ID   RPOB_PIPCE              Reviewed;        1070 AA.
AC   Q06GR8;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 65.
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   Piper cenocladum (Ant piper).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Magnoliidae; Piperales; Piperaceae; Piper.
OX   NCBI_TaxID=398741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17020608; DOI=10.1186/1471-2148-6-77;
RA   Cai Z., Penaflor C., Kuehl J.V., Leebens-Mack J., Carlson J.E.,
RA   dePamphilis C.W., Boore J.L., Jansen R.K.;
RT   "Complete plastid genome sequences of Drimys, Liriodendron, and Piper:
RT   implications for the phylogenetic relationships of magnoliids.";
RL   BMC Evol. Biol. 6:77-77(2006).
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; DQ887677; ABI14464.1; -; Genomic_DNA.
DR   RefSeq; YP_784465.1; NC_008457.1.
DR   AlphaFoldDB; Q06GR8; -.
DR   SMR; Q06GR8; -.
DR   PRIDE; Q06GR8; -.
DR   GeneID; 4363713; -.
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; 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..1070
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000276595"
SQ   SEQUENCE   1070 AA;  120871 MW;  E59286A72DA6B698 CRC64;
     MLRNRNEGMS TIPEFSQIQF EGFCRFIDWG LAEELHKFPK IEDTDQEIEF QLFVETYQLA
     EPLIKERDAV YESLTYSSEL YVPAGLIWKP GKDMQEQTVF IGNIPLMSSL GIFIVNGIYR
     IVINQILQSP GIYYRSELDH NGIFIYTGTI ISDWGGRSEL EIDRKARIWA RVSRKQKISI
     LVSSSAMGSN LREILENVRY PEIFLSFLNE RDKKKIGSRE NAILEFYQQF ACVGGDPVFS
     ESLCRELQKK FFQQRCELGR IGRRNMNRRL NLDIPQNNTF LLPRDVLAAA DHLIGMKFGM
     GTLDDMNHLK NKRIRSVADL LQDQFGLALV RLENVVRGTI CGAIRHKLIP TPQNLVTSTP
     LTTTYESFFG LHPLSQVLDR TNPLTQIVHG RKSSYLGPGG LTGRTASFRI RDIHTSHYGR
     ICPIDTSEGI NVGLIGSLAI HARVGPWGSI KTPFYEISER SKRLQLVYLS PSVDEYHMVA
     AGNSLALNRG IQEEQAVPAR YRQEFLTIAW EQIHLRSIFP FQYFSMGASL IPFIEHNDAN
     RALMSSNMQR QAVPLSRSEK CIVGTGLERQ AALDSGVSAI SEREGKVIYT NTDKIILSGN
     GDTITIPLVM YQRSNKNTCM HQKTQVSRGK CIKKGQILAN GAATVGGELA LGKNVLVAYM
     PWEGYNFEDA VLISERLVYE DIYTSFHIRK YEIQTHVTSQ GPERITKEIP HLETHLLRNL
     DRNGIVMLGS WVETGDILVG KLTPQTAKES SYAPEDRLLR AILGIQVSTS KETCLKLPIG
     GRGRVIDVRW IQKKGGSSYN PETIRVYISQ KREMKVGDKV AGRHGNKGII SKILPRQDMP
     YLQDGTPVDM VFNPLGVPSR MNVGQIFECS LGLAGDFLGR HYRVAPFDER YEQEASRKLV
     FSELYEASKQ TANPWVFEPE YPGKSRIFDG RTGDPFDQPV LIGKSYILKL IHQVDDKIHG
     RSSGHYALVT QQPLRGRAKQ GGQRVGEMEV WALEGFGVAH ILQEMLTYKS DHIRSRQEVL
     GTTIVGGTIA NPGDAPESFR LLVRELRSLA LELNHFLLSE KDFQIHRKEA