ID   RPOB1_ENTFC             Reviewed;        1208 AA.
AC   Q8GCR6;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 77.
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};
OS   Enterococcus faecium (Streptococcus faecium).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1352;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=343-3;
RA   Enne V.I., Bennett P.M.;
RT   "Rifampin resistance and its fitness cost in Enterococcus faecium.";
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY167138; AAO00728.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8GCR6; -.
DR   SMR; Q8GCR6; -.
DR   STRING; 1352.AL014_12570; -.
DR   eggNOG; COG0085; Bacteria.
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..1208
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000047899"
FT   REGION          1182..1208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1182..1200
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1208 AA;  135022 MW;  A2DB22DA213ED397 CRC64;
     MKSLAGHVVK YGKHRERRSF ARISEVLELP NLIEIQTDSY QWFLDEGLRE MFEDILPIDD
     FNGNLSLEFV DYELKEPKYT VAEARAHDAN YSAPLHVTLR LTNRETGEIK AQEVFFGDFP
     LMTEQGTFII NGAERVIVSQ LVRSPGVYFH GKVDKNGKEG FGSTVIPNRG AWLEMETDAK
     DISYVRIDRT RKIPLTVLVR ALGFGSDDTI FEIFGDSETL RNTVEKDLHK NASDSRTEEG
     LKDVYERLRP GEPKTADSSR NLLNARFFDP KRYDLANVGR YKVNKKLDLK TRLLNLTLAE
     TLVDPETGEI IVEKGTVLTH QVMETLAPFI DNGLNSGTYY PSEDGVVTDP MTVQVIKVFS
     PRDPEREVNV IGNGYPEAAV KTVRPADIIA SMSYFLNLME GIGNVDDIDH LGNRRIRSVG
     ELLQNQFRIG LARMERVVRE RMSIQDTETL TPQQLINIRP VVASIKEFFG SSQLSQFMDQ
     TNPLGELTHK RRLSALGPGG LTRDRAGYEV RDVHYSHYGR MCPIETPEGP NIGLINSLSS
     YAKVNKFGFI ETPYRRVDRE TGRVTDQIDY LTADIEDHYI VAQANSPLNE DGTFAQDVVM
     ARAQSENLEV SIDKVDYMDV SPKQVVAVAT ACIPFLENDD SNRALMGANM QRQAVPLINP
     QAPWVGTGME YKSAHDSGAA LLCKHDGVVE YVDASEIRVR RDNGALDKYD VTKFRRSNSG
     TSYNQRPIVH LGEKVEKGVT LADGPSMEQG EMALGQNVLV GFMTWEGYNY EDAIIMSRRL
     VKDDVYTSIH IEEYESEARD TKLGPEEITR EIPNVGEDAL KDLDEMGIIR IGAEVQDGDL
     LVGKVTPKGV TELSAEERLL HAIFGEKARE VRDTSLRVPH GGGGIVHDVK IFTREAGDEL
     SPGVNMLVRV YIVQKRKIHE GDKMAGRHGN KGVVSRIMPE EDMPFLPDGT PIDIMLNPLG
     VPSRMNIGQV LELHLGMAAR QLGIHVATPV FDGASDEDVW ETVREAGMAS DAKTVLYDGR
     TGEPFDGRVS VGVMYMIKLA HMVDDKLHAR SIGPYSLVTQ QPLGGKAQFG GQRFGEMEVW
     ALEAYGAAYT LQEILTYKSD DVVGRVKTYE AIVKGEPIPK PGVPESFRVL VKELQSLGLD
     MRVLDIEETE IELRDMDDED DDLITVDALT KFAEQQTAKE LEKKAAEQVE DEKDDVIQNF
     ETAEDNLD