ID   RPOB_STRPF              Reviewed;        1188 AA.
AC   Q1J8X1;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
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};
GN   OrderedLocusNames=MGAS10750_Spy0090;
OS   Streptococcus pyogenes serotype M4 (strain MGAS10750).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=370554;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS10750;
RX   PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA   Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R.,
RA   Musser J.M.;
RT   "Molecular genetic anatomy of inter- and intraserotype variation in the
RT   human bacterial pathogen group A Streptococcus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
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; CP000262; ABF37040.1; -; Genomic_DNA.
DR   RefSeq; WP_002986567.1; NC_008024.1.
DR   AlphaFoldDB; Q1J8X1; -.
DR   SMR; Q1J8X1; -.
DR   EnsemblBacteria; ABF37040; ABF37040; MGAS10750_Spy0090.
DR   KEGG; spi:MGAS10750_Spy0090; -.
DR   HOGENOM; CLU_000524_4_1_9; -.
DR   OMA; FMTWEGY; -.
DR   Proteomes; UP000002434; 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_0000300412"
SQ   SEQUENCE   1188 AA;  132855 MW;  1F2B555D1E1D7F1A CRC64;
     MAGHEVRYGK HRTRRSFSRI KEVLDLPNLI EIQTDSFQDF LDSGLKEVFE DVLPISNFTD
     TMELEFVGYE FKEPKYTLEE ARIHDASYSA PIFVTFRLVN KETGEIKTQE VFFGDFPIMT
     EMGTFIINGG ERIIVSQLVR SPGVYFNDKV DKNGKVGYGS TVIPNRGAWL ELETDSKDIA
     YTRIDRTRKI PFTTLVRALG FSGDDEIVDI FGESDLVRNT IEKDIHKNPS DSRTDEALKE
     IYERLRPGEP KTADSSRSLL IARFFDARRY DLAAVGRYKV NKKLNIKTRL LNQIIAENLV
     DAETGEILVE AGTEMTRSVI ESIEEHLDGD LNKFVYTPND YAVVTEPVVL QKFKVVSPID
     PDRVVTIVGN ANPDDKVRAL TPADILAEMS YFLNLAEGLG KVDDIDHLGN RRIRAVGELL
     ANQFRIGLAR MERNVRERMS VQDNDVLTPQ QIINIRPVTA AVKEFFGSSQ LSQFMDQHNP
     LSELSHKRRL SALGPGGLTR DRAGYEVRDV HYTHYGRMCP IETPEGPNIG LINNLSSFGH
     LNKYGFIQTP YRKVDRATGR VTNEIVWLTA DEEDEYTVAQ ANSKLNEDGT FAEEIVMGRH
     QGNNQEFSAS VVDFVDVSPK QVVAVATACI PFLENDDSNR ALMGANMQRQ AVPLIDPKAP
     YVGTGMEYQA AHDSGAAVIA QHNGKVVFSD AEKVEIRRQD GSLDVYHITK FRRSNSGTAY
     NQRTLVKVGD IVEKGDFIAD GPSMENGEMA LGQNPVVAYM TWEGYNFEDA VIMSERLVKE
     DVYTSVHLEE FESETRDTKL GPEEITREIP NVGEEALKDL DEMGIIRIGA EVKEGDILVG
     KVTPKGEKDL SAEERLLHAI FGDKSREVRD TSLRVPHGGD GIVRDVKIFT RANGDELQSG
     VNMLVRVYIA QKRKIKVGDK MAGRHGNKGV VSRIVPVEDM PYLPDGTPVD IMLNPLGVPS
     RMNIGQVMEL HLGMAARNLG IHIATPVFDG ASSEDLWDTV REAGMDSDAK TVLYDGRTGE
     PFDNRVSVGV MYMIKLHHMV DDKLHARSVG PYSLVTQQPL GGKAQFGGQR FGEMEVWALE
     AYGASNVLQE ILTYKSDDVT GRLKAYEAIT KGKPIPKPGV PESFRVLVKE LQSLGLDMRV
     LDEDDNEVEL RDLDEGEDDD IMHVDDLEKA REKQAQETQE VSETTDEK