ID   RPOB_CYACA              Reviewed;        1081 AA.
AC   Q9TM35;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 94.
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   Cyanidium caldarium (Red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; Cyanidium.
OX   NCBI_TaxID=2771;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RK-1;
RX   PubMed=11040290; DOI=10.1007/s002390010101;
RA   Gloeckner G., Rosenthal A., Valentin K.-U.;
RT   "The structure and gene repertoire of an ancient red algal plastid
RT   genome.";
RL   J. Mol. Evol. 51:382-390(2000).
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; AF022186; AAF13014.1; -; Genomic_DNA.
DR   RefSeq; NP_045031.1; NC_001840.1.
DR   AlphaFoldDB; Q9TM35; -.
DR   SMR; Q9TM35; -.
DR   GeneID; 800292; -.
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; IPR019462; DNA-dir_RNA_pol_bsu_external_1.
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; PF10385; RNA_pol_Rpb2_45; 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..1081
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000048019"
SQ   SEQUENCE   1081 AA;  121882 MW;  D55A402F8E6A7FB0 CRC64;
     MKKNQFANKL IVIDLLSVQR ESFYSFLTEG LAKELNNFSP IIDYTGKLEL HLVTNQLVIK
     KPKFSFEEAK RRDCSYTISI NIVTQLFNKN SGDVKEQEIL LGEIPLMTQK GTFVINGAER
     VIVNQIVRSP GIYFNSEMDK NNLKTFNFLI IPNRGAWLKC EIDKNDLIWI RIDKNKKINL
     SIFFKALGID HDDLRIKNAF RQPEFIYKNL NKDENYTQQE ALEELHKKLF PGEPATSEAS
     TKILYFKFFN PKKYDLGIVG RKKINKKLDL NSPENIRILT IQDILSGINY LINLKFGFGN
     IDDIDHLANR RLKSVGELLQ SQISIGLIRL ERLIKERMTI CEQSSLVPSA LINPKPIFAA
     IKEFFNSSQL SQFMDQVNPL AELTHKRRVS SLGPGGLSKE RAGFAVRDIH PSHYGRICPI
     ETPEGPNAGL IGSLAIYARI NPDGFIEAPF YKVNQGQVLK NKGIIYLDAE QEDEFKIAPG
     DIRINETNFI KEINVPVRYR QEFTQCPAEE IDFIAVSPIQ VISAATSLIP FLEHNDANRA
     LMGSNMQRQA VPLIFPERPL VGTGLEAQIA KDSGIMAISR SNGIVKFTSA EKIIVTDSSN
     NQITYNLQKY QKSNQETCIN HRPIVWPGER IKKGQILADG SATDTGELAL GRDVLVAYMP
     WEGYNYEDAF LISDRLVYED LYTSIHIEKY EIEARQTKLG PEEITRNIPN VGENSLKQLD
     ENGIVVVSSF VESGSILVGK VTPKGESDQP PESKLLQAIF GEKNKDVKDT SLRLPNGTRG
     RVVDVRIFSR EKGDELAVGI NYIVRIYVAQ KRKIQIGDKM AGRHGNKGII SKILPRQDMP
     YLPNGTPVDI ILNPLGVPSR MNVGQIFECI LGISAFNLKK RFRILPFDEM YESDSSRILI
     NQKLKEAQTL TNLDYLFNEN HLGKVALFDG RSGEKFDNPV LVGKIYMMKL VHLVDDKIHS
     RSTGPYSLVT QQPLGGKAQQ GGQRLGEMEV WAFEAFGAAY ALQELLTIKS DDIQGRNEAL
     TAIVRGKTIP KPGTPESLKV LMREIQSLGL DIAAYRLPNL HHGEIKSIEI DLTHNKIVQK
     R