RPOB_POLNS
ID RPOB_POLNS Reviewed; 1366 AA.
AC B1XSP3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=Pnec_0042;
OS Polynucleobacter necessarius subsp. necessarius (strain STIR1).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=452638;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STIR1;
RX PubMed=24167248; DOI=10.1073/pnas.1316687110;
RA Boscaro V., Felletti M., Vannini C., Ackerman M.S., Chain P.S.,
RA Malfatti S., Vergez L.M., Shin M., Doak T.G., Lynch M., Petroni G.;
RT "Polynucleobacter necessarius, a model for genome reduction in both free-
RT living and symbiotic bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:18590-18595(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.
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; CP001010; ACB43370.1; -; Genomic_DNA.
DR RefSeq; WP_012357139.1; NC_010531.1.
DR AlphaFoldDB; B1XSP3; -.
DR SMR; B1XSP3; -.
DR STRING; 452638.Pnec_0042; -.
DR PRIDE; B1XSP3; -.
DR EnsemblBacteria; ACB43370; ACB43370; Pnec_0042.
DR KEGG; pne:Pnec_0042; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_4; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
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..1366
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000141718"
SQ SEQUENCE 1366 AA; 152450 MW; 822541CA99091B15 CRC64;
MNYSFTERKR VRKSFAKRVN NHQVPYLIAT QLESYAKFLQ ADKPAMSRLT EGLQAAFTSA
FPIVSNNGYA RMEYVSYQLS QPPFDVKECQ QRGYTYHSAL RAKVRLIIYD REAPTKVKEV
KESEVYMGEI PLMTENGSFV INGTERVIVS QLHRSPGVFF EHDKGKTHSS GKLLFSARII
PYRGSWLDFE FDPKDILYFR IDRRRKMPVT ILLKAIGLNN EQILANFFNF DHFSLTANGG
SMEFVPERLR GQLASFDVLD ENGVVVIQKD KRINTKHIRE LEAAKTKTIA VPDDYLIGRV
VARNIVDPDS GEILAYANDE ITEELLATLR DAGIKQLETI YTNDLDSGAY ISQTLRTDET
ADQMAARIAI YRMLRPGEPP IEDAVEVLFQ RLFYSEDTYD LSRVGRMKVN SRLNRPEMEG
PMVLSSEDIL DTIKSLVDLR NGKGEVDDID HLGNRRVRCV GELAENQFRA GLSRVERAVK
ERLGQAETEN LMPHDLTNSK PISSAIREFF GSSQLSQFMD QTNPLSEITH KRRISALGPG
GLMRERAGFE VRDVHPTHYG RVCPIETPEG PNIGLINSLA LFARLNEHGF LETPYRKVSN
SKVSDEVVYL SAIEEAKYVI AQANATIDKS GKLADELVSA RQAGETMMVS PERIDFIDVA
PSQIVSAAAS LVPFLEHDDA NRALMGANMQ RQAVPCLRPD KPLVGTGLER IVAVDSGTVV
LAARGGIVDY VDANRVVIRV NDDETTAGEV GVDIYNLIKY TRSNQNTNIN QRPIVKVGDR
VARGDVVADG ASTDLGELAL GQNMTVAFMP WNGYNFEDSI LISEKVVADD RYTSIHIEEL
SVVARDTKLG SEEITRDISN LAESQLSRLD ESGIVYIGAE VEAGDVLVGK VTPKGETTLT
PEEKLLRAIF GEKASDVKDT SLRVPSGMIG TIIDVQVFTR EGIERDARAQ SIIQEELQRY
RLGLNDQLRI VEGDAFMRLE KLLIGKVANG GPKKLAKGTK IDKEYLADLD KYHRFDVRPA
DDEVASQVEA IKSSIEAKRK QFDEAFEEKR TKLTQGDDLQ PGVTKMVKVY LAVKRRLQPG
DKMAGRHGNK GVVSKIAPAE DMPFMADGRP VDIVLNPLGV PSRMNVGQIL ETHLGWAAQG
IGKRVDEMVR QQAKQAELRE FLKQLYNETG RIEDIDNFTD EQITVLAENL RQGLPFATPV
FDGATEAEIG RMLELAYPEE VATSLKMTPS RQQMILCDGR TGDQFERPAT VGVMHVLKLH
HLVDDKMHAR STGPYSLVTQ QPLGGKAQFG GQRFGEMEVW ALEAYGASYV LQEMLTVKSD
DVAGRTKVYE NIVKGEHTID AGMPESFNVL VKEIRSLGIE IDMERN
