ID   RPOB_CORGB              Reviewed;        1165 AA.
AC   A4QBG2;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-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=cgR_0591;
OS   Corynebacterium glutamicum (strain R).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=340322;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R;
RX   PubMed=17379713; DOI=10.1099/mic.0.2006/003657-0;
RA   Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M.,
RA   Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.;
RT   "Comparative analysis of the Corynebacterium glutamicum group and complete
RT   genome sequence of strain R.";
RL   Microbiology 153:1042-1058(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; AP009044; BAF53559.1; -; Genomic_DNA.
DR   RefSeq; WP_011896752.1; NC_009342.1.
DR   AlphaFoldDB; A4QBG2; -.
DR   SMR; A4QBG2; -.
DR   PRIDE; A4QBG2; -.
DR   EnsemblBacteria; BAF53559; BAF53559; cgR_0591.
DR   GeneID; 58309600; -.
DR   KEGG; cgt:cgR_0591; -.
DR   HOGENOM; CLU_000524_4_3_11; -.
DR   OMA; FMTWEGY; -.
DR   PhylomeDB; A4QBG2; -.
DR   Proteomes; UP000006698; 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; 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   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..1165
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000300304"
SQ   SEQUENCE   1165 AA;  128801 MW;  409A3EB48C70F09F CRC64;
     MLEGPILAVS RQTKSVVDIP GAPQRYSFAK VSAPIEVPGL LDLQLDSYSW LIGTPEWRAR
     QKEEFGEGAR VTSGLENILE ELSPIQDYSG NMSLSLSEPR FEDVKNTIDE AKEKDINYAA
     PLYVTAEFVN NTTGEIKSQT VFIGDFPMMT DKGTFIINGT ERVVVSQLVR SPGVYFDQTI
     DKSTERPLHA VKVIPSRGAW LEFDVDKRDS VGVRIDRKRR QPVTVLLKAL GWTTEQITER
     FGFSEIMMST LESDGVANTD EALLEIYRKQ RPGEQPTRDL AQSLLDNSFF RAKRYDLARV
     GRYKINRKLG LGGDHDGLMT LTEEDIATTI EYLVRLHAGE RVMTSPNGEE IPVETDDIDH
     FGNRRLRTVG ELIQNQVRVG LSRMERVVRE RMTTQDAESI TPTSLINVRP VSAAIREFFG
     TSQLSQFMDQ NNSLSGLTHK RRLSALGPGG LSRERAGIEV RDVHPSHYGR MCPIETPEGP
     NIGLIGSLAS YARVNPFGFI ETPYRRIIDG KLTDQIDYLT ADEEDRFVVA QANTHYDEEG
     NITDETVTVR LKDGDIAMVG RNAVDYMDVS PRQMVSVGTA MIPFLEHDDA NRALMGANMQ
     KQAVPLIRAE APFVGTGMEQ RAAYDAGDLV ITPVAGVVEN VSADFITIMA DDGKRETYLL
     RKFQRTNQGT SYNQKPLVNL GERVEAGQVI ADGPGTFNGE MSLGRNLLVA FMPWEGHNYE
     DAIILNQNIV EQDILTSIHI EEHEIDARDT KLGAEEITRD IPNVSEEVLK DLDDRGIVRI
     GADVRDGDIL VGKVTPKGET ELTPEERLLR AIFGEKAREV RDTSMKVPHG ETGKVIGVRH
     FSREDDDDLA PGVNEMIRIY VAQKRKIQDG DKLAGRHGNK GVVGKILPQE DMPFLPDGTP
     VDIILNTHGV PRRMNIGQVL ETHLGWLASA GWSVDPEDPE NAELVKTLPA DLLEVPAGSL
     TATPVFDGAS NEELSGLLAN SRPNRDGDVM VNADGKATLI DGRSGEPYPY PVSIGYMYML
     KLHHLVDEKI HARSTGPYSM ITQQPLGGKA QFGGQRFGEM EVWAMQAYGA AYTLQELLTI
     KSDDVVGRVK VYEAIVKGEN IPDPGIPESF KVLLKELQSL CLNVEVLSAD GTPMELAGDD
     DDFDQAGASL GINLSRDERS DADTA