7U"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:1N7U"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:1N7V"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:1N7V"
FT STRAND 301..320
FT /evidence="ECO:0007829|PDB:1N7V"
FT STRAND 324..330
FT /evidence="ECO:0007829|PDB:1N7V"
FT TURN 333..335
FT /evidence="ECO:0007829|PDB:1N7V"
FT STRAND 340..344
FT /evidence="ECO:0007829|PDB:1N7V"
FT STRAND 348..352
FT /evidence="ECO:0007829|PDB:1N7V"
FT STRAND 354..360
FT /evidence="ECO:0007829|PDB:1N7V"
FT STRAND 362..384
FT /evidence="ECO:0007829|PDB:1N7V"
FT STRAND 387..396
FT /evidence="ECO:0007829|PDB:1N7V"
FT HELIX 398..400
FT /evidence="ECO:0007829|PDB:1N7V"
FT HELIX 404..415
FT /evidence="ECO:0007829|PDB:1N7V"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:1N7U"
FT STRAND 425..433
FT /evidence="ECO:0007829|PDB:1N7V"
FT HELIX 434..438
FT /evidence="ECO:0007829|PDB:1N7V"
FT TURN 446..449
FT /evidence="ECO:0007829|PDB:1N7V"
FT STRAND 451..454
FT /evidence="ECO:0007829|PDB:1N7V"
FT STRAND 467..471
FT /evidence="ECO:0007829|PDB:1N7V"
FT STRAND 474..480
FT /evidence="ECO:0007829|PDB:1N7V"
FT STRAND 490..495
FT /evidence="ECO:0007829|PDB:1N7V"
FT STRAND 501..505
FT /evidence="ECO:0007829|PDB:1N7V"
FT HELIX 507..510
FT /evidence="ECO:0007829|PDB:1N7V"
FT STRAND 513..515
FT /evidence="ECO:0007829|PDB:1N7V"
FT STRAND 522..526
FT /evidence="ECO:0007829|PDB:1N7V"
FT STRAND 529..534
FT /evidence="ECO:0007829|PDB:1N7V"
FT STRAND 547..553
FT /evidence="ECO:0007829|PDB:1N7V"
SQ SEQUENCE 591 AA; 63822 MW; FAF2DAACBE83DD79 CRC64;
MANFNVPKLG VFPVAAVFDI DNVPEDSSAT GSRWLPSIYQ GGNYWGGGPQ ALHAQVSNFD
SSNRLPYNPR TENNPAGNCA FAFNPFGQYI SNISSAQSVH RRIYGIDLND EPLFSPNAAS
ITNGGNPTMS QDTGYHNIGP INTAYKAEIF RPVNPLPMSD TAPDPETLEP GQTEPLIKSD
GVYSNSGIAS FIFDRPVTEP NPNWPPLPPP VIPIIYPTPA LGIGAAAAYG FGYQVTVYRW
EEIPVEFIAD PETCPAQPTT DKVIIRTTDL NPEGSPCAYE AGIILVRQTS NPMNAVAGRL
VPYVEDIAVD IFLTGKFFTL NPPLRITNNY FADDEVKENT VTIGNYTTTL SSAYYAVYKT
DGYGGATCFI ASGGAGISAL VQLQDNSVLD VLYYSLPLSL GGSKAAIDEW VANNCGLFPM
SGGLDKTTLL EIPRRQLEAI NPQDGPGQYD LFILDDSGAY ASFSSFIGYP EAAYYVAGAA
TFMDVENPDE IIFILRNGAG WYACEIGDAL KIADDEFDSV DYFAYRGGVM FIGSARYTEG
GDPLPIKYRA IIPGLPRGRL PRVVLEYQAV GMSFIPCQTH CLGKGGIISK V
