ID   RPOB_BUCAT              Reviewed;        1342 AA.
AC   B8D6V0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 73.
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};
GN   OrderedLocusNames=BUAPTUC7_034;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain Tuc7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=561501;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuc7;
RX   PubMed=19150844; DOI=10.1126/science.1167140;
RA   Moran N.A., McLaughlin H.J., Sorek R.;
RT   "The dynamics and time scale of ongoing genomic erosion in symbiotic
RT   bacteria.";
RL   Science 323:379-382(2009).
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; CP001158; ACL29865.1; -; Genomic_DNA.
DR   RefSeq; WP_012619406.1; NC_011834.1.
DR   AlphaFoldDB; B8D6V0; -.
DR   SMR; B8D6V0; -.
DR   KEGG; bau:BUAPTUC7_034; -.
DR   HOGENOM; CLU_000524_4_3_6; -.
DR   OMA; FMTWEGY; -.
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; -; 2.
DR   Gene3D; 2.40.50.150; -; 1.
DR   Gene3D; 3.90.1110.10; -; 2.
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..1342
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_1000165795"
SQ   SEQUENCE   1342 AA;  151540 MW;  53E439F308A844DC CRC64;
     MVYSYTEKKR IRKDFGKRPK VLDIPYLLSI QLNSFKKFIQ PDLSGQHGLE AAFRSVFPIR
     GYNGNSELQY VSYRLGETIF DVKECQIRGA TYSAPLRVKL RLVIYERDIL EATVKDIKEQ
     EVYMGEIPLM TNNGTFIING TERVVVSQLH RSPGVFFDSD KGKTHSSGKV LYNARIIPYR
     GSWLDFEFDP KDNLFVRIDR RRKLPVSIIL RALNYNTEEI LNIFFEKNIF KIENNKIVLE
     LVPERLRGET ASFNIKKNGI IYVEKGRRIT AKHIQELKNN KIKSITVPVE YILGRIVSKN
     YVDKKTGETI ISSNTELSLE ILEKLKKSGF YSIETLFTND LDHGPYISET LRIDSSNDRM
     SALIEIYRVM RPGEPPTKEA TENLFENLFF SEDRYDLSTV GRMKFNRSLL REETKGSSTL
     NKEDIIDVIK KIIDIRNGKG EVDDIDHLGN RRVRSVGEMA ENQFRIGLVR VERAVKERLS
     IGDLDTLMPQ DMINAKPISA AVKEFFGSSQ LSQFMDQNNP LSEITHKRRI SALGLGGLTR
     ERAGFEVRDV HPTHYGRVCP IETPEGPNIG LINSLSVYAQ TNSYGFLETP YRKVCNGLVS
     EEIHYLSAIE EGNYIIAQAN TNIDKTGFFT DDLVTCRHKG ESSLFNRNQV NYMDVSTQQI
     VSVGASLIPF LEHDDANRAL MGANMQRQAV PTLKTDKPLI GTGMERAVAV DSGVTAVAKR
     SGVVQYVDAS RIVIKVDEKE MYSREAGIDI YNLTKYTRSN QNTCINQQPC VNLGEKIKKG
     DVLADGPSTD LGELALGQNM RVAFMPWNGY NFEDSILVSE RVVQEDRFTT IHIQELSCIS
     RDTKLGAEEI SSDIPNVGEA ALSKLDESGI VYIGAEVTGG DILVGKVTPK GETQLTPEEK
     LLRAIFGEKA SDVKDSSLRV PNGVSGTVID VQIFTRDGVK KDKRALEIED MQLKKIKQDL
     TEEFKIFESS LFTHIKKTFI SLDIETKQLD TLPFEKWFSV DIKQKDKKKE IEKLAKQHHE
     LKEEFNKKIE IKRQKITQGD DLAPGVLKIV KVYLAVKRQI QPGDKMAGRH GNKGVISKIN
     PVEDMPYDEN GIPVDIVLNP LGVPSRMNIG QILETHLGMA AKGIGDKINH MLKTQEKISN
     LRKFIQKAFD LGDNLRQKVN LDTFSNEEIL RLAKNLKNGI PISTPVFDGA QENEIKQMLK
     FAGLPTSGQI ILFDGRTGEK FERPVTVGYM YMLKLNHLVD DKMHARSTGS YSLVTQQPLG
     GKAQFGGQRF GEMEVWALEA YGASYTLQEM LTVKSDDVNG RTKMYKNIVD GNHQMEPGMP
     ESFNVLLKEI RSLGINIELE SE