B1_VACCC
ID B1_VACCC Reviewed; 300 AA.
AC P20505;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=B1 kinase;
DE AltName: Full=Serine/threonine-protein kinase 1;
DE EC=2.7.11.1;
DE AltName: Full=Vaccinia protein kinase 1;
GN Name=VPK1; ORFNames=B1R;
OS Vaccinia virus (strain Copenhagen) (VACV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10249;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2219722; DOI=10.1016/0042-6822(90)90294-2;
RA Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA Paoletti E.;
RT "The complete DNA sequence of vaccinia virus.";
RL Virology 179:247-266(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA Paoletti E.;
RT "Appendix to 'The complete DNA sequence of vaccinia virus'.";
RL Virology 179:517-563(1990).
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 In addition, inhibits B12 repressive activity on viral DNA replication
CC via a phosphorylation-dependent mechanism.
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 Interacts with protein B12; this interaction inhibits the repressive
CC activity of B12 pseudokinase on viral replication factory formation.
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 -!- INDUCTION: Expressed early in the viral replication cycle.
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; M35027; AAA48194.1; -; Genomic_DNA.
DR PIR; I42525; TVVZ9Z.
DR SMR; P20505; -.
DR IntAct; P20505; 3.
DR MINT; P20505; -.
DR BRENDA; 2.7.11.1; 6591.
DR Proteomes; UP000008269; 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 2: Evidence at transcript level;
KW ATP-binding; Host cytoplasm; Host-virus interaction; Kinase; Magnesium;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Virion.
FT CHAIN 1..300
FT /note="B1 kinase"
FT /id="PRO_0000086791"
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; 34302 MW; 1FDB517490497142 CRC64;
MNFQGLVLTD NCKNQWVVGP LIGKGGFGSI YTTNDNNYVV KIEPKANGSL FTEQAFYTRV
LKPSVIEEWK KSHNIKHVGL ITCKAFGLYK SINVEYRFLV INRLGVDLDA VIRANNNRLP
KRSVMLIGIE ILNTIQFMHE QGYSHGDIKA SNIVLDQIDK NKLYLVDYGL VSKFMSNGEH
VPFIRNPNKM DNGTLEFTPI DSHKGYVVSR RGDLETLGYC MIRWLGGILP WTKISETKNC
ALVSATKQKY VNNTATLLMT SLQYAPRELL QYITMVNSLT YFEEPNYDEF RHILMQGVYY
