YONO_BACSU
ID YONO_BACSU Reviewed; 839 AA.
AC O31945;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=DNA-directed RNA polymerase YonO;
DE EC=2.7.7.6 {ECO:0000269|PubMed:28585540};
DE AltName: Full=DNA-dependent RNA polymerase YonO {ECO:0000303|PubMed:28585540};
DE AltName: Full=SPbeta prophage-derived protein YonO;
GN Name=yonO; OrderedLocusNames=BSU21040;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP DISCUSSION OF SEQUENCE.
RX PubMed=12553882; DOI=10.1186/1472-6807-3-1;
RA Iyer L.M., Koonin E.V., Aravind L.;
RT "Evolutionary connection between the catalytic subunits of DNA-dependent
RT RNA polymerases and eukaryotic RNA-dependent RNA polymerases and the origin
RT of RNA polymerases.";
RL BMC Struct. Biol. 3:1-1(2003).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP INDUCTION BY MITOMYCIN C, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 535-ASP--ASP-539.
RC STRAIN=168;
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. Transcribes the late genes
CC of the SPbeta prophage starting from yonK (approximately 35 genes are
CC encoded in the prophage downstream from yonK).
CC {ECO:0000269|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:0000269|PubMed:28585540};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:28585540};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:28585540};
CC Note=Uses Mg(2+) and Mn(2+) equivalently.
CC {ECO:0000269|PubMed:28585540};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.8 uM for ATP (at 10 degrees Celsius)
CC {ECO:0000269|PubMed:28585540};
CC -!- INDUCTION: No expression under phage non-inducing conditions; induced
CC by mitomycin C (at protein level). {ECO:0000269|PubMed:28585540}.
CC -!- DISRUPTION PHENOTYPE: No longer forms lytic phage.
CC {ECO:0000269|PubMed:28585540}.
CC -!- MISCELLANEOUS: Encoded by the SPbeta prophage. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the YRH RNA polymerase family.
CC {ECO:0000305|PubMed:12553882}.
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DR EMBL; AL009126; CAB14022.1; -; Genomic_DNA.
DR RefSeq; NP_389987.1; NC_000964.3.
DR RefSeq; WP_004399271.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; O31945; -.
DR STRING; 224308.BSU21040; -.
DR PaxDb; O31945; -.
DR PRIDE; O31945; -.
DR EnsemblBacteria; CAB14022; CAB14022; BSU_21040.
DR GeneID; 939167; -.
DR KEGG; bsu:BSU21040; -.
DR PATRIC; fig|224308.179.peg.2298; -.
DR eggNOG; ENOG502ZBCM; Bacteria.
DR BioCyc; BSUB:BSU21040-MON; -.
DR Proteomes; UP000001570; Chromosome.
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 1: Evidence at protein level;
KW DNA-directed RNA polymerase; Magnesium; Manganese; Metal-binding;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase.
FT CHAIN 1..839
FT /note="DNA-directed RNA polymerase YonO"
FT /id="PRO_0000360544"
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"
FT MUTAGEN 535..539
FT /note="DNDGD->NNNGN: Loss of RNA polymerase activity."
FT /evidence="ECO:0000269|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
