ID   RPOB_STRGC              Reviewed;        1188 AA.
AC   A8AZI3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=SGO_1927;
OS   Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS   DL1 / V288).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=467705;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX   PubMed=17720781; DOI=10.1128/jb.01023-07;
RA   Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT   "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT   to competence signaling peptide.";
RL   J. Bacteriol. 189:7799-7807(2007).
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; CP000725; ABV10072.1; -; Genomic_DNA.
DR   RefSeq; WP_012130944.1; NC_009785.1.
DR   AlphaFoldDB; A8AZI3; -.
DR   SMR; A8AZI3; -.
DR   STRING; 467705.SGO_1927; -.
DR   EnsemblBacteria; ABV10072; ABV10072; SGO_1927.
DR   KEGG; sgo:SGO_1927; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_1_9; -.
DR   OMA; FMTWEGY; -.
DR   Proteomes; UP000001131; 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; 2.40.270.10; -; 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; 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; Reference proteome;
KW   Transcription; Transferase.
FT   CHAIN           1..1188
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_1000086387"
SQ   SEQUENCE   1188 AA;  132685 MW;  7AC3C03BA9DCC8D7 CRC64;
     MAGHDVQYGK HRTRRSFSRI KEVLDLPNLI EIQTDSFKDF LDHGLKEVFE DVLPISNFTD
     TMELEFVGYE IREPKYTLEE ARIHDASYSA PIFVTFRLIN KETGEIKTQE VFFGDFPIMT
     EMGTFIINGG ERIIVSQLVR SPGVYFNDKV DKNGKIGYGS TVIPNRGAWL ELETDSKDIA
     YTRIDRTRKI PFTTLVRALG FSGDDEIFDI FGDSDLVRNT IEKDIHKNPM DSRTDEALKE
     IYERLRPGEP KTAESSRSLL VARFFDPHRY DLAAVGRYKI NKKLNIKTRL LNQTIAEPLV
     DAETGEILVE AGTLMTRSVI DSIAEQLDNG LNKITYIPND SAVLTEPVEL QKFKVVAPTD
     PDRVVTIIGN ANPSDKVRTV TPADILAEMS YFLNLAEGIG RVDDIDHLGN RRIRAVGELL
     ANQVRLGLSR MERNVRERMS VQDNEVLTPQ QIINIRPVTA AIKEFFGSSQ LSQFMDQHNP
     LSELSHKRRL SALGPGGLTR DRAGYEVRDV HYTHYGRMCP IETPEGPNIG LINNLSSYGH
     LNKYGFIQTP YRKVDREAGV VTNEIVWLTA DEEDEFIVAQ ANSKLNEEGG FAEPIVMGRH
     QGNNQEFPSD QVDYMDVSPK QVVAVATACI PFLENDDSNR ALMGANMQRQ AVPLIDPKAP
     YVGTGMEYQA AHDSGAAVIA QHDGKVTYAD ADKVEVRRED GSLDVYHIQK FRRSNSGTAY
     NQRTLVKVGD VVEKGDFIAD GPSMENGEMA LGQNPIVAYM TWEGYNFEDA VIMSERLVKD
     DVYTSVHLEE YESETRDTKL GPEEITREIP NVGEDALRNL DEMGIIRIGA EVKEGDILVG
     KVTPKGEKDL SAEERLLHAI FGDKSREVRD TSLRVPHGAD GVVRDVKIFT RANGDELQSG
     VNMLVRVYIA QKRKIKVGDK MAGRHGNKGV VSRIVPVEDM PYLPDGTPVD IMLNPLGVPS
     RMNIGQVMEL HLGMAARNLG IHIATPVFDG ASSDDLWDTV REAGMDSDAK TVLYDGRTGE
     PFDNRVSVGV MYMIKLHHMV DDKLHARSVG PYSMVTQQPL GGKAQFGGQR FGEMEVWALE
     AYGASNVLQE ILTYKSDDVN GRLKAYEAIT KGKPIPKPGV PESFRVLVKE LQSLGLDMRV
     LDEDDNEVEL RDLDEGEDDD VIHVDDLEKA REKAAQEAKA AFEAEGKE