ID   RPOB_PORPU              Reviewed;        1143 AA.
AC   P51252;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 105.
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   Porphyra purpurea (Red seaweed) (Ulva purpurea).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Porphyra.
OX   NCBI_TaxID=2787;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Avonport;
RA   Reith M.E., Munholland J.;
RT   "Complete nucleotide sequence of the Porphyra purpurea chloroplast
RT   genome.";
RL   Plant Mol. Biol. Rep. 13:333-335(1995).
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; U38804; AAC08138.1; -; Genomic_DNA.
DR   PIR; S73173; S73173.
DR   RefSeq; NP_053862.1; NC_000925.1.
DR   AlphaFoldDB; P51252; -.
DR   SMR; P51252; -.
DR   GeneID; 809881; -.
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..1143
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000048042"
SQ   SEQUENCE   1143 AA;  129058 MW;  407E43E7061F3FC7 CRC64;
     MVQRISLKNK LLPDLVEIQR DSFKWFLLEG LTEVLEFFPN ISDPTSRLEL QLFGKEYKIK
     FPRYSVRQAK SRDRTYSAQI YVPAKLTRKD IDLPSKDQNK TIKSLDLSSN HLQFSAEKQI
     KNKKYKKRLV FIGDLPIMTN RGTFIVSGTE RVIINQIIRS PGIYYKQDID KNGKQIYSAS
     LISNRGSWLK FEIDPKGEIW IRIDKTHKVN AYIFLRAIGL NKNEIQKGLS KYAFLISASQ
     SYSVKELAKE IGKNDIEEVT DEEALLIVYS KLRPNEPATV PVAKQMLYSR FFDPKRYDLG
     EVGRYKINKK LGLNIPKTFR VLSPQDILSS IDYLINIKDK NSGNLDDIDH LGNRRVRSVG
     ELLQNQFRVG LNRLERIIRE RMMICDIDSL SLSNLINPKP LIASVREFFG SSQLSQFMDQ
     TNPVAELTHK RRISALGPGG FNKDRAGFAV RDLHPSHYGR ICPIETPEGP NAGLIGSLAT
     CARVNIFGFI ETPFYPVHNG QVDYSNNPIY LTADEEDDFR VAPGDVKVNV QNYIEGDIIP
     VRYRQEFVTT IPNQVDYIAI SPIQVISAAT SLIPFLEHDD ANRALMGSNM QRQAVPLLYP
     EKPIIGTGLE TKIARDSGMV VISRTSGCVN YVSANKIGIQ DNNGRTVLYR LKKYYRSNQD
     TCINQRPIVW VGEKIVVGQT LADGASTDCG EIALGRNILV AYMPWEGYNY EDAFLISERL
     VYEDVYTSIH IEKYEVECRQ TKLGPEEITR EIPNVSDHSL KDLDRNGIVV CGSWVEAGDI
     LVGKITPKGE ADQLPEGKLL RAIFGEKARD VRDTSLRLPN AAKGRVVNVR VFTRQKGDEL
     PPGTNAMIRV YVAQKRKIQV GDKMAGRHGN KGIISRILPK QDMPYLCDGT PVDIVLNPLG
     VPSRMNVGQV FECLLGLAGG YLDKRFKIIP FDEMYGAEAS RALVNRKLQE ASILTKNKWI
     FNDQHPGKMQ VFDGRTGEPF DNPVTIGRAY MLKLVHLVDD KIHARSTGPY SLVTQQPLGG
     RAQHGGQRLG EMEVWALEAF GAAYTLQELL TVKSDDMQAR NEALNAIVKG KPIPKPGTPE
     SFKVLMRELQ SLGLDIAVHK LKLFENGQRR TVEVDLMSDS KEDRVARSNY EVLPVDDFEQ
     FLY