ID   RPOB2_ENTFC             Reviewed;        1208 AA.
AC   Q8GCR4;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=40-4;
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}.
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DR   EMBL; AY167140; AAO00730.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8GCR4; -.
DR   SMR; Q8GCR4; -.
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_0000047900"
SQ   SEQUENCE   1208 AA;  135020 MW;  BE049EDDF6B30AD7 CRC64;
     MKSLAGHVVK YGKHRERKSF 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 DNGLNSVTYY PSEDGVVTDP MTVQVIKVFS
     PKDPEREVNV IGNGYPESAV 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 FVDASEIRVR RDNGALDKYA VTKFRRSNSG
     TSYNQRPIVH LGEKVEKGDT 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 DAKTILYDGR
     TGEPFDGRVS VGVMYMIKLA HMVDDKLHAR SIGPYSLVTQ QPLGGKAQFG GQRFGEMEVW
     ALEAYGAAYT LQEILTYKSD DVVGRVKTYE AIVKGEPIPK PGVPESFRVL VKELQSLGLD
     MRVLDIKDSE IELRDMDDED DDLITVDALT KFAEQQTAKE LEKKAAEQVE DERQDIIQNF
     ETAEDNLD