ID   RPOB_CHLAT              Reviewed;        1088 AA.
AC   Q19V98;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 2.
DT   03-AUG-2022, entry version 66.
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   Chlorokybus atmophyticus (Soil alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Chlorokybophyceae; Chlorokybales;
OC   Chlorokybaceae; Chlorokybus.
OX   NCBI_TaxID=3144;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAG 48.80;
RX   PubMed=17222354; DOI=10.1186/1741-7007-5-2;
RA   Lemieux C., Otis C., Turmel M.;
RT   "A clade uniting the green algae Mesostigma viride and Chlorokybus
RT   atmophyticus represents the deepest branch of the Streptophyta in
RT   chloroplast genome-based phylogenies.";
RL   BMC Biol. 5:2-2(2007).
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}.
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; DQ422812; ABD62240.2; -; Genomic_DNA.
DR   RefSeq; YP_001019104.1; NC_008822.1.
DR   AlphaFoldDB; Q19V98; -.
DR   SMR; Q19V98; -.
DR   GeneID; 4783298; -.
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; -; 2.
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; 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; 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   Transcription; Transferase.
FT   CHAIN           1..1088
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000300437"
SQ   SEQUENCE   1088 AA;  122307 MW;  45133C4C3127ED08 CRC64;
     MIQQYNPFKK DAFDILLPDL VGIQLESFST FLKKGLIEQL RDFSVITDPT NNLELRLLVE
     QYKLKRPRYN EKKCIRRACT YASQLYIPAQ LINKKTGKVQ EQDVFLGEMP IMTSRGNFII
     NGSARVIVNQ IVRSPGIYYK REIDPKEGIK TYSASIICNR GAWLRLETDK NGFVWARIGK
     VRKVSGFILL RAMGLTKSKI LNSLRHPEFF QKTIEEGDPY SENDALIDLH SQLYPERPST
     LFAARELLKS KFFDPKYYDL GKVGRYKINK KLQLSIPEDI RVLTPQDILT AIDYLINLEF
     NIGTLDDIDH LKNRRVRSVG ELIENQVRVG LSRLERMTYK RMAESHPDAL TPASLINPKP
     LVGVLREFFG SSQLSQFMDQ TNPLSEMTHK RRISCLGPGG LSKERAGLAV RDIHPSHYGR
     ICPIETPEGP NAGLIGSLAT HARVNPYGFL ESPFYPTKNR KVFKKTLPIY LSPDQEDELR
     VSPGDLLLSS SGKLEGKTVP IRYKQDFSTS RSDQVDYVGI SPIQAISIAT SLIPFLEHDD
     ANRALMGSNM QRQAVPVIRP ERPVVGTGLE AQAALDSGTV IVARHDGIVS LVDSNKIILR
     SSCGSNQTKV DSVGLNFDYQ IDRYHLQKYN RSNQDTCINQ RPVVHQGEFI KKGDILADGA
     ATVGGQLTLG KNVLVAYMPW EGYNFEDAIL ISQRLVYDDI YTSIHIEKYE IEARKTKLGP
     EKITREVPNL GDYVLRNLDE NGIVIPGAWV EAGDILVGKV TPKEDLDQHP EGKLLRAIFS
     EKARDVRDTS LRVPNGVRGR VVDVRRLKGS ELPSGVNMVV HIFISQKRKI QVGDKMAGRH
     GNKGIISRIL PRQDMPYLQD GTPVDMVLNP LGVPSRMNVG QVYECLLGLA GHFLGEEYKL
     IPFDEMYGKE ASRGFVYSKL YEARKKTGYP WLFDIANPGK SQLFDGRTGE PFDQPVTVGR
     AYMLKLVHLV DDKIHARSTG PYSLVTQQPL GGKAKHGGQR LGEMEVWALE GFGAAYTLQE
     LLTVKSDDMK GRNEAQHAII KGRPIPKPGT PESFKVLIRE LQSLCLDIGI YKIDKTKKGQ
     EIDLMMSM