ID   RPOB_STREM              Reviewed;        1188 AA.
AC   B4U047;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=Sez_0108;
OS   Streptococcus equi subsp. zooepidemicus (strain MGCS10565).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=552526;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGCS10565;
RX   PubMed=18716664; DOI=10.1371/journal.pone.0003026;
RA   Beres S.B., Sesso R., Pinto S.W.L., Hoe N.P., Porcella S.F., Deleo F.R.,
RA   Musser J.M.;
RT   "Genome sequence of a lancefield group C Streptococcus zooepidemicus strain
RT   causing epidemic nephritis: new information about an old disease.";
RL   PLoS ONE 3:E3026-E3026(2008).
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; CP001129; ACG61490.1; -; Genomic_DNA.
DR   RefSeq; WP_012514773.1; NC_011134.1.
DR   AlphaFoldDB; B4U047; -.
DR   SMR; B4U047; -.
DR   EnsemblBacteria; ACG61490; ACG61490; Sez_0108.
DR   KEGG; sez:Sez_0108; -.
DR   HOGENOM; CLU_000524_4_1_9; -.
DR   OMA; FMTWEGY; -.
DR   Proteomes; UP000001873; 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; -; 1.
DR   Gene3D; 2.40.50.150; -; 1.
DR   Gene3D; 3.90.1110.10; -; 1.
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; 2.
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   TIGRFAMs; TIGR02013; rpoB; 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..1188
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_1000141740"
SQ   SEQUENCE   1188 AA;  132952 MW;  B0180677D1D5A7B5 CRC64;
     MAGHDVQYGK HRTRRSFSRI KEVLDLPNLI EIQTDSFQDF LDSGLKEVFE DVLPISNFTD
     TMELEFVGYE FKEPKYTLEE ARIHDASYSA PIFVTFRLIN KETGEIKTQE VFFGDFPIMT
     EMGTFIINGG ERIIVSQLVR SPGVYFNDKV DKNGKVGYGS TVIPNRGAWL ELETDSKDIA
     YTRIDRTRKI PFTTLVRALG FSGDDEIIDI FGDSELVRNT IEKDIHKNQS DSRTDEALKE
     IYERLRPGEP KTADSSRSLL TARFFDARRY DLAAVGRYKI NKKLNIKTRL LNQIIAENLI
     DSETGEILVE AGTEMTRSVI ESIEEQLDGD LNKFVYTPND YAVVTEPVIL QKFKVVSPVD
     PDRVVTIVGN ANPDDKVRAL TPADILAEMS YFLNLAEGLG KVDDIDHLGN RRIRAVGELL
     ANQFRIGLAR MERNVRERMS VQDNDVLTPQ QIINIRPVTA AVKEFFGSSQ LSQFMDQHNP
     LSELSHKRRL SALGPGGLTR DRAGYEVRDV HYTHYGRMCP IETPEGPNIG LINNLSSFGH
     LNKYGFIQTP YRKVDRVIGR VTNEIVWLTA DEEDEFTVAQ ANSKLNPDGT FAEEIVMGRH
     QGNNQEFPAS QVDFVDVSPK QVVAVATACI PFLENDDSNR ALMGANMQRQ AVPLIDPKAP
     YVGTGMEYQA AHDSGAAVIA QHNGKVVFSD AERVEVRRED GSLDVYHITK FRRSNSGTAY
     NQRTLVKIGD IVEKGDFIAD GPSMEKGEMA LGQNPIVAYM TWEGYNFEDA VIMSERLVKE
     DVYTSVHLEE FESETRDTKL GPEEITREVP NVGEEALKDL DEMGIIRIGA EVKEGDILVG
     KVTPKGEKDL SAEERLLHAI FGDKSREVRD TSLRVPHGGD GIVRDVKIFT RANGDELQSG
     VNMLVRVYIA QKRKIKVGDK MAGRHGNKGV VSRIVPVEDM PYLPDGTPVD IMLNPLGVPS
     RMNIGQVMEL HLGMAARNLG IHIATPVFDG ATSEDLWETV REAGMDSDAK TVLYDGRTGE
     PFDNRVSVGV MYMIKLHHMV DDKLHARSVG PYSLVTQQPL GGKAQFGGQR FGEMEVWALE
     AYGASNVLQE ILTYKSDDVN GRLKAYEAIT KGKPIPKPGV PESFRVLVKE LQSLGLDMRV
     LDEDDNEVEL RDLDEGEDDD VMHVDDLEKA REKQAQETQD IAESTEDN