ID   RPOB_EMIHU              Reviewed;        1093 AA.
AC   Q4G3A7;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01321};
DE   AltName: Full=PEP {ECO:0000255|HAMAP-Rule:MF_01321};
DE   AltName: Full=Plastid-encoded RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE            Short=RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
GN   Name=rpoB {ECO:0000255|HAMAP-Rule:MF_01321};
OS   Emiliania huxleyi (Coccolithophore) (Pontosphaera huxleyi).
OG   Plastid; Chloroplast.
OC   Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Isochrysidales;
OC   Noelaerhabdaceae; Emiliania.
OX   NCBI_TaxID=2903;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP373 / CSIRO-CS-57 / BT6;
RX   PubMed=16303746; DOI=10.1093/dnares/12.2.151;
RA   Sanchez-Puerta M.V., Bachvaroff T.R., Delwiche C.F.;
RT   "The complete plastid genome sequence of the haptophyte Emiliania huxleyi:
RT   a comparison to other plastid genomes.";
RL   DNA Res. 12:151-156(2005).
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: In plastids the minimal PEP RNA polymerase catalytic core is
CC       composed of four subunits: alpha, beta, beta', and beta''. When a
CC       (nuclear-encoded) sigma factor is associated with the core the
CC       holoenzyme is formed, which can initiate transcription.
CC       {ECO:0000255|HAMAP-Rule:MF_01321}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_01321}.
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DR   EMBL; AY741371; AAX13859.1; -; Genomic_DNA.
DR   RefSeq; YP_277360.1; NC_007288.1.
DR   AlphaFoldDB; Q4G3A7; -.
DR   SMR; Q4G3A7; -.
DR   GeneID; 3562436; -.
DR   Proteomes; UP000013827; Unassembled WGS sequence.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; 1.
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   Chloroplast; DNA-directed RNA polymerase; Nucleotidyltransferase; Plastid;
KW   Reference proteome; Transcription; Transferase.
FT   CHAIN           1..1093
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000224127"
SQ   SEQUENCE   1093 AA;  122779 MW;  59B0E5678B1E2A53 CRC64;
     MLDRNKNIYK YLLPNLLDVQ RASYCWFLEK GFVQELRTFS VIRDYLGDLE LNFATKFYTI
     NPPRYTLEEA KRKDATYSVR IFIRAQLNYL EGADPQEKQV FLGDIPLMTD SGTFLVNGIE
     RIIINQIVRS PGIYYKSEAD KQGVRIYTAS LISNRGTWVK FEIDKDDLVY IKIDKAKKFS
     IFVFLKALGL DNQEIFNSIE NINYFRKTSN TDEQLTTEQC LLEVHSHLKP EEPATAKGCQ
     KLLYAKFFDS KKYDLGYVGR HKLNQALMLD IDSDVRILTS LDLIGIINQL IRFRFMPIVS
     DDIDHLGNRR IRSVGELMAN QIRIGLNRLE RVVRERMAIC EHSYLRVNTL VNPKPLAASI
     REFFGSNPLS QFMDQTNPLA ELTHKRRISV LGPGGIARDR AGFVVRDIHP SQYGRICPVE
     TPEGPNAGLI GSLSTYGKIN AYGFIETPFY KVKQGKVLKD LPPIYLDAIA EEQYKLAAGD
     VATDEHGVLK QPDVPVRYQQ NIVTVSKNEV DYIAVSPIQV VSLATSLIPF LEHDDANRAL
     MGSNMQRQSV PLLYADAPLV GTGLESQTAR DSGMAILSSN CGKVVTLSDE QIVVQDKNGN
     QLIYNLTKYK RSNQDTCINQ KPCVSLYEKV RVGQLLADGT STETGELAVG QNILIAYMPW
     EGYNYEDAFV VNERLLYDDL HTSIHIEKFE IESRQTKLGA EEITRDLPNV NEKSLSKLDE
     NGIIHIGSWV EPGDILVGKL TPKGESDYLP EGKLLRAIFG EKSRDVRNTS LKLHHGVNGR
     VLDVKIFSRA NQDDLSPGTN EVIKVYIAQI RKIQIGDKVA GRHGNKGIIS KILPRQDMPY
     LPDGTPVDIL LNPLGVPSRM NVGQIFECLL GLAAEHLNAR FKVIPFDEMN GVEASRGFVN
     NTLMEAAEKQ PWVFSTQHPG KMMLTDGQTG EMFDNPITVG RAYVLKLVHL VDDKIHARST
     GPYSLVTQQP LGGRAQQGGQ RLGEMEVWAL EAFGAAYTLQ ELLTIKSDDM QGRNETLNAI
     VKGYPIPRPG TPESFKVLLR ELQALCLDIA AYKIEDTTLL TEDKEINLMS ELNSSRDDQS
     VANNYLLTRG TTP