ID   YONO_BPSPB              Reviewed;         839 AA.
AC   O64076;
DT   05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=DNA-directed RNA polymerase YonO;
DE            EC=2.7.7.6 {ECO:0000305|PubMed:28585540};
DE   AltName: Full=DNA-dependent RNA polymerase YonO {ECO:0000303|PubMed:28585540};
GN   Name=yonO;
OS   Bacillus phage SPbeta (Bacillus phage SPBc2) (Bacteriophage SP-beta).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae; Spbetavirus.
OX   NCBI_TaxID=66797;
OH   NCBI_TaxID=1408; Bacillus pumilus (Bacillus mesentericus).
OH   NCBI_TaxID=1423; Bacillus subtilis.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9465078; DOI=10.1073/pnas.95.4.1692;
RA   Lazarevic V., Soldo B., Duesterhoeft A., Hilbert H., Maueel C.,
RA   Karamata D.;
RT   "Introns and intein coding sequence in the ribonucleotide reductase genes
RT   of Bacillus subtilis temperate bacteriophage SPbeta.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:1692-1697(1998).
RN   [2]
RP   FUNCTION.
RX   PubMed=28585540; DOI=10.1038/ncomms15774;
RA   Forrest D., James K., Yuzenkova Y., Zenkin N.;
RT   "Single-peptide DNA-dependent RNA polymerase homologous to multi-subunit
RT   RNA polymerase.";
RL   Nat. Commun. 8:15774-15774(2017).
CC   -!- FUNCTION: A single subunit DNA-dependent RNA polymerase (RNAP) that
CC       catalyzes the transcription of DNA into RNA using the four
CC       ribonucleoside triphosphates (rNTPs) as substrates. The enzyme is more
CC       highly processive than the multisubunit RNAP from E.coli but is
CC       considerably more error-prone. It has no detectable proof-reading
CC       function but can perform pyrophosphorolysis. Probably transcribes the
CC       late genes of the SPbeta phage starting from yonK.
CC       {ECO:0000305|PubMed:28585540}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC         EC=2.7.7.6; Evidence={ECO:0000305|PubMed:28585540};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000305|PubMed:28585540};
CC   -!- SIMILARITY: Belongs to the YRH RNA polymerase family. {ECO:0000305}.
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DR   EMBL; AF020713; AAC13036.1; -; Genomic_DNA.
DR   PIR; T12827; T12827.
DR   RefSeq; NP_046615.1; NC_001884.1.
DR   GeneID; 1261348; -.
DR   KEGG; vg:1261348; -.
DR   BRENDA; 2.7.7.6; 8808.
DR   Proteomes; UP000009091; Genome.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Reference proteome; Transcription; Transferase.
FT   CHAIN           1..839
FT                   /note="DNA-directed RNA polymerase YonO"
FT                   /id="PRO_0000447365"
FT   BINDING         535
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8T7,
FT                   ECO:0000305|PubMed:28585540"
FT   BINDING         537
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8T7,
FT                   ECO:0000305|PubMed:28585540"
FT   BINDING         539
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8T7,
FT                   ECO:0000305|PubMed:28585540"
SQ   SEQUENCE   839 AA;  97979 MW;  6373C4EBA9A92C98 CRC64;
     MKGKKDGLNK QVHIYSIDTS AFYNDQENKL HNKILKSYRY RDHLRKLEHV DKKHKKYITQ
     RIISLKEKLY NAFNDHNQIR TLRTDSLKDN NVISLFDSVL TRTLGIKENS LSEEIMVVQT
     YHFQILRDII DKGFIHNNEK YVYFTSSAGQ IRTKKSCFIK QSTLDKYQNA LTCGLSVEHI
     NAQGGSSINK WNSYMALSNS ASSSWEIDID KAIVVNDLET NVSSLVDYID RDTYEITRKI
     MDIPIEHTDG CGMMLPSLSQ KSFMVRLPWV KGLLVPFDFR KFAEKHSSFI VKDVYGKEWD
     IIKDDIQIIF TKSQFKMWKY YDSWDDYRYK FKKYGCLGAK LNEEDPSVEG KLTYQMLQTL
     TDITDEELKQ ISSKTVSEIT QLGTDKETMM KVLGATEKNK HKTSLQEALL IYPELLNDDH
     TKEIIKNKKK SMIKDAKSGK LLVSDARYTY LCPDLYAFCE RLFLGIESPK GLLSGSDVHC
     SLYDEGYIDI LRSPHLFREH GVRWNKKNEE YEKWFITPGV YTSIHDPISK LLQFDNDGDK
     ALIISDELIV NIAKRNMADI VPLYYEMSVA QKQEINSRNI YEALTLAYGI NIGEYSNNIT
     KIWNSDNINL DVIKWLCMEN NFTIDFAKTL FMPTRPDHVD EKIKDYIKNK VPHFFINAKD
     KEEHSVESIN ESTVNKLDSI IPSDRINFAA VAGKFDYRFL LKNKEIKLNE AVINEYKRLD
     RNKKWLMNDE EAKPGQKLYV YKIIKQKLLE IHNDDGFITD VLVKHLYKKK SKYKSTLWEC
     FGDIVLENIK HNLKTFKGCC ICGKAFKPTS NKAKYCQSCG KKKERDKYKK YNKKRINHR