PK_BPT7
ID PK_BPT7 Reviewed; 359 AA.
AC P00513;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Protein kinase 0.7;
DE EC=2.7.11.1;
DE AltName: Full=Gene product 0.7;
DE Short=Gp0.7;
DE AltName: Full=Protein kinase gp0.7;
GN OrderedLocusNames=0.7;
OS Escherichia phage T7 (Bacteriophage T7).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Autographiviridae; Studiervirinae; Teseptimavirus.
OX NCBI_TaxID=10760;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=6864790; DOI=10.1016/s0022-2836(83)80282-4;
RA Dunn J.J., Studier F.W.;
RT "Complete nucleotide sequence of bacteriophage T7 DNA and the locations of
RT T7 genetic elements.";
RL J. Mol. Biol. 166:477-535(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7310871; DOI=10.1016/0022-2836(81)90178-9;
RA Dunn J.J., Studier F.W.;
RT "Nucleotide sequence from the genetic left end of bacteriophage T7 DNA to
RT the beginning of gene 4.";
RL J. Mol. Biol. 148:303-330(1981).
RN [3]
RP FUNCTION IN PHOSPHORYLATION OF HOST RPOB AND RPOC.
RX PubMed=1101258; DOI=10.1073/pnas.72.7.2506;
RA Zillig W., Fujiki H., Blum W., Janekovic D., Schweiger M., Rahmsdorf H.,
RA Ponta H., Hirsch-Kauffmann M.;
RT "In vivo and in vitro phosphorylation of DNA-dependent RNA polymerase of
RT Escherichia coli by bacteriophage-T7-induced protein kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 72:2506-2510(1975).
RN [4]
RP FUNCTION.
RX PubMed=1310178; DOI=10.1016/0042-6822(92)90010-m;
RA Michalewicz J., Nicholson A.W.;
RT "Molecular cloning and expression of the bacteriophage T7 0.7(protein
RT kinase) gene.";
RL Virology 186:452-462(1992).
RN [5]
RP FUNCTION IN PHOSPHORYLATION OF HOST INFA; INFB; INFC AND RPSA.
RX PubMed=1534259; DOI=10.1021/bi00135a012;
RA Robertson E.S., Nicholson A.W.;
RT "Phosphorylation of Escherichia coli translation initiation factors by the
RT bacteriophage T7 protein kinase.";
RL Biochemistry 31:4822-4827(1992).
RN [6]
RP FUNCTION IN PHOSPHORYLATION OF HOST FUSA AND RPSF.
RX PubMed=8022276; DOI=10.1111/j.1365-2958.1994.tb00382.x;
RA Robertson E.S., Aggison L.A., Nicholson A.W.;
RT "Phosphorylation of elongation factor G and ribosomal protein S6 in
RT bacteriophage T7-infected Escherichia coli.";
RL Mol. Microbiol. 11:1045-1057(1994).
RN [7]
RP FUNCTION IN PHOSPHORYLATION OF HOST RNE AND RHLB.
RX PubMed=11722741; DOI=10.1046/j.1365-2958.2001.02668.x;
RA Marchand I., Nicholson A.W., Dreyfus M.;
RT "Bacteriophage T7 protein kinase phosphorylates RNase E and stabilizes
RT mRNAs synthesized by T7 RNA polymerase.";
RL Mol. Microbiol. 42:767-776(2001).
RN [8]
RP FUNCTION IN PHOSPHORYLATION OF HOST RPOC.
RX PubMed=16672600; DOI=10.1128/jb.188.10.3470-3476.2006;
RA Severinova E., Severinov K.;
RT "Localization of the Escherichia coli RNA polymerase beta' subunit residue
RT phosphorylated by bacteriophage T7 kinase Gp0.7.";
RL J. Bacteriol. 188:3470-3476(2006).
RN [9]
RP PHOSPHORYLATION AT SER-216.
RX PubMed=22951189; DOI=10.1016/j.pep.2012.08.008;
RA Gone S., Nicholson A.W.;
RT "Bacteriophage T7 protein kinase: Site of inhibitory autophosphorylation,
RT and use of dephosphorylated enzyme for efficient modification of protein in
RT vitro.";
RL Protein Expr. Purif. 85:218-223(2012).
CC -!- FUNCTION: Serine/threonine kinase that modulates host metabolism to
CC favor virus replication cycle. Participates together with gene 2
CC protein (gp2) in the host transcription shutoff. Phosphorylates host
CC RNA polymerase subunit RpoC and to a lesser extent subunit RpoB. This
CC modification seems to increase rho-dependent transcription termination,
CC which may help to switch from host to viral RNA polymerase
CC transcription during phage development. Phosphorylates host components
CC of the RNA degradosome rne and RhlB, leading to stabilization of mRNAs
CC synthesized by T7 RNA polymerase. Phosphorylates host dsRNA specific
CC processing enzyme RNase III/rnc, leading to enhance activity of the
CC ribonuclease that may increase maturation of T7 late transcripts
CC possessing multiple Rnase III processing sites. Phosphorylates several
CC components of the host translational machinery including initiation
CC factors InfA, InfB, and InfC, ribosomal subunit RpsA and RpsF, as well
CC as elongation factor G/FusA. These phosphorylations may enhance T7 late
CC protein production. {ECO:0000269|PubMed:1101258,
CC ECO:0000269|PubMed:11722741, ECO:0000269|PubMed:1310178,
CC ECO:0000269|PubMed:1534259, ECO:0000269|PubMed:16672600,
CC ECO:0000269|PubMed:8022276}.
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 -!- 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;
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DR EMBL; V01146; CAA24389.1; -; Genomic_DNA.
DR EMBL; V01127; CAA24332.1; -; Genomic_DNA.
DR PIR; D94615; KIBPO7.
DR RefSeq; NP_041959.1; NC_001604.1.
DR IntAct; P00513; 1.
DR MINT; P00513; -.
DR iPTMnet; P00513; -.
DR GeneID; 1261070; -.
DR KEGG; vg:1261070; -.
DR Proteomes; UP000000840; Genome.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR InterPro; IPR014374; Protein_kinase_T7-type.
DR PIRSF; PIRSF000547; Prot_kinase_T7; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Bacterial host gene expression shutoff by virus;
KW Bacterial host transcription shutoff by virus; Coiled coil;
KW Host gene expression shutoff by virus; Host-virus interaction; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..359
FT /note="Protein kinase 0.7"
FT /id="PRO_0000106465"
FT COILED 231..283
FT /evidence="ECO:0000255"
FT MOD_RES 216
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:22951189"
SQ SEQUENCE 359 AA; 41124 MW; 029457CA245B4308 CRC64;
MNITDIMNAI DAIKALPICE LDKRQGMLID LLVEMVNSET CDGELTELNQ ALEHQDWWTT
LKCLTADAGF KMLGNGHFSA AYSHPLLPNR VIKVGFKKED SGAAYTAFCR MYQGRPGIPN
VYDVQRHAGC YTVVLDALKD CERFNNDAHY KYAEIASDII DCNSDEHDEL TGWDGEFVET
CKLIRKFFEG IASFDMHSGN IMFSNGDVPY ITDPVSFSQK KDGGAFSIDP EELIKEVEEV
ARQKEIDRAK ARKERHEGRL EARRFKRRNR KARKAHKAKR ERMLAAWRWA ERQERRNHEV
AVDVLGRTNN AMLWVNMFSG DFKALEERIA LHWRNADRMA IANGLTLNID KQLDAMLMG
