ID   RPOB_HELAN              Reviewed;        1060 AA.
AC   Q1KXX2;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
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   Helianthus annuus (Common sunflower).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   Heliantheae alliance; Heliantheae; Helianthus.
OX   NCBI_TaxID=4232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. HA383;
RA   Timme R.E., Kuehl J.V., Boore J.L., Jansen R.K.;
RT   "A comparison of the first two published chloroplast genomes in Asteraceae:
RT   Lactuca and Helianthus.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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; DQ383815; ABD47133.1; -; Genomic_DNA.
DR   RefSeq; YP_588104.1; NC_007977.1.
DR   AlphaFoldDB; Q1KXX2; -.
DR   SMR; Q1KXX2; -.
DR   GeneID; 4055679; -.
DR   KEGG; han:4055679; -.
DR   OrthoDB; 944344at2759; -.
DR   PhylomeDB; Q1KXX2; -.
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; 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; 3.
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   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..1060
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000276589"
SQ   SEQUENCE   1060 AA;  120595 MW;  462B38FE88CAEA0A CRC64;
     MSTIPGFNQI QFEGFCRFID QGLAEELSKF PKIEDTNQEI DFEFFLERYQ LVEPLIKERD
     AVYESLTYSS ELYVSARLIW KNDRRRYIQE QTILIGKIPI MTSLGAFIVN GIYRIVINQI
     LQSPGIYYQS ELNDNGISVY TGTIISDWGG RLELEIDRKA RIWVRVSRQQ KLSILVLLSA
     MGLNIREILE NVCYPELFLS FLNDKKKIGS KENAILEFYQ QFACVEGDPV FSESLSKDLQ
     KKFFQQRCEL GGIGRRNMNR RLNLDIPQNN TFLLPRDILA AADRLIRIKF GMGTLDDMNH
     LQNKRIRSVA DLLQEQFGLA LVRLENMARG NIYAALKHNW TPTPQNLVNS TPLTDTYKVF
     FRLHPLSQVL DRTNPLTQIV HGRKLSYLGP GGLTARTATF PIRDIHPSHY GRICPIDTSE
     GINVGLIGSL AIHARIGRWG SLESPFYQIS ERSKGAQMLY LSPGRDEYYM VAAGNSLALN
     QGIQEEQVVP ARYRQEFLTI AWEQVQLRSI FAFQYFSIGA SLIPFIEHND ANRALMSSNM
     QRQAVPLSQS EKCIVGTGLE GQAALDSGAL AIAEHEGKIF YTDTDKILLS GNGDTLRIPL
     VMYQRSNKNT CMHQKPQVRR GKCIKKGQIL AYGAATVGGE LALGKNVLVA YMPWEGYNFE
     DAVLISERLV YEDIYTSFHI RKYEIQINQG PERVTNEIPH LEVHLLRNLD KNGIVMLGSW
     VETGDILVGK LTPQMVKESS YAPEDRLLRT ILGMRVYTSK ETCLKLPIGG RGRVIDVRWV
     QSSKTDETEK TESIRVYILQ KREIKVGDKV AGRHGNKGII SKILPRQDMP YLQDGRPVDM
     VFNPLGVPSR MNVGQIFESS LGLAGDLLDR HYRIAPFDER YEQEASRKLV FSELYEASKQ
     TANPWIFEPE SPGKSRIFDG RTGDPFEQPV IIGKPYILKL IHQVDDKIHG RSSGRYSRLT
     QQPLKGRAKK GGQRVGEMEV WALEGFGVAY ILQEMLTYKS DHIRARQEVL GTIIFGGRIP
     TPEDAPESFR LFVRELRSLA LELNHFLVSE KTFQLNRKEA