ID   RPOB_MAIZE              Reviewed;        1075 AA.
AC   P16023;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 138.
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   Zea mays (Maize).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2381419; DOI=10.1007/bf00259403;
RA   Igloi G.L., Meinke A., Doery I., Koessel H.;
RT   "Nucleotide sequence of the maize chloroplast rpo B/C1/C2 operon:
RT   comparison between the derived protein primary structures from various
RT   organisms with respect to functional domains.";
RL   Mol. Gen. Genet. 221:379-394(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2308853; DOI=10.1093/nar/18.3.663;
RA   Igloi G.L., Meinke A., Doery I., Koessel H.;
RT   "Nucleotide and derived amino acid sequence of rps2 from maize
RT   chloroplasts.";
RL   Nucleic Acids Res. 18:663-663(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. B73;
RX   PubMed=7666415; DOI=10.1006/jmbi.1995.0460;
RA   Maier R.M., Neckermann K., Igloi G.L., Koessel H.;
RT   "Complete sequence of the maize chloroplast genome: gene content, hotspots
RT   of divergence and fine tuning of genetic information by transcript
RT   editing.";
RL   J. Mol. Biol. 251:614-628(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-88.
RX   PubMed=2304916; DOI=10.1073/pnas.87.4.1531;
RA   Hu J., Bogorad L.;
RT   "Maize chloroplast RNA polymerase: the 180-, 120-, and 38-kilodalton
RT   polypeptides are encoded in chloroplast genes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:1531-1535(1990).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
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; X17318; CAA35195.1; -; Genomic_DNA.
DR   EMBL; X86563; CAA60276.1; -; Genomic_DNA.
DR   EMBL; M31206; AAA84490.1; -; Genomic_DNA.
DR   PIR; S12800; RNZMB.
DR   RefSeq; NP_043015.1; NC_001666.2.
DR   AlphaFoldDB; P16023; -.
DR   SMR; P16023; -.
DR   STRING; 4577.GRMZM5G877454_P01; -.
DR   PaxDb; P16023; -.
DR   PRIDE; P16023; -.
DR   GeneID; 845225; -.
DR   KEGG; zma:845225; -.
DR   MaizeGDB; 69580; -.
DR   eggNOG; KOG0214; Eukaryota.
DR   HOGENOM; CLU_000524_4_3_1; -.
DR   OMA; FMTWEGY; -.
DR   OrthoDB; 944344at2759; -.
DR   Proteomes; UP000007305; Chloroplast.
DR   ExpressionAtlas; P16023; baseline and differential.
DR   Genevisible; P16023; ZM.
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   Reference proteome; Transcription; Transferase.
FT   CHAIN           1..1075
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000048029"
FT   CONFLICT        16
FT                   /note="S -> M (in Ref. 4; AAA84490)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1075 AA;  121571 MW;  67043F73FBA6CD75 CRC64;
     MLRNGNEGMS TIPGFSQIQF EGFCRFINQG LAEELEKFPT IKDPDHEIAF QLFAKGYQLL
     EPSIKERNAV YESLTYSSEL YVSARLIFGF DVQKETISIG NIPIMNSLGT FIINGIYRIV
     INQILLSPGI YYRSELDHKG ISIYTGTIIS DWGGRSELAI DKKERIWARV SRKQKISILV
     LSSAMGSNLR EILDNVSYPE IFLSFPNAKE KKRIESKEKA ILEFYQQFAC VGGDLVFSES
     LCEELQKKFF QQKCELGRVG RRNMNRRLNL DIPQNNTFLL PRDVLAATDH LIGMKFGTGI
     LDDDDMNHLK NKRIRSVADL LQDQFGLALG RLQHAVQKTI RRVFIRQSKP TPQTLVTPTS
     TSILLITTYE TFFGTYPLAQ VFDQTNPLTQ TVHGRKVSCL GPGGLTGRTA SFRSRDIHPS
     HYGRICPIDT SEGINVGLTG SLAIHARIDH WWGSIESPFY EISEKAKEKK ERQVVYLSPN
     RDEYYMIAAG NSLSLNQGIQ EEQVVPARYR QEFLTIAWEQ IHVRSIFPFQ YFSIGGSLIP
     FIEHNDANRA LMSSNMQRQA VPLSRSEKCI VGTGLERQTA LDSRVSVIAQ REGKIISSDS
     HKILLSSSGK TISIPLVAHR RSNKNTCMHQ KPRVPRGKSI KKGQILAEGA ATVGGELALG
     KNVLVAYMPW EGYNFEDAVL ISERLVYEDI YTSFHIRKYE IQTDTTSQGS AEKITKQIPH
     LEEHLLRNLD RNGVVRLGSW VETGDILVGK LTPQIASESS YIAEAGLLRA IFGLEVSTSK
     ETSLKLPIGG RGRVIDVKWI QRDPFDIMVR VYILQKREIK VGDKVAGRHG NKGIISKILP
     RQDMPYLQDG APVDMVFNPL GVPSRMNVGQ IFESSLGLAG DLLKKHYRIA PFDERYEQEA
     SRKLVFSELY EASKQTKNPW VFEPEYPGKS RIFDGRTGDP FEQPVLIGKS YILKLIHQVD
     EKIHGRSTGP YSLVTQQPVR GRAKQGGQRI GEMEVWALEG FGVAHILQEI LTYKSDHLIA
     RQEILNATIW GKRMPNHEDP PESFRVLVRE LRSLALELNH FLVSEKNFQV NREDV