ID   RPOB_BIGNA              Reviewed;        1099 AA.
AC   Q06J17;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 62.
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   Bigelowiella natans (Pedinomonas minutissima) (Chlorarachnion sp. (strain
OS   CCMP621)).
OG   Plastid; Chloroplast.
OC   Eukaryota; Sar; Rhizaria; Cercozoa; Chlorarachniophyceae; Bigelowiella.
OX   NCBI_TaxID=227086;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16990439; DOI=10.1093/molbev/msl129;
RA   Rogers M.B., Gilson P.R., Su V., McFadden G.I., Keeling P.J.;
RT   "The complete chloroplast genome of the chlorarachniophyte Bigelowiella
RT   natans: evidence for independent origins of chlorarachniophyte and euglenid
RT   secondary endosymbionts.";
RL   Mol. Biol. Evol. 24:54-62(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DQ851108; ABG91442.1; -; Genomic_DNA.
DR   RefSeq; YP_778610.1; NC_008408.1.
DR   AlphaFoldDB; Q06J17; -.
DR   SMR; Q06J17; -.
DR   GeneID; 4353027; -.
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; -; 3.
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; 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   PANTHER; PTHR20856; PTHR20856; 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..1099
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000300458"
SQ   SEQUENCE   1099 AA;  126538 MW;  50504F4241E9CB6B CRC64;
     MYITPLFFPN LLKLQRKSFL TFLKYGIKKE IKKLDITKNK KKLLVYPNLF QLNLPTYTCN
     ECVITSKTYN CELVIPIRLI SYKDEIEWIT LTNIPIMTNK CNFITNGSPR VIMSQITRAP
     GIYYHKENEN TYYADIIAER GNWLRIEIDK KNNIWMKVKK VPKVPALMFL QALGVTKSNL
     IKLLKYPIPN QNHNLGNFKS QKEALEKIEL YSQLESSINS RNLKNQNKIT IFDRFMNPKY
     YDLGTRGRIQ INKKFNNIEE TIQHSTLTSK DFILAVHFLL KIKYKIEETD DIDNLKNKRV
     KIAGELIQSQ FGIGILRLQK YVKDKLGNIK NNLHLTNIFS STPINTTLAE FFGVNPLSQF
     MDEVNPLATL THKRRLSSLG IGGVNRDTAT LTIRSIHPTL YGRICPIETP EGKNAGLVNS
     FALFAEINSE GLIETPFFRV CNGRILYEMG INYLSANQED KSNIVPFDIK KSRIGFLSKN
     KIAARIKQQF KEVSKKKVDF ISISQLQMLS VATSLIPFME HNDANRVLMG SNMQRQAVPL
     LKTECCLVGT GLETKIFFDL QDNVKSPPNG FISYLSLKKI TISNIRNEHK SFNFKSNPLE
     TITCIKSKSR NFNRLKYNLK DLLTNSKESL KITNYMSYVR EQKIQYYIKQ YNSSNQGTCS
     VNRLTLNEGQ FIIKKNPLIS GLSSCRNELA LGKNLFVGYI SWKGYNFEDA IVLNEQLVIN
     NIYTSTHLEK FETEIKKNKE NSEIITRDIK NISFLNKKNL DKNGIIKIGS RVFSDDILVG
     KLLPIETRIL SPYRKLLYEI LQKQNDHYRN TSLRVPKYKR GRITFVDYIK DKGKIKKKTE
     ILKDLKTIKI HLMQNRLIQI GDKISGRHGN KGVISKILKI QEMPYLNDGI PLDILLNPLG
     VPSRMNIGQV LECLLGLSCF YLQRRFKVIP FDESFGFEVS RNFIYSNLYF SNIKTGNNWL
     LHPYYPGKNR IFDSYSGLPF DQPITIGKAY ILKLIHLVEE KVHARSTGSY SLVTQQPLKG
     KSKKGGQRVG EMEVWALEGY GAAYTLHEIL TVKSDDIKSR QKVLTSILNS ETIKFGTTET
     FKVLIRELQS LCLNIQFFK