ID   RPOB_STRCO              Reviewed;        1161 AA.
AC   Q9L0L0;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 116.
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=SCO4654;
GN   ORFNames=SCD82.26;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
RN   [2]
RP   SUBUNIT.
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=23605043; DOI=10.1093/nar/gkt277;
RA   Tabib-Salazar A., Liu B., Doughty P., Lewis R.A., Ghosh S., Parsy M.L.,
RA   Simpson P.J., O'Dwyer K., Matthews S.J., Paget M.S.;
RT   "The actinobacterial transcription factor RbpA binds to the principal sigma
RT   subunit of RNA polymerase.";
RL   Nucleic Acids Res. 41:5679-5691(2013).
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. The RNAP
CC       complex including the principal sigma factor HrdB also interacts with
CC       RNA-binding protein RbpA. {ECO:0000255|HAMAP-Rule:MF_01321,
CC       ECO:0000269|PubMed:23605043}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_01321}.
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DR   EMBL; AL939121; CAB77428.1; -; Genomic_DNA.
DR   RefSeq; NP_628815.1; NC_003888.3.
DR   RefSeq; WP_011029792.1; NZ_VNID01000028.1.
DR   AlphaFoldDB; Q9L0L0; -.
DR   SMR; Q9L0L0; -.
DR   STRING; 100226.SCO4654; -.
DR   PRIDE; Q9L0L0; -.
DR   GeneID; 1100095; -.
DR   KEGG; sco:SCO4654; -.
DR   PATRIC; fig|100226.15.peg.4725; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_1_11; -.
DR   InParanoid; Q9L0L0; -.
DR   OMA; FMTWEGY; -.
DR   PhylomeDB; Q9L0L0; -.
DR   Proteomes; UP000001973; 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   1: Evidence at protein level;
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_0000047972"
SQ   SEQUENCE   1161 AA;  128494 MW;  A9C27B928EE191A8 CRC64;
     MAASRNASTA NTNNAASTAP LRISFAKIKE PLEVPNLLAL QTESFDWLLG NDAWKARVES
     ALESGQDVPT KSGLEEIFEE ISPIEDFSGS MSLTFRDHRF EPPKNSIDEC KDRDFTYAAP
     LFVTAEFTNN ETGEIKSQTV FMGDFPLMTN KGTFVINGTE RVVVSQLVRS PGVYFDSSID
     KTSDKDIFSA KIIPSRGAWL EMEIDKRDMV GVRIDRKRKQ SVTVLLKALG WTTEQILEEF
     GEYESMRATL EKDHTQGQDD ALLDIYRKLR PGEPPTREAA QTLLENLYFN PKRYDLAKVG
     RYKVNKKLGA DEPLDAGVLT TDDVIATIKY LVKLHAGETE TVGESGREIV VETDDIDHFG
     NRRIRNVGEL IQNQVRTGLA RMERVVRERM TTQDVEAITP QTLINIRPVV ASIKEFFGTS
     QLSQFMDQNN PLSGLTHKRR LNALGPGGLS RERAGFEVRD VHPSHYGRMC PIETPEGPNI
     GLIGSLASYG RINPFGFIET PYRKVVEGQV TDDVDYLTAD EEDRFVIAQA NAALGDDMRF
     AEARVLVRRR GGEVDYVPGD DVDYMDVSPR QMVSVATAMI PFLEHDDANR ALMGANMMRQ
     AVPLIKSESP LVGTGMEYRS AADAGDVVKA EKAGVVQEVS ADYITTTNDD GTYITYRLAK
     FSRSNQGTSV NQKVIVAEGD RIIEGQVLAD GPATENGEMA LGKNLLVAFM PWEGHNYEDA
     IILSQRLVQD DVLSSIHIEE HEVDARDTKL GPEEITRDIP NVSEEVLADL DERGIIRIGA
     EVVAGDILVG KVTPKGETEL TPEERLLRAI FGEKAREVRD TSLKVPHGEI GKVIGVRVFD
     REEGDELPPG VNQLVRVYVA QKRKITDGDK LAGRHGNKGV ISKINPIEDM PFLEDGTPVD
     IILNPLAVPS RMNPGQVLEI HLGWLASRGW DVSGLAEEWA QRLQVIGADK VEPGTNVATP
     VFDGAREDEL AGLLQHTIPN RDGERMVLPS GKARLFDGRS GEPFPEPISV GYMYILKLHH
     LVDDKLHARS TGPYSMITQQ PLGGKAQFGG QRFGEMEVWA LEAYGAAYAL QELLTIKSDD
     VTGRVKVYEA IVKGENIPEP GIPESFKVLI KEMQSLCLNV EVLSSDGMSI EMRDTDEDVF
     RAAEELGIDL SRREPSSVEE V