ID   RPOB_STRAW              Reviewed;        1161 AA.
AC   Q82DQ5;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   03-AUG-2022, entry version 108.
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=SAV_4914;
OS   Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS   14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=227882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC   8165 / MA-4680;
RX   PubMed=11572948; DOI=10.1073/pnas.211433198;
RA   Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA   Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M.;
RT   "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT   deducing the ability of producing secondary metabolites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC   8165 / MA-4680;
RX   PubMed=12692562; DOI=10.1038/nbt820;
RA   Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M., Omura S.;
RT   "Complete genome sequence and comparative analysis of the industrial
RT   microorganism Streptomyces avermitilis.";
RL   Nat. Biotechnol. 21:526-531(2003).
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; BA000030; BAC72626.2; -; Genomic_DNA.
DR   RefSeq; WP_037647936.1; NZ_JZJK01000077.1.
DR   AlphaFoldDB; Q82DQ5; -.
DR   SMR; Q82DQ5; -.
DR   STRING; 227882.SAV_4914; -.
DR   PRIDE; Q82DQ5; -.
DR   EnsemblBacteria; BAC72626; BAC72626; SAVERM_4914.
DR   KEGG; sma:SAVERM_4914; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_1_11; -.
DR   OMA; FMTWEGY; -.
DR   OrthoDB; 9601at2; -.
DR   Proteomes; UP000000428; 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; Reference proteome;
KW   Transcription; Transferase.
FT   CHAIN           1..1161
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000047971"
SQ   SEQUENCE   1161 AA;  128297 MW;  3352070E6955EF22 CRC64;
     MAASRTASTA NTNNGASTAP LRISFAKIKE PLEVPNLLAL QTESFDWLLG NDAWKARVEA
     ALDSGQDVPT KSGLEEIFEE ISPIEDFSGS MSLTFRDHRF EPPKNSIDEC KDRDFTYAAP
     LFVTAEFTNN ETGEIKSQTV FMGDFPLMTN KGTFVINGTE RVVVSQLVRS PGVYFDSSID
     KTSDKDIFSA KVIPSRGAWL EMEIDKRDMV GVRIDRKRKQ SVTVLLKALG WTTEQILEEF
     GEYESMRATL EKDHTQGQDD ALLDIYRKLR PGEPPTREAA QTLLENLYFN PKRYDLAKVG
     RYKVNKKLGG EAPLDAGILT VEDIISSIKY LVKLHAGETE TVGDNGTSIV VETDDIDHFG
     NRRLRNVGEL IQNQVRTGLA RMERVVRERM TTQDVEAITP QTLINIRPVV ASIKEFFGTS
     QLSQFMDQNN PLSGLTHKRR LSALGPGGLS RERAGFEVRD VHPSHYGRMC PIETPEGPNI
     GLIGSLASYG RVNAFGFVET PYRRVTDGVV TDEVDYLTAD EEDRFVIAQA NAPLGDDFRF
     EETRVLVRRR GGEVDYVPGD DVDYMDVSPR QMVSVATAMI PFLEHDDANR ALMGANMMRQ
     AVPLIKSEAP LVGTGMEYRC AVDAGDVLKS EKDGVVQEVS ADYVTTANDD GTYTTYRLHK
     FSRSNQGTSV NQKVVVDEGA RVIAGQVLAD GPATENGEMA LGKNLLVAFM PWEGHNYEDA
     IILSQRLVQD DVLSSIHIEE HEVDARDTKL GPEEITRDIP NVSEEVLADL DERGIIRIGA
     EVVAGDILVG KVTPKGETEL TPEERLLRAI FGEKAREVRD TSLKVPHGEI GKVIGVRVFD
     REEGDELPPG VNQLVRVYVA QKRKITDGDK LAGRHGNKGV ISKILPIEDM PFLEDGTPVD
     IILNPLGVPS RMNPGQVLEI HLGWLASRGW DVSGLADDWA QRLQAIEADQ VAPGTNVATP
     VFDGAREDEL AGLLQHTIPN RDGERMVLPT GKAPLFDGRS GEPFPEPISV GYMYILKLHH
     LVDDKLHARS TGPYSMITQQ PLGGKAQFGG QRFGEMEVWA LEAYGAAYAL QELLTIKSDD
     VTGRVKVYEA IVKGENIPEP GIPESFKVLI KEMQSLCLNV EVLSSDGMSI EMRDTDEDVF
     RAAEELGIDL SRREPSSVEE V