ID   RPOB_PSINU              Reviewed;        1066 AA.
AC   Q8WI24;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 81.
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   Psilotum nudum (Whisk fern) (Lycopodium nudum).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Polypodiopsida; Ophioglossidae; Psilotales; Psilotaceae; Psilotum.
OX   NCBI_TaxID=3240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kingyoku;
RX   PubMed=15240838; DOI=10.1093/molbev/msh203;
RA   Nishiyama T., Wolf P.G., Kugita M., Sinclair R.B., Sugita M., Sugiura C.,
RA   Wakasugi T., Yamada K., Yoshinaga K., Yamaguchi K., Ueda K., Hasebe M.;
RT   "Chloroplast phylogeny indicates that bryophytes are monophyletic.";
RL   Mol. Biol. Evol. 21:1813-1819(2004).
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; AP004638; BAB84208.1; -; Genomic_DNA.
DR   RefSeq; NP_569621.1; NC_003386.1.
DR   AlphaFoldDB; Q8WI24; -.
DR   SMR; Q8WI24; -.
DR   PRIDE; Q8WI24; -.
DR   GeneID; 2545167; -.
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..1066
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000048043"
SQ   SEQUENCE   1066 AA;  121287 MW;  EC24DB2726A763F8 CRC64;
     MILEENKGMF ALPGFDLIQY EGFKRFINQG LMEELLKFPK IQDADQEVEF LLVGDQYKLR
     EPSIKEKDAV YKCVTYSSEL YVPARLTQKR NRRIREQILF MGSIPLMTSQ GTFIINGVTR
     VLVNQIVRSP GIFYSREPDH KRIPLYTGTI ISNWGGRFKL EIDGRMRIWA RISKERKFSI
     ITLLLALGLT RKDILNGVCY PNILLDLWKR QDKDIKSSED AIIELYKNLY CVSGDVTFSE
     SIRKELQRKL FKQRFELGQI GRRNPNNKLN LNVPENESFL LPQDLLAAID YLIGIKYGIG
     TLDDIDHLKN RRVRSVANFL QGQLRLALTH LENSIRQTMH KAIKRKRSLT PKGLVISTPL
     LTTFKEFFGS HPLSQFLDQT NPLAEMIHKR RLSTLGPGGL TRRTASFQVR DIHPSYYGRI
     CPIETSEGIN AGLITSLALH ARVNDYGYLH SSFYNISDDE EHIVYLSPAE DEYYRIATGN
     QLASNWGTQE KQVTLARYRQ EFLTIAWEQV HFRSLFPLQY FSIGASLIPF LEHNDANRAL
     MGSHMQRQAV PLLKPEKCIV GTGLEGQVAL DSGSVTRSTQ EGQIVYVDGA KITLSLNDNE
     TIDTELITYK RSNNKTCIKE RPIISTGTYL KEGQLLADGT ATVGGELAPG RNILVAYMPW
     EGYNFEDAIL ISERLISEDI FTSLHIERYE IEVRITNQGI EEITKDIPHL DSYVLRHLDS
     NGLVVLGSWV ETGDVLVGKL TPQEDSLRAP EGKLLQAIFG IQVADTKESC LKVPIGGQGR
     VIDARWVYKE NILINNAKTI HIYILQKRKI RVGDKVAGRH GNKGIVSKIL PRQDMPHLQD
     GTPVDMILSP LGVPSRMNVG QIFECLLGLA GDFMQRHYRI TPFDERFERE ASRKLVFSEL
     CEASEKTRNP WLFEPDYPGK SRLIDGRTGD TFEQPVTVGK AYMMKLIHQV DDKIHARSSG
     PYALITQQPL RGRSRRGGQR VGEMEVWALE SFGAAYILQE MLTLKSDHIQ ARYKVLGAIV
     TGKPIPKPNS VPESFRLLVR ELRSLALNLN YFLISEKDLE REMKNV