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RPOB_MESH2
ID   RPOB_MESH2              Reviewed;        1220 AA.
AC   Q5ZZS1;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=mhp636;
OS   Mesomycoplasma hyopneumoniae (strain 232) (Mycoplasma hyopneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mesomycoplasma.
OX   NCBI_TaxID=295358;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=232;
RX   PubMed=15489423; DOI=10.1128/jb.186.21.7123-7133.2004;
RA   Minion F.C., Lefkowitz E.J., Madsen M.L., Cleary B.J., Swartzell S.M.,
RA   Mahairas G.G.;
RT   "The genome sequence of Mycoplasma hyopneumoniae strain 232, the agent of
RT   swine mycoplasmosis.";
RL   J. Bacteriol. 186:7123-7133(2004).
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; AE017332; AAV28003.1; -; Genomic_DNA.
DR   RefSeq; WP_011206467.1; NC_006360.1.
DR   AlphaFoldDB; Q5ZZS1; -.
DR   SMR; Q5ZZS1; -.
DR   STRING; 295358.mhp636; -.
DR   EnsemblBacteria; AAV28003; AAV28003; mhp636.
DR   KEGG; mhy:mhp636; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_1_14; -.
DR   OMA; FMTWEGY; -.
DR   PhylomeDB; Q5ZZS1; -.
DR   Proteomes; UP000006822; 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_0000224075"
SQ   SEQUENCE   1220 AA;  137630 MW;  424F0C4B7CC13BDC 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 RAAISGKVTY 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 QAFENPVSVG YMYMLKLLHM VDDKMHARSI GPYSLTTQQP
     LGGKSQNGGQ RFGEMETWAL ESFGATSVLS ELLTYKSDNI QGRNLLYNNI ISGGKIPSPG
     TPESFNVLAY ELRGLLIKLE VHKNDQENQE GEEIKDPLEL PEIPSNFIDE YNQDGRIELN
     KLEEFADFDE ENIDFDKLTR
 
 
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