ID   RPOB_ANGEV              Reviewed;        1070 AA.
AC   A2T324;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 60.
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   Angiopteris evecta (Mule's foot fern) (Polypodium evectum).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Polypodiopsida; Marattiidae; Marattiales; Marattiaceae; Angiopteris.
OX   NCBI_TaxID=13825;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Roper J.M., Hansen S.K., Wolf P.G., Karol K.G., Mandoli D.F.,
RA   Everett K.D.E., Kuehl J.V., Boore J.L.;
RT   "The complete plastid genome sequence of Angiopteris evecta (G. Forst.)
RT   Hoffm. (Marattiaceae).";
RL   Am. Fern J. 97:95-106(2007).
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; DQ821119; ABG79591.1; -; Genomic_DNA.
DR   RefSeq; YP_001023692.1; NC_008829.1.
DR   AlphaFoldDB; A2T324; -.
DR   SMR; A2T324; -.
DR   GeneID; 4788203; -.
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..1070
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000300431"
SQ   SEQUENCE   1070 AA;  121389 MW;  CA08FB380DEF3509 CRC64;
     MILKENKKMF VLPEFGRIQF EGFQRFIHQD LVEELTNFPK IEDIDQEVEF RLFGERYRLT
     EPCIKERDAV YQSFTYSSDL YVPAQLMRRR NGRIQRQTVH FGSIPLMNSQ GTFVINGIAR
     VVINQILRSP GIYYDSELDH NGNSIYTGTI ISDWGGRFKS EIDGKKRIWV RLSKNRKVSI
     IILLLAMGLN MNDILKNVRY PNIFLRLFQR QAENIQSYED AIVELYKNLY SAGGNLVFSD
     SICKELQTKF FQQKFELGQF GRRNLNKKLN LDVPGNEHLL LPQDLLAAVD YLIGVNYGIG
     TLDDIDDLKN RRVRSVADLL REQLGLALDR LEILIRQTIH TVARRKRLVT PKGLITSAPL
     TTIFQDFFGS HSLSQFLDQT NPLAELTHKR RLSSLGPGGL TRRTASFQVR DINPSHYGRI
     CPIETSEGMN AGLIASLAIH AKVNDRGSLL SPFYKISKTL GEEHIVYLSS EEDEYYRIAT
     GNTLSLDREI REERATPARY RQEFLTIAWK QIHFRSIFPF QYFSIGTSLI PFLEHNDANR
     ALMGSNMQRQ AVPLSQPEKC IVGTGLESQI ALDSGSVVVS NQDGQIAYLD GETISILLQN
     EKTVDIKSII YERSNNNTCI HQRPVVSQGE RLRKGQLLAD GTATVGGELA LGRNILVAYM
     PWEGYNFEDA VLISERLIYE DIYTSFHIER YEINIYTTSQ GPEKITKEIP HLDSYVLRHL
     DNNGLVVPGS WVETGDVLVG KLTPQEAENS LRVPEGKLLQ AISGIQLANT RESCLKVPIG
     GRGRVIDVRW IYDEDTLPNI ANMVHVYILQ KRKIQVGDKV AGRHGNKGIV SKILPRQDMP
     YLQDGTPVDM ILSPLGVPSR MNVGQIFECL LGLAGDILKK HYRITPFDER YEREASRKLV
     FSELHEASQE AAIPWLFEPD HPGKSRLIDG RTGDIFEQPV TIGKAYMMKL IHQVDDKIHA
     RSSGPYALVT QQPLRGRSRG GGQRVGEMEV WALEGFGVSY ILQEMLTIKS DHIPARSKLL
     GSIVTGKSIP KPNTVPESFR LLVRELRSLA VNSDHNLIFE KDLRKKVKDV