D13_VACCW
ID D13_VACCW Reviewed; 551 AA.
AC P68440; P04321; Q85329;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-1987, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Scaffold protein D13;
DE AltName: Full=62 kDa protein;
DE AltName: Full=Rifampicin resistance protein;
GN OrderedLocusNames=VACWR118; ORFNames=D13L;
OS Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS WR)).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10254;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3739227; DOI=10.1016/0042-6822(86)90011-5;
RA Niles E.G., Condit R.C., Caro P., Davidson K., Matusick L., Seto J.;
RT "Nucleotide sequence and genetic map of the 16-kb vaccinia virus HindIII D
RT fragment.";
RL Virology 153:96-112(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3008103; DOI=10.1093/nar/14.7.3003;
RA Weinrich S.L., Hruby D.E.;
RT "A tandemly-oriented late gene cluster within the vaccinia virus genome.";
RL Nucleic Acids Res. 14:3003-3016(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3811229; DOI=10.1016/0042-6822(87)90444-2;
RA Baldick C.J. Jr., Moss B.;
RT "Resistance of vaccinia virus to rifampicin conferred by a single
RT nucleotide substitution near the predicted NH2 terminus of a gene encoding
RT an Mr 62,000 polypeptide.";
RL Virology 156:138-145(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J.,
RA Wohlhueter R.;
RT "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT redundancy and an error rate of 0.16/10kb.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUBUNIT, AND MUTAGENESIS OF ASP-513.
RX PubMed=16144903; DOI=10.1083/jcb.200504026;
RA Szajner P., Weisberg A.S., Lebowitz J., Heuser J., Moss B.;
RT "External scaffold of spherical immature poxvirus particles is made of
RT protein trimers, forming a honeycomb lattice.";
RL J. Cell Biol. 170:971-981(2005).
RN [6]
RP MUTAGENESIS OF LYS-17; VAL-24; ASP-25; SER-26; GLN-27; THR-30; MET-33;
RP CYS-94; ASP-175; VAL-222; SER-227; ARG-234; THR-243; GLU-314; LYS-429;
RP ILE-439; GLU-465; ASN-480; LYS-484; ILE-485; ARG-488 AND THR-511.
RX PubMed=17055024; DOI=10.1016/j.virol.2006.09.031;
RA Charity J.C., Katz E., Moss B.;
RT "Amino acid substitutions at multiple sites within the vaccinia virus D13
RT scaffold protein confer resistance to rifampicin.";
RL Virology 359:227-232(2007).
RN [7]
RP INTERACTION WITH A17.
RX PubMed=19570860; DOI=10.1128/jvi.00875-09;
RA Bisht H., Weisberg A.S., Szajner P., Moss B.;
RT "Assembly and disassembly of the capsid-like external scaffold of immature
RT virions during vaccinia virus morphogenesis.";
RL J. Virol. 83:9140-9150(2009).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 2-551.
RX PubMed=21742267; DOI=10.1016/j.str.2011.03.023;
RA Bahar M.W., Graham S.C., Stuart D.I., Grimes J.M.;
RT "Insights into the evolution of a complex virus from the crystal structure
RT of vaccinia virus D13.";
RL Structure 19:1011-1020(2011).
CC -!- FUNCTION: Scaffold protein which forms a transitory spherical honeycomb
CC lattice providing curvature and rigidity to the convex membrane of
CC crescent and immature virions (IV). This association occurs
CC concomitantly with viral membrane formation. Targeted by the drug
CC rifampicin, which prevents the formation of this lattice, and hence
CC virus morphogenesis. In the presence of rifampicin, irregularly shaped
CC membranes that lack the honeycomb layer accumulate around areas of
CC electron-dense viroplasm. This layer is lost from virions during
CC maturation from IV to mature virion (MV), through the proteolysis of
CC A17 N-terminus.
CC -!- SUBUNIT: Homotrimer. Self-assembles to form a layer. Interacts with A17
CC (via N-terminus); this interaction is necessary for D13 association
CC with membranes. {ECO:0000269|PubMed:16144903,
CC ECO:0000269|PubMed:19570860}.
CC -!- INTERACTION:
CC P68440; P68440: VACWR118; NbExp=2; IntAct=EBI-15935427, EBI-15935427;
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC Note=Associates transitorily with crescent and IV membranes.
CC -!- MISCELLANEOUS: Displays structure similarities to capsid proteins.
CC -!- SIMILARITY: Belongs to the poxviridae protein D13 family.
CC {ECO:0000305}.
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DR EMBL; M15058; AAA48273.1; -; Genomic_DNA.
DR EMBL; X03729; CAA27368.1; -; Genomic_DNA.
DR EMBL; AY243312; AAO89397.1; -; Genomic_DNA.
DR PIR; C01146; QQVZ25.
DR RefSeq; YP_233000.1; NC_006998.1.
DR PDB; 2YGB; X-ray; 2.81 A; A/B/C=2-551.
DR PDB; 2YGC; X-ray; 3.02 A; A/B/C=2-551.
DR PDB; 3SAM; X-ray; 2.55 A; A/B/C=1-551.
DR PDB; 3SAQ; X-ray; 3.51 A; A/B=1-551.
DR PDB; 6BEB; X-ray; 2.55 A; A/B/C=1-551.
DR PDB; 6BEC; X-ray; 2.91 A; A/B/C=1-551.
DR PDB; 6BED; X-ray; 2.75 A; A/B/C=1-551.
DR PDB; 6BEE; X-ray; 3.11 A; A/B/C=1-551.
DR PDB; 6BEF; X-ray; 3.21 A; A/B/C=1-551.
DR PDB; 6BEG; X-ray; 3.10 A; A/B/C=1-551.
DR PDB; 6BEH; X-ray; 3.00 A; A/B/C=1-551.
DR PDB; 6BEI; X-ray; 2.81 A; A/B/C=1-551.
DR PDB; 7VFD; EM; 2.25 A; A/B/C=1-548.
DR PDB; 7VFE; EM; 2.63 A; A/B/C=1-548.
DR PDB; 7VFF; EM; 4.10 A; A/B/C=18-548.
DR PDB; 7VFG; EM; 3.87 A; A/B/C/D/E/F=1-548.
DR PDB; 7VFH; EM; 3.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=18-548.
DR PDBsum; 2YGB; -.
DR PDBsum; 2YGC; -.
DR PDBsum; 3SAM; -.
DR PDBsum; 3SAQ; -.
DR PDBsum; 6BEB; -.
DR PDBsum; 6BEC; -.
DR PDBsum; 6BED; -.
DR PDBsum; 6BEE; -.
DR PDBsum; 6BEF; -.
DR PDBsum; 6BEG; -.
DR PDBsum; 6BEH; -.
DR PDBsum; 6BEI; -.
DR PDBsum; 7VFD; -.
DR PDBsum; 7VFE; -.
DR PDBsum; 7VFF; -.
DR PDBsum; 7VFG; -.
DR PDBsum; 7VFH; -.
DR SMR; P68440; -.
DR DIP; DIP-59139N; -.
DR DNASU; 3707516; -.
DR GeneID; 3707516; -.
DR KEGG; vg:3707516; -.
DR EvolutionaryTrace; P68440; -.
DR Proteomes; UP000000344; Genome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046677; P:response to antibiotic; IEA:InterPro.
DR InterPro; IPR005008; Poxvirus_Rif-R.
DR Pfam; PF03340; Pox_Rif; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Late protein; Membrane; Reference proteome.
FT CHAIN 1..551
FT /note="Scaffold protein D13"
FT /id="PRO_0000099127"
FT MUTAGEN 17
FT /note="K->R: Confers 30% resistance to rifampicin."
FT /evidence="ECO:0000269|PubMed:17055024"
FT MUTAGEN 24
FT /note="V->F: Confers 35% resistance to rifampicin."
FT /evidence="ECO:0000269|PubMed:17055024"
FT MUTAGEN 25
FT /note="D->N: Confers 60% resistance to rifampicin."
FT /evidence="ECO:0000269|PubMed:17055024"
FT MUTAGEN 25
FT /note="D->V: Confers 45% resistance to rifampicin."
FT /evidence="ECO:0000269|PubMed:17055024"
FT MUTAGEN 26
FT /note="S->C: Confers 40% resistance to rifampicin."
FT /evidence="ECO:0000269|PubMed:17055024"
FT MUTAGEN 27
FT /note="Q->K: Confers 50% resistance to rifampicin."
FT /evidence="ECO:0000269|PubMed:17055024"
FT MUTAGEN 30
FT /note="T->I: Confers 50% resistance to rifampicin."
FT /evidence="ECO:0000269|PubMed:17055024"
FT MUTAGEN 33
FT /note="M->I: Confers 20% resistance to rifampicin."
FT /evidence="ECO:0000269|PubMed:17055024"
FT MUTAGEN 94
FT /note="C->Y: Confers 30% resistance to rifampicin."
FT /evidence="ECO:0000269|PubMed:17055024"
FT MUTAGEN 175
FT /note="D->Y: Confers 50% resistance to rifampicin."
FT /evidence="ECO:0000269|PubMed:17055024"
FT MUTAGEN 222
FT /note="V->A: Confers 40% resistance to rifampicin."
FT /evidence="ECO:0000269|PubMed:17055024"
FT MUTAGEN 227
FT /note="S->L: Confers 50% resistance to rifampicin."
FT /evidence="ECO:0000269|PubMed:17055024"
FT MUTAGEN 234
FT /note="R->I: Confers 50% resistance to rifampicin."
FT /evidence="ECO:0000269|PubMed:17055024"
FT MUTAGEN 243
FT /note="T->M: Confers 30% resistance to rifampicin."
FT /evidence="ECO:0000269|PubMed:17055024"
FT MUTAGEN 314
FT /note="E->K: Confers 30% resistance to rifampicin."
FT /evidence="ECO:0000269|PubMed:17055024"
FT MUTAGEN 429
FT /note="K->M: Confers 40% resistance to rifampicin."
FT /evidence="ECO:0000269|PubMed:17055024"
FT MUTAGEN 439
FT /note="I->N: Confers 45% resistance to rifampicin."
FT /evidence="ECO:0000269|PubMed:17055024"
FT MUTAGEN 465
FT /note="E->D: Confers 50% resistance to rifampicin."
FT /evidence="ECO:0000269|PubMed:17055024"
FT MUTAGEN 480
FT /note="N->D: Confers 80% resistance to rifampicin."
FT /evidence="ECO:0000269|PubMed:17055024"
FT MUTAGEN 484
FT /note="K->M: Confers 70% resistance to rifampicin."
FT /evidence="ECO:0000269|PubMed:17055024"
FT MUTAGEN 485
FT /note="I->L: Confers 60% resistance to rifampicin."
FT /evidence="ECO:0000269|PubMed:17055024"
FT MUTAGEN 485
FT /note="I->T: Confers 40% resistance to rifampicin."
FT /evidence="ECO:0000269|PubMed:17055024"
FT MUTAGEN 488
FT /note="R->M: Confers 40% resistance to rifampicin."
FT /evidence="ECO:0000269|PubMed:17055024"
FT MUTAGEN 511
FT /note="T->A: Confers 35% resistance to rifampicin."
FT /evidence="ECO:0000269|PubMed:17055024"
FT MUTAGEN 513
FT /note="D->G: Induces the protein to polymerize into flat,
FT purely hexagonal sheets instead of the curved
FT hexagonal/pentagonal coats that are normally seen on the
FT surface of IV membranes."
FT /evidence="ECO:0000269|PubMed:16144903"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:3SAM"
FT STRAND 32..40
FT /evidence="ECO:0007829|PDB:3SAM"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:3SAM"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:2YGC"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:3SAM"
FT STRAND 65..75
FT /evidence="ECO:0007829|PDB:3SAM"
FT STRAND 78..86
FT /evidence="ECO:0007829|PDB:3SAM"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:3SAM"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:3SAM"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:3SAM"
FT HELIX 112..119
FT /evidence="ECO:0007829|PDB:3SAM"
FT HELIX 123..128
FT /evidence="ECO:0007829|PDB:3SAM"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:3SAM"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:3SAM"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:3SAM"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:3SAM"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:3SAM"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:3SAM"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:3SAM"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:3SAM"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:3SAM"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:6BEI"
FT HELIX 199..205
FT /evidence="ECO:0007829|PDB:3SAM"
FT STRAND 210..219
FT /evidence="ECO:0007829|PDB:3SAM"
FT STRAND 227..236
FT /evidence="ECO:0007829|PDB:3SAM"
FT STRAND 242..247
FT /evidence="ECO:0007829|PDB:3SAM"
FT STRAND 250..262
FT /evidence="ECO:0007829|PDB:3SAM"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:6BEF"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:3SAM"
FT HELIX 280..295
FT /evidence="ECO:0007829|PDB:3SAM"
FT STRAND 296..302
FT /evidence="ECO:0007829|PDB:3SAM"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:3SAM"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:3SAM"
FT STRAND 326..334
FT /evidence="ECO:0007829|PDB:3SAM"
FT STRAND 340..344
FT /evidence="ECO:0007829|PDB:3SAM"
FT STRAND 347..350
FT /evidence="ECO:0007829|PDB:3SAM"
FT HELIX 361..364
FT /evidence="ECO:0007829|PDB:3SAM"
FT STRAND 365..373
FT /evidence="ECO:0007829|PDB:3SAM"
FT TURN 374..377
FT /evidence="ECO:0007829|PDB:3SAM"
FT STRAND 378..386
FT /evidence="ECO:0007829|PDB:3SAM"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:3SAM"
FT HELIX 397..400
FT /evidence="ECO:0007829|PDB:3SAM"
FT HELIX 414..418
FT /evidence="ECO:0007829|PDB:3SAM"
FT STRAND 421..423
FT /evidence="ECO:0007829|PDB:6BEB"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:6BEI"
FT STRAND 440..447
FT /evidence="ECO:0007829|PDB:3SAM"
FT STRAND 450..457
FT /evidence="ECO:0007829|PDB:3SAM"
FT HELIX 459..468
FT /evidence="ECO:0007829|PDB:3SAM"
FT STRAND 475..478
FT /evidence="ECO:0007829|PDB:3SAM"
FT TURN 484..486
FT /evidence="ECO:0007829|PDB:3SAM"
FT TURN 496..499
FT /evidence="ECO:0007829|PDB:3SAM"
FT STRAND 502..509
FT /evidence="ECO:0007829|PDB:3SAM"
FT HELIX 517..520
FT /evidence="ECO:0007829|PDB:3SAM"
FT STRAND 521..536
FT /evidence="ECO:0007829|PDB:3SAM"
FT STRAND 538..540
FT /evidence="ECO:0007829|PDB:6BEB"
FT STRAND 542..545
FT /evidence="ECO:0007829|PDB:3SAM"
SQ SEQUENCE 551 AA; 61891 MW; 5E75F14646330A0B CRC64;
MNNTIINSLI GGDDSIKRSN VFAVDSQIPT LYMPQYISLS GVMTNDGPDN QAIASFEIRD
QYITALNHLV LSLELPEVKG MGRFGYVPYV GYKCINHVSI SSCNGVIWEI EGEELYNNCI
NNTIALKHSG YSSELNDISI GLTPNDTIKE PSTVYVYIKT PFDVEDTFSS LKLSDSKITV
TVTFNPVSDI VIRDSSFDFE TFNKEFVYVP ELSFIGYMVK NVQIKPSFIE KPRRVIGQIN
QPTATVTEVH AATSLSVYTK PYYGNTDNKF ISYPGYSQDE KDYIDAYVSR LLDDLVIVSD
GPPTGYPESA EIVEVPEDGI VSIQDADVYV KIDNVPDNMS VYLHTNLLMF GTRKNSFIYN
ISKKFSAITG TYSDATKRTI FAHISHSINI IDTSIPVSLW TSQRNVYNGD NRSAESKAKD
LFINDPFIKG IDFKNKTDII SRLEVRFGND VLYSENGPIS RIYNELLTKS NNGTRTLTFN
FTPKIFFRPT TITANVSRGK DKLSVRVVYS TMDVNHPIYY VQKQLVVVCN DLYKVSYDQG
VSITKIMGDN N
