B1_VACCA
ID B1_VACCA Reviewed; 300 AA.
AC O57252;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=B1 kinase;
DE AltName: Full=Serine/threonine-protein kinase 1;
DE EC=2.7.11.1;
GN Name=VPK1; OrderedLocusNames=MVA167R, ACAM3000_MVA_167; ORFNames=B1R;
OS Vaccinia virus (strain Ankara) (VACV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=126794;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9601507; DOI=10.1006/viro.1998.9123;
RA Antoine G., Scheiflinger F., Dorner F., Falkner F.G.;
RT "The complete genomic sequence of the modified vaccinia Ankara strain:
RT comparison with other orthopoxviruses.";
RL Virology 244:365-396(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate Acambis 3000;
RA Esposito J.J., Frace M., Sammons S.A., Olsen-Rasmussen M.S., Osborne J.,
RA Khristova M., Wohlhueter R.M.;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential serine/threonine-protein kinase that plays
CC different role in the viral life cycle. Phosphorylates the host small
CC ribosomal protein RACK1 thereby customizing the ribosomes to a state
CC optimal for viral mRNAs (which contain poly-A leaders) but not for host
CC mRNAs. Facilitates viral DNA replication by inhibiting host BANF1, a
CC cellular host defense responsive to foreign DNA. Phosphorylates host
CC BANF1 on serine and threonine residues; this leads to BANF1
CC relocalization to the cytoplasm, loss of dimerization and impaired DNA
CC binding activity. Indeed, BANF1 activity depends on its DNA-binding
CC property which is blocked by VPK1-mediated phosphorylation. Required
CC for viral intermediate genes expression, probably by inhibiting host
CC BANF1. Modulates cellular responses via host JUN by two different
CC mechanisms, either by direct phosphorylation or by modulation of
CC upstream JIP1-MAPK complexes. Seems to participate in the
CC accumulation/processing of late proteins and thus in virion maturation.
CC {ECO:0000250|UniProtKB:P16913}.
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:0000250|UniProtKB:P16913};
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:0000250|UniProtKB:P16913};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P16913};
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 {ECO:0000250|UniProtKB:P16913}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P16913}. Host
CC cytoplasm {ECO:0000250|UniProtKB:P16913}. Note=Localizes in cytoplasmic
CC viral factories and is a minor component of the virion.
CC {ECO:0000250|UniProtKB:P16913}.
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:P16913}.
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; U94848; AAB96545.1; -; Genomic_DNA.
DR EMBL; AY603355; AAT10565.1; -; Genomic_DNA.
DR PIR; T37440; T37440.
DR SMR; O57252; -.
DR Proteomes; UP000159908; Genome.
DR Proteomes; UP000172909; 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: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 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 3: Inferred from homology;
KW ATP-binding; Host cytoplasm; Kinase; Magnesium; Nucleotide-binding;
KW Phosphoprotein; Serine/threonine-protein kinase; Transferase; Virion.
FT CHAIN 1..300
FT /note="B1 kinase"
FT /id="PRO_0000086790"
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"
SQ SEQUENCE 300 AA; 34273 MW; 04C9D7FD3BC0F7C6 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 YFEEPNYDKF RHILMQGVYY
