ID   RPOB_STAPU              Reviewed;        1068 AA.
AC   Q32RW5;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 63.
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   Staurastrum punctulatum (Green alga) (Cosmoastrum punctulatum).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Zygnemophyceae; Zygnematophycidae;
OC   Desmidiales; Desmidiaceae; Staurastrum.
OX   NCBI_TaxID=102822;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16236178; DOI=10.1186/1741-7007-3-22;
RA   Turmel M., Otis C., Lemieux C.;
RT   "The complete chloroplast DNA sequences of the charophycean green algae
RT   Staurastrum and Zygnema reveal that the chloroplast genome underwent
RT   extensive changes during the evolution of the Zygnematales.";
RL   BMC Biol. 3:22-22(2005).
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; AY958085; AAX45747.1; -; Genomic_DNA.
DR   RefSeq; YP_636411.1; NC_008116.1.
DR   AlphaFoldDB; Q32RW5; -.
DR   SMR; Q32RW5; -.
DR   GeneID; 4108609; -.
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; 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; 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..1068
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000224134"
SQ   SEQUENCE   1068 AA;  120562 MW;  B0D9A4DFE96B62D7 CRC64;
     MEMNMFILPD FLQIQIESFR RFLHNCIFEE LSKFPIIYDS NQGIEFKLIP EKYLLTEPLF
     TEREAVYKFT TYSSDLYVPI QLTLTKEKKS RIQTVCLGSL PLMTPQGTFV INGVSWTIVN
     QILRNPGIYY VLNRNGMYTA TILCLDVDKR LRLEIDKKGR LSVRINNRHK IPLVFLLIAL
     GLDINDIPDW LQSRTKKLED LLSGLKNEGE RTLELIALYK QLPGPKKVKP KANPLIISEQ
     IQQWCAQVYK LGTSGRLNLN RRLNLNFSKS NDSLLPQDLI AAAELLVKMS LLHPGPKGGK
     DSSDDIDHLK NKHVISVAEM LRKQLSLCLI DLQIQVRRAI RRGISSKRIL SPRSMMISRP
     LTQMFNQFFG SHELIQFLDQ TNPLAEMAHK RKLSLLGPGG LTRRTASFRT RDIHPSHYGR
     ICTIETSEGM NAGVIPSLSI CARVDSEGVI ENPLHKIGGN IKEQYTVYVR AGRDERLKIG
     TNNCLAIGQK GQERSTSTQY QQEFVSMSWD QINLRSILPI QYFAIGASLI PFLEHNDATR
     TLMGSSMQRQ AVPLVKPEKS IVGTGIEAHI SLDSGTVLIS LKDGKIKYVD GKQIVLVDKD
     NVQQKFNLIT YERSNNGTCI HQRPTVKIGF SVRKGQLLAD GSATVGGELA LGKNVLVAYM
     PWEGYNFEDA VLISDRLVNE DIYTSIHIQR YEISVQENIE GFDIITREIP HVDKYLLRHL
     DYRGIIKIGA WVEPGDVLVG KLAPLEAPHL LRSPEGKLLQ AIFGVQAITT RESCLKLPAG
     GTGRVIDVRW IEQQGPSGVS SLHVYILQKR KIQVGDKVAG RHGNKGVVSR ILPREDMPYM
     QDGTPIDMVL SPLGVPSRMN VGQLFECLLG LAGSYLNNHY RIMPFDERFE REASRKLVFS
     ELYKARKFTG YPWLFEPNSP GKSSLFDGRT GEIFEQSITV GKAYMMKLIH MVDEKIHARS
     SGPYALVTQQ PLRGRSNKGG QRVGEMEVWA FEGFGAAYML QEILTIKSDH VKGRSQVRGA
     IVAKESIPKP IDPPDCFRLL IRELRCLGIE IKHTIISEKN FFLDQKPI