B1_VACCW
ID B1_VACCW Reviewed; 300 AA.
AC P16913; Q76ZM2;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=B1 kinase;
DE AltName: Full=Serine/threonine-protein kinase 1;
DE EC=2.7.11.1 {ECO:0000269|PubMed:1602551};
DE AltName: Full=Vaccinia protein kinase 1;
GN Name=VPK1; OrderedLocusNames=VACWR183; ORFNames=B1R;
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=2600076; DOI=10.1016/s0021-9258(20)88203-9;
RA Traktman P., Anderson M.K., Rempel R.E.;
RT "Vaccinia virus encodes an essential gene with strong homology to protein
RT kinases.";
RL J. Biol. Chem. 264:21458-21461(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2607336; DOI=10.1099/0022-1317-70-12-3187;
RA Howard S.T., Smith G.L.;
RT "Two early vaccinia virus genes encode polypeptides related to protein
RT kinases.";
RL J. Gen. Virol. 70:3187-3201(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2045793; DOI=10.1099/0022-1317-72-6-1349;
RA Smith G.L., Chan Y.S., Howard S.T.;
RT "Nucleotide sequence of 42 kbp of vaccinia virus strain WR from near the
RT right inverted terminal repeat.";
RL J. Gen. Virol. 72:1349-1376(1991).
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 SUBCELLULAR LOCATION.
RX PubMed=1448924; DOI=10.1016/0042-6822(92)90256-o;
RA Banham A.H., Smith G.L.;
RT "Vaccinia virus gene B1R encodes a 34-kDa serine/threonine protein kinase
RT that localizes in cytoplasmic factories and is packaged into virions.";
RL Virology 191:803-812(1992).
RN [6]
RP FUNCTION.
RX PubMed=1560522; DOI=10.1128/jvi.66.5.2717-2723.1992;
RA Lin S., Chen W., Broyles S.S.;
RT "The vaccinia virus B1R gene product is a serine/threonine protein
RT kinase.";
RL J. Virol. 66:2717-2723(1992).
RN [7]
RP FUNCTION, COFACTOR, AND MUTAGENESIS OF GLY-79 AND GLY-227.
RC STRAIN=mutant ts2, and mutant ts25;
RX PubMed=1602551; DOI=10.1128/jvi.66.7.4413-4426.1992;
RA Rempel R.E., Traktman P.;
RT "Vaccinia virus B1 kinase: phenotypic analysis of temperature-sensitive
RT mutants and enzymatic characterization of recombinant proteins.";
RL J. Virol. 66:4413-4426(1992).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF GLY-227.
RX PubMed=11287554; DOI=10.1128/jvi.75.9.4048-4055.2001;
RA Kovacs G.R., Vasilakis N., Moss B.;
RT "Regulation of viral intermediate gene expression by the vaccinia virus B1
RT protein kinase.";
RL J. Virol. 75:4048-4055(2001).
RN [9]
RP FUNCTION, AND INTERACTION WITH HOST JIP1.
RX PubMed=16840345; DOI=10.1128/jvi.00967-06;
RA Santos C.R., Blanco S., Sevilla A., Lazo P.A.;
RT "Vaccinia virus B1R kinase interacts with JIP1 and modulates c-Jun-
RT dependent signaling.";
RL J. Virol. 80:7667-7675(2006).
RN [10]
RP FUNCTION.
RX PubMed=18005698; DOI=10.1016/j.chom.2007.03.007;
RA Wiebe M.S., Traktman P.;
RT "Poxviral B1 kinase overcomes barrier to autointegration factor, a host
RT defense against virus replication.";
RL Cell Host Microbe 1:187-197(2007).
RN [11]
RP FUNCTION.
RX PubMed=23891157; DOI=10.1016/j.virol.2013.07.002;
RA Ibrahim N., Wicklund A., Jamin A., Wiebe M.S.;
RT "Barrier to autointegration factor (BAF) inhibits vaccinia virus
RT intermediate transcription in the absence of the viral B1 kinase.";
RL Virology 444:363-373(2013).
RN [12]
RP FUNCTION.
RX PubMed=24600006; DOI=10.1128/jvi.00427-14;
RA Jamin A., Wicklund A., Wiebe M.S.;
RT "Cell- and virus-mediated regulation of the barrier-to-autointegration
RT factor's phosphorylation state controls its DNA binding, dimerization,
RT subcellular localization, and antipoxviral activity.";
RL J. Virol. 88:5342-5355(2014).
RN [13]
RP FUNCTION.
RX PubMed=26223647; DOI=10.1128/jvi.01252-15;
RA Jamin A., Ibrahim N., Wicklund A., Weskamp K., Wiebe M.S.;
RT "Vaccinia virus B1 kinase is required for postreplicative stages of the
RT viral life cycle in a BAF-Independent manner in U2OS cells.";
RL J. Virol. 89:10247-10259(2015).
RN [14]
RP FUNCTION.
RX PubMed=28636603; DOI=10.1038/nature22814;
RA Jha S., Rollins M.G., Fuchs G., Procter D.J., Hall E.A., Cozzolino K.,
RA Sarnow P., Savas J.N., Walsh D.;
RT "Trans-kingdom mimicry underlies ribosome customization by a poxvirus
RT kinase.";
RL Nature 546:651-655(2017).
RN [15]
RP DISRUPTION PHENOTYPE.
RX PubMed=28515294; DOI=10.1128/jvi.00635-17;
RA Olson A.T., Rico A.B., Wang Z., Delhon G., Wiebe M.S.;
RT "Deletion of the vaccinia virus B1 kinase reveals essential functions of
RT this enzyme complemented partly by the homologous cellular kinase VRK2.";
RL J. Virol. 91:0-0(2017).
RN [16]
RP FUNCTION, AND INTERACTION WITH B12.
RX PubMed=31341052; DOI=10.1128/jvi.00855-19;
RA Rico A.B., Wang Z., Olson A.T., Linville A.C., Bullard B.L., Weaver E.A.,
RA Jones C., Wiebe M.S.;
RT "The Vaccinia Virus (VACV) B1 and Cellular VRK2 Kinases Promote VACV
RT Replication Factory Formation through Phosphorylation-Dependent Inhibition
RT of VACV B12.";
RL J. Virol. 93:0-0(2019).
CC -!- FUNCTION: Essential serine/threonine-protein kinase that plays
CC different role in the viral life cycle (PubMed:1560522,
CC PubMed:1602551). Phosphorylates the host small ribosomal protein RACK1
CC thereby customizing the ribosomes to a state optimal for viral mRNAs
CC (which contain poly-A leaders) but not for host mRNAs
CC (PubMed:28636603). Facilitates viral DNA replication by inhibiting host
CC BANF1, a cellular host defense responsive to foreign DNA
CC (PubMed:18005698, PubMed:1602551). Phosphorylates host BANF1 on serine
CC and threonine residues; this leads to BANF1 relocalization to the
CC cytoplasm, loss of dimerization and impaired DNA binding activity
CC (PubMed:24600006). Indeed, BANF1 activity depends on its DNA-binding
CC property which is blocked by VPK1-mediated phosphorylation
CC (PubMed:18005698). Required for viral intermediate genes expression,
CC probably by inhibiting host BANF1 (PubMed:11287554, PubMed:23891157).
CC Modulates cellular responses via host JUN by two different mechanisms,
CC either by direct phosphorylation or by modulation of upstream JIP1-MAPK
CC complexes (PubMed:16840345). Seems to participate in the
CC accumulation/processing of late proteins and thus in virion maturation
CC (PubMed:26223647). In addition, inhibits B12 repressive activity on
CC viral DNA replication via a phosphorylation-dependent mechanism
CC (PubMed:31341052). {ECO:0000269|PubMed:11287554,
CC ECO:0000269|PubMed:1560522, ECO:0000269|PubMed:1602551,
CC ECO:0000269|PubMed:16840345, ECO:0000269|PubMed:18005698,
CC ECO:0000269|PubMed:23891157, ECO:0000269|PubMed:24600006,
CC ECO:0000269|PubMed:26223647, ECO:0000269|PubMed:28636603,
CC ECO:0000269|PubMed:31341052}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:1602551};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:1602551};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:1602551};
CC -!- SUBUNIT: Interacts with host JIP1; this interaction increases the
CC amount of MAPK bound to JIP1 and subsequently increases the activity of
CC transcription factors, such as JUN, that respond to these complexes.
CC Interacts with protein B12; this interaction inhibits the repressive
CC activity of B12 pseudokinase on viral replication factory formation
CC (PubMed:31341052). {ECO:0000269|PubMed:16840345,
CC ECO:0000269|PubMed:31341052}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:1448924}. Host
CC cytoplasm {ECO:0000269|PubMed:1448924}. Note=Localizes in cytoplasmic
CC viral factories and is a minor component of the virion.
CC {ECO:0000269|PubMed:1448924}.
CC -!- INDUCTION: Expressed early in the viral replication cycle.
CC -!- PTM: Autophosphorylated.
CC -!- DISRUPTION PHENOTYPE: Up to 650-fold decreased virus production.
CC {ECO:0000269|PubMed:28515294}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. Poxviruses subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; D11079; BAA01831.1; -; Genomic_DNA.
DR EMBL; J05178; AAA47963.1; -; Genomic_DNA.
DR EMBL; D00628; BAA00519.1; -; Genomic_DNA.
DR EMBL; AY243312; AAO89462.1; -; Genomic_DNA.
DR PIR; A34152; TVVZVW.
DR RefSeq; YP_233065.1; NC_006998.1.
DR SMR; P16913; -.
DR BioGRID; 3509008; 3.
DR DIP; DIP-2170N; -.
DR IntAct; P16913; 1.
DR MINT; P16913; -.
DR DNASU; 3707654; -.
DR GeneID; 3707654; -.
DR KEGG; vg:3707654; -.
DR BRENDA; 2.7.11.1; 6591.
DR Proteomes; UP000000344; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0019068; P:virion assembly; IDA:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Host cytoplasm; Kinase; Magnesium; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Viral release from host cell; Virion.
FT CHAIN 1..300
FT /note="B1 kinase"
FT /id="PRO_0000086792"
FT DOMAIN 16..282
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 147
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 22..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 79
FT /note="G->D: Complete loss of enzymatic activity and loss
FT of viral intermediate gene expression (mutant ts2)."
FT /evidence="ECO:0000269|PubMed:11287554,
FT ECO:0000269|PubMed:1602551"
FT MUTAGEN 227
FT /note="G->S: 97% loss of enzymatic activity (mutant ts25)."
FT /evidence="ECO:0000269|PubMed:1602551"
SQ SEQUENCE 300 AA; 34274 MW; 04C9D7F08DC0F7C6 CRC64;
MNFQGLVLTD NCKNQWVVGP LIGKGGFGSI YTTNDNNYVV KIEPKANGSL FTEQAFYTRV
LKPSVIEEWK KSHNIKHVGL ITCKAFGLYK SINVEYRFLV INRLGADLDA VIRANNNRLP
KRSVMLIGIE ILNTIQFMHE QGYSHGDIKA SNIVLDQIDK NKLYLVDYGL VSKFMSNGEH
VPFIRNPNKM DNGTLEFTPI DSHKGYVVSR RGDLETLGYC MIRWLGGILP WTKISETKNC
ALVSATKQKY VNNTATLLMT SLQYAPRELL QYITMVNSLT YFEEPNYDEF RHILMQGVYY
