ID   RPOB_NEOSE              Reviewed;        1357 AA.
AC   Q93MK9;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 79.
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   Neorickettsia sennetsu (Ehrlichia sennetsu).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Neorickettsia.
OX   NCBI_TaxID=951;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC VR-367 / Miyayama;
RX   PubMed=12710612; DOI=10.1099/ijs.0.02411-0;
RA   Taillardat-Bisch A.V., Raoult D., Drancourt M.;
RT   "RNA polymerase beta-subunit-based phylogeny of Ehrlichia spp., Anaplasma
RT   spp., Neorickettsia spp. and Wolbachia pipientis.";
RL   Int. J. Syst. Evol. Microbiol. 53:455-458(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; AF401088; AAK83924.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q93MK9; -.
DR   SMR; Q93MK9; -.
DR   PRIDE; Q93MK9; -.
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..1357
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000047897"
SQ   SEQUENCE   1357 AA;  151551 MW;  D7BDF7393EF75495 CRC64;
     MSEFHRLYFD ELLFDFPDLV KVQKDSYASF VGGGDTGFSI SDIFASVFPV NDGYGRASLE
     FVSCRMGEPK HDEYGCVERG ITYSAPLRAI LRLVVFGDET SGEGSEGVST EPAVKDVREQ
     EIYMGDIPIM SKNGTFIING VERVVVSQMH RAPGVFFDND KARSISGKLN YIARIIPYRG
     SWLDFEFDAK DVLYFRIDKK RKLPVTFLLR ALGLSNKDIF AQFCEVSECR LTKDGKWTVC
     FVPEKFKGVR LQYDLINAET GELVLAKGNR ISIVLARNLY AKGLRYCYMD LEVMKDMYLA
     DDLVSTKGEV LLPHGTKLTK EHVAKLEFLD VDSIKLVELK GNYVFSTVLQ YDCSYEEAML
     SIYRVVRPGE IPSVESAEKL FESLFFSPER YDLLNVGRIR LNAKFNLSHD ESLTVLTKED
     IFCTVKELAL LQREVGDVDD IDHLGNRRVR SVGEFMDNQF RIGLVRMAKV IVENMATADF
     DTVMPCEMIN SKILGAVIRE FFMSSALSQF MDQTNPLSEI THKRRISALG PGGLNRGRAG
     FEVRDVHTTH YGRICATETP EGATIGLINS LAIYAKINKY GFIETPYRYV RDGRVTDEVT
     YLSAIDEIKA NICQASVRVD EEGYIVDDLV YCRRNYENVF IPRSEVQFAD VSAKQIVSVA
     ASLIPFLEND DANRALMGSN MQRQAVPLIM PEAPLVGTGM EGYVARGSGA VIVAKRAGVV
     QYIDARNIVV ASESKDDFWI DSYTLCKFRK SNHNTCIHQR CVVHQGQRVK KGDILADGPA
     IQKGELALGR NLVVAFLSWR GYNFEDSVVI SSNVVRDDLF TSVHLEGFEC VVRDTRLGPE
     EITRDVSGVA EEFLHCLDEF GIACVGANVE AGDVLVGKVT PKSSSPVTPE EKLLRAIFGE
     KAIDVKDSSL YLPPGVSGCV VDVKVLQRRG IEKVGRALLI EKQAIDAEKT RRDHELAVLT
     NYIYSLLKEM LVGKVALSTL APISKGDLIT EEALEKIDRE NWWKISVDGI SSIKLLRQRF
     VDRFDEINKT YEENFEKIRG DDDLAQGVLM VVKVFVAVKH TLQPGDKMSG RHGNKGVISR
     IVPAEDTPYL ADGTPVDIIL NPLGVPSRMN VGQILETHLG WAAYNLGKKI SKLLDEGNYS
     EVKSLVLEIY KNDRKMMARL NEMTDAEIVE YSRSLRGGVP VAASVFEGPK TDEIERLLVL
     AGKDPSGQEV LYDGVTGEKF DRKVTVGCKY MLKLHHLVND KIHARSIGST VDTQQPLGGK
     SHFGGQRFGE MECWALQAYG ATFALQEMLT IKSDDVVGRV NVYDSIVRGD NDFYYGVPES
     FNVMMNELRA LCLNVEFCSD LEKKKDFGDL ALAASGQ