ID   RPOB_MESHJ              Reviewed;        1220 AA.
AC   Q4A969;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE            Short=RNAP subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01321};
DE   AltName: Full=RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE   AltName: Full=Transcriptase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
GN   Name=rpoB {ECO:0000255|HAMAP-Rule:MF_01321}; OrderedLocusNames=MHJ_0618;
OS   Mesomycoplasma hyopneumoniae (strain J / ATCC 25934 / NCTC 10110)
OS   (Mycoplasma hyopneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mesomycoplasma.
OX   NCBI_TaxID=262719;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J / ATCC 25934 / NCTC 10110;
RX   PubMed=16077101; DOI=10.1128/jb.187.16.5568-5577.2005;
RA   Vasconcelos A.T.R., Ferreira H.B., Bizarro C.V., Bonatto S.L.,
RA   Carvalho M.O., Pinto P.M., Almeida D.F., Almeida L.G.P., Almeida R.,
RA   Alves-Junior L., Assuncao E.N., Azevedo V.A.C., Bogo M.R., Brigido M.M.,
RA   Brocchi M., Burity H.A., Camargo A.A., Camargo S.S., Carepo M.S.,
RA   Carraro D.M., de Mattos Cascardo J.C., Castro L.A., Cavalcanti G.,
RA   Chemale G., Collevatti R.G., Cunha C.W., Dallagiovanna B., Dambros B.P.,
RA   Dellagostin O.A., Falcao C., Fantinatti-Garboggini F., Felipe M.S.S.,
RA   Fiorentin L., Franco G.R., Freitas N.S.A., Frias D., Grangeiro T.B.,
RA   Grisard E.C., Guimaraes C.T., Hungria M., Jardim S.N., Krieger M.A.,
RA   Laurino J.P., Lima L.F.A., Lopes M.I., Loreto E.L.S., Madeira H.M.F.,
RA   Manfio G.P., Maranhao A.Q., Martinkovics C.T., Medeiros S.R.B.,
RA   Moreira M.A.M., Neiva M., Ramalho-Neto C.E., Nicolas M.F., Oliveira S.C.,
RA   Paixao R.F.C., Pedrosa F.O., Pena S.D.J., Pereira M., Pereira-Ferrari L.,
RA   Piffer I., Pinto L.S., Potrich D.P., Salim A.C.M., Santos F.R., Schmitt R.,
RA   Schneider M.P.C., Schrank A., Schrank I.S., Schuck A.F., Seuanez H.N.,
RA   Silva D.W., Silva R., Silva S.C., Soares C.M.A., Souza K.R.L., Souza R.C.,
RA   Staats C.C., Steffens M.B.R., Teixeira S.M.R., Urmenyi T.P.,
RA   Vainstein M.H., Zuccherato L.W., Simpson A.J.G., Zaha A.;
RT   "Swine and poultry pathogens: the complete genome sequences of two strains
RT   of Mycoplasma hyopneumoniae and a strain of Mycoplasma synoviae.";
RL   J. Bacteriol. 187:5568-5577(2005).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       {ECO:0000255|HAMAP-Rule:MF_01321}.
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:0000255|HAMAP-Rule:MF_01321};
CC   -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta'
CC       and 1 omega subunit. When a sigma factor is associated with the core
CC       the holoenzyme is formed, which can initiate transcription.
CC       {ECO:0000255|HAMAP-Rule:MF_01321}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_01321}.
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DR   EMBL; AE017243; AAZ44702.1; -; Genomic_DNA.
DR   RefSeq; WP_011284347.1; NC_007295.1.
DR   AlphaFoldDB; Q4A969; -.
DR   SMR; Q4A969; -.
DR   STRING; 262719.MHJ_0618; -.
DR   EnsemblBacteria; AAZ44702; AAZ44702; MHJ_0618.
DR   KEGG; mhj:MHJ_0618; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_1_14; -.
DR   OMA; FMTWEGY; -.
DR   Proteomes; UP000000548; Chromosome.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   CDD; cd00653; RNA_pol_B_RPB2; 1.
DR   Gene3D; 2.30.150.10; -; 1.
DR   Gene3D; 2.40.270.10; -; 2.
DR   Gene3D; 2.40.50.150; -; 1.
DR   Gene3D; 3.90.1110.10; -; 2.
DR   HAMAP; MF_01321; RNApol_bact_RpoB; 1.
DR   InterPro; IPR042107; DNA-dir_RNA_pol_bsu_ext_1_sf.
DR   InterPro; IPR019462; DNA-dir_RNA_pol_bsu_external_1.
DR   InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR   InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR   InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR   InterPro; IPR010243; RNA_pol_bsu_bac.
DR   InterPro; IPR007121; RNA_pol_bsu_CS.
DR   InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR   InterPro; IPR007642; RNA_pol_Rpb2_2.
DR   InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR   InterPro; IPR007645; RNA_pol_Rpb2_3.
DR   InterPro; IPR007641; RNA_pol_Rpb2_7.
DR   InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR   PANTHER; PTHR20856; PTHR20856; 1.
DR   Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR   Pfam; PF04561; RNA_pol_Rpb2_2; 1.
DR   Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR   Pfam; PF10385; RNA_pol_Rpb2_45; 1.
DR   Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR   Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR   PROSITE; PS01166; RNA_POL_BETA; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Nucleotidyltransferase; Transcription;
KW   Transferase.
FT   CHAIN           1..1220
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000224077"
SQ   SEQUENCE   1220 AA;  137715 MW;  4843AB8DB6A44BDB CRC64;
     MNHIYKLKSY GIGTDRRFYG VANKTLETPD FLDPVRESFD WFLHVGIPEA FDRIFPIVSA
     NGKLEISFRR GSLRVEKPEN EYLAIREAKI KGKTYSARVY VTLVKVHSED GEMEEQEILL
     AEFPFMTQGG TFIINGFEKV VVSQLIRSPG VCFRENVRNQ QADDLFNKVE IIPQLGSWME
     IFHKVTGNQV DTVKFRIDKH KNIPLLSFLR AIGFTNETVR KYFGNSPELL ESIRRHKLES
     LEENLELIYR IVRKDDRITE EGLKNLIPSI IFNERRYNLA STGRFMLNAK LNLVERISQT
     YLAEDLVSKK NKILFKKGTY ITRQLALEIQ EKFNNEEIPL SEIEGVDSTI YARQLEITRN
     ENLWKRFYVA IVKVWPNKKS MLQESEPVNV IATDPNLNEK TLVLSDIIAI VSYYFNLLSN
     LGKSDDPDSL VNKRIVSVGE LLQNQFLIAL TKIEKNSKEK ISTKSDLSQL TVKSIINNKP
     IYNQFKNFFN SSKLSQFMDQ INPLGEMASK RKVTSLGPGG LNRDTAQFEV RDVHTTHYGR
     ICPVETPEGQ NIGLILNFSV FSRINQYGFI ITPYYQVKNR IVDYSKVHWL AASEEFDKSF
     AQSGVEIDQN NRIIPDKLTV RKNQTYLVLD AEQVNYIDVS SMQMTSISAS AIPFLENNDA
     NRALMGSNMQ RQAVPLIKSE APLVATGIEE AVARFSATNL RASISGKVTY VDAKKIIIDD
     GEKPEIHYLR YFEKSNQETL ILQKPTVKVG DKVKKGQLIC DGPSTDNGEL ALGKNVLVAF
     STWYGYNYED AIIISEKLVK DDVFTSIHIQ EQTIKFRSTK AGNDILTAEI PNASAKSRLH
     LDANGIVIVG SEVDTGDILV GRTSPKGEDN PTAEEKLMAA IWGKKALAQK DTSLRVKNGE
     GGTVIDVQIL SRDQGDNLEE GVGMLIKILI AQKRKIKVGD KMAGRHGNKG VVSVILPVED
     MPFLEDGTPV DIVLNPQGVP SRMNIGQVLE LHLGMVAKKL KTKFVTPVFD GIKIETIKKL
     FDEANIPESG KFKLFDGISG QPFENPVSVG YMYMLKLLHM VDDKMHARSI GPYSLTTQQP
     LGGKSQNGGQ RFGEMETWAL ESFGATSVLS ELLTYKSDNI QGRNLLYNNI ISGGKIPSPG
     TPESFNVLAY ELRGLLIKLE VHKNDQENQE VEEIKDPLEL PEIPSNFIDE YNQDGRIELN
     KLEEFADFDE ENIDFDKLTR