P4_BPPH6
ID P4_BPPH6 Reviewed; 332 AA.
AC P11125;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Packaging enzyme P4;
DE EC=3.6.1.15;
GN Name=P4;
OS Pseudomonas phage phi6 (Bacteriophage phi-6).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Vidaverviricetes;
OC Mindivirales; Cystoviridae; Cystovirus.
OX NCBI_TaxID=10879;
OH NCBI_TaxID=319; Pseudomonas savastanoi pv. phaseolicola (Pseudomonas syringae pv. phaseolicola).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3346944; DOI=10.1128/jvi.62.4.1180-1185.1988;
RA Mindich L., Nemhauser I., Gottlieb P., Romantschuk M., Carton J.,
RA Frucht S., Strassman J., Bamford D.H., Kalkkinen N.;
RT "Nucleotide sequence of the large double-stranded RNA segment of
RT bacteriophage phi 6: genes specifying the viral replicase and
RT transcriptase.";
RL J. Virol. 62:1180-1185(1988).
RN [2]
RP FUNCTION, AND NTPASE ACTIVITY.
RX PubMed=12239286; DOI=10.1128/jvi.76.20.10122-10127.2002;
RA Pirttimaa M.J., Paatero A.O., Frilander M.J., Bamford D.H.;
RT "Nonspecific nucleoside triphosphatase P4 of double-stranded RNA
RT bacteriophage phi6 is required for single-stranded RNA packaging and
RT transcription.";
RL J. Virol. 76:10122-10127(2002).
RN [3]
RP SUBUNIT.
RX PubMed=12966097; DOI=10.1074/jbc.m306928200;
RA Kainov D.E., Pirttimaa M.J., Tuma R., Butcher S.J., Thomas G.J. Jr.,
RA Bamford D.H., Makeyev E.V.;
RT "RNA packaging device of double-stranded RNA bacteriophages, possibly as
RT simple as hexamer of P4 protein.";
RL J. Biol. Chem. 278:48084-48091(2003).
RN [4]
RP IDENTIFICATION IN THE PACKAGING COMPLEX.
RX PubMed=23077625; DOI=10.1371/journal.pone.0047489;
RA Katz G., Wei H., Alimova A., Katz A., Morgan D.G., Gottlieb P.;
RT "Protein P7 of the cystovirus phi6 is located at the three-fold axis of the
RT unexpanded procapsid.";
RL PLoS ONE 7:E47489-E47489(2012).
RN [5]
RP REVIEW.
RX PubMed=22297533; DOI=10.1007/978-1-4614-0980-9_27;
RA Mancini E.J., Tuma R.;
RT "Mechanism of RNA packaging motor.";
RL Adv. Exp. Med. Biol. 726:609-629(2012).
RN [6]
RP STRUCTURE BY ELECTRON MICROSCOPY (14.0 ANGSTROMS).
RX PubMed=17292834; DOI=10.1016/j.str.2006.12.004;
RA Jaalinoja H.T., Huiskonen J.T., Butcher S.J.;
RT "Electron cryomicroscopy comparison of the architectures of the enveloped
RT bacteriophages phi6 and phi8.";
RL Structure 15:157-167(2007).
CC -!- FUNCTION: Packaging motor with helicase and translocase activities.
CC Part of the packaging complex that packages the viral RNA segments,
CC replicate them into a double-stranded form and transcribe them. is one
CC of the structural proteins of the polyhedral procapsid, which is
CC responsible for genomic replication and transcription. Displays single-
CC stranded RNA-stimulated NTPase activity. {ECO:0000269|PubMed:12239286}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC -!- SUBUNIT: Homohexamer. Part of the packaging complex composed of RDRP,
CC P4 and P7. {ECO:0000269|PubMed:12966097, ECO:0000269|PubMed:23077625}.
CC -!- SUBCELLULAR LOCATION: Virion. Note=Capsid protein found in 72 copies.
CC Prior to RNA packaging, localizes on the outer procapsid surface at the
CC 12 potential RNA portal sites.
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DR EMBL; M17461; AAA32356.1; -; Genomic_RNA.
DR PIR; C29885; P4BPF6.
DR RefSeq; NP_620347.1; NC_003715.1.
DR PDB; 4BLO; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L=1-309.
DR PDB; 5MUU; EM; 4.00 A; C=1-332.
DR PDB; 5MUV; EM; 9.10 A; A/B/I/J/K/L=1-309.
DR PDB; 5MUW; EM; 2.80 A; A/B/I/J/K/L=1-309.
DR PDB; 6HY0; EM; 3.50 A; C=1-332.
DR PDBsum; 4BLO; -.
DR PDBsum; 5MUU; -.
DR PDBsum; 5MUV; -.
DR PDBsum; 5MUW; -.
DR PDBsum; 6HY0; -.
DR SMR; P11125; -.
DR GeneID; 956437; -.
DR KEGG; vg:956437; -.
DR SABIO-RK; P11125; -.
DR Proteomes; UP000002610; Genome.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0046729; C:viral procapsid; IDA:CACAO.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IDA:CACAO.
DR GO; GO:0019072; P:viral genome packaging; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020973; Packaging_enz_P4.
DR Pfam; PF11602; NTPase_P4; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Capsid protein; Direct protein sequencing;
KW Hydrolase; Nucleotide-binding; Reference proteome; Transcription;
KW Viral genome packaging; Viral release from host cell; Virion.
FT INIT_MET 1
FT /note="Removed; by host"
FT CHAIN 2..332
FT /note="Packaging enzyme P4"
FT /id="PRO_0000164639"
FT REGION 111..138
FT /note="Involved in the regulation and mechanisms of
FT transcription, replication and genome packaging"
FT /evidence="ECO:0000250"
FT REGION 310..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 126..133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT HELIX 7..22
FT /evidence="ECO:0007829|PDB:4BLO"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:4BLO"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:4BLO"
FT HELIX 38..54
FT /evidence="ECO:0007829|PDB:4BLO"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:4BLO"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:4BLO"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:4BLO"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:4BLO"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:4BLO"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:4BLO"
FT STRAND 117..127
FT /evidence="ECO:0007829|PDB:4BLO"
FT HELIX 132..138
FT /evidence="ECO:0007829|PDB:4BLO"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:4BLO"
FT HELIX 154..157
FT /evidence="ECO:0007829|PDB:4BLO"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:4BLO"
FT HELIX 167..179
FT /evidence="ECO:0007829|PDB:4BLO"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:4BLO"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:4BLO"
FT HELIX 208..222
FT /evidence="ECO:0007829|PDB:4BLO"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:4BLO"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:4BLO"
FT HELIX 240..248
FT /evidence="ECO:0007829|PDB:4BLO"
FT STRAND 252..258
FT /evidence="ECO:0007829|PDB:4BLO"
FT STRAND 261..269
FT /evidence="ECO:0007829|PDB:4BLO"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:4BLO"
FT HELIX 297..300
FT /evidence="ECO:0007829|PDB:6HY0"
SQ SEQUENCE 332 AA; 35164 MW; 96E8091C521395E4 CRC64;
MPIVVTQAHI DRVGIAADLL DASPVSLQVL GRPTAINTVV IKTYIAAVME LASKQGGSLA
GVDIRPSVLL KDTAIFTKPK AKSADVESDV DVLDTGIYSV PGLARKPVTH RWPSEGIYSG
VTALMGATGS GKSITLNEKL RPDVLIRWGE VAEAYDELDT AVHISTLDEM LIVCIGLGAL
GFNVAVDSVR PLLFRLKGAA SAGGIVAVFY SLLTDISNLF TQYDCSVVMV VNPMVDAEKI
EYVFGQVMAS TVGAILCADG NVSRTMFRTN KGRIFNGAAP LAADTHMPSM DRPTSMKALD
HTSIASVAPL ERGSVDTDDR NSAPRRGANF SL
