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