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RPOB_HUPLU
ID   RPOB_HUPLU              Reviewed;        1080 AA.
AC   Q5SCX8;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 69.
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   Huperzia lucidula (Shining clubmoss) (Lycopodium lucidulum).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Lycopodiopsida; Lycopodiales; Lycopodiaceae; Huperzioideae; Huperzia.
OX   NCBI_TaxID=37429;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15788152; DOI=10.1016/j.gene.2005.01.018;
RA   Wolf P.G., Karol K.G., Mandoli D.F., Kuehl J.V., Arumuganathan K.,
RA   Ellis M.W., Mishler B.D., Kelch D.G., Olmstead R.G., Boore J.L.;
RT   "The first complete chloroplast genome sequence of a lycophyte, Huperzia
RT   lucidula (Lycopodiaceae).";
RL   Gene 350:117-128(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; AY660566; AAT80747.1; -; Genomic_DNA.
DR   RefSeq; YP_209551.2; NC_006861.1.
DR   AlphaFoldDB; Q5SCX8; -.
DR   SMR; Q5SCX8; -.
DR   GeneID; 3283789; -.
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..1080
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000048026"
SQ   SEQUENCE   1080 AA;  122783 MW;  E23F5AA67ACED106 CRC64;
     MKIDLEQNED IYVLPDFRKI QLEAFHRFIN QGIMEELDNF PKIEDTDQEF EFQLFGEKYY
     LLEPSVKEGD SLYESIITNS CKLYVPARLT QRKKGKVKEQ TVFIGNIPLM SSQGTFVING
     IARVIINQML RSPGIYYKSE KDPDSGEITT YTATIISNWG ERLQLELDAN NRIWFRIDKK
     HKVSILLLLL AMGLNEEKIL DTVHYPEVMS DIIREAKDEE NIEWKENAVS ELYEQIFGTT
     DEEDVESYDI FEELKKEFFE PKFELGRIGR FNINKKLNLN VPKDEIFLLP KDVLAAIDYS
     IKLRIGVGTF DDVDHLKNKR IRSVADFLQN RFKLALERLG DLVHRRINRL TRRKRVPTIG
     SLVTSDPLLK TFKEFFGSYP LSQFLDQTNP LTQVIHKRRF SSLGPGGLTK RIASIKARDI
     HPSIYGRICP IETSEGMNAG LISSMAIYAS IDHWGFLQST LHKEYDEVLF EEQNQDMADV
     SAEEYFRIAT EACLAVSPEE DENKEIFTVA QLQQEFLTTS WDRIKLRIIS PLQYFSVGVC
     PIPSFEHNDA NRALMGSNMQ RQAVPLFEPE RCIVGTGLEG QAASDSGSVV IAEQGGKVDY
     VDGKEITLLV NGGGTINTKL ITYQRSNNNT CMHQKPRVNL GEYLKEGQIL ADGAATEGGE
     PASGKNILVA YMPWEGYNFE DAVLINECLI YENVFTSIHI EKYEVEARIT LNGPEILTRE
     IPHLDDYFLR HLDENGLVLP GSWVETGDVI VGKLTPRDPE ESLKIPEGNL LQAIFGIDIT
     ATRETCLKVP PGGKGQVIDV RSVYPEDDNQ YRNFIYVYIL QKREIKVGDK VAGRHGNKGI
     ISKILPREDM PYLQDGTPIE MILSPLGVPS RMNVGQIFEC LLGLAGGFLK RHYRVIPFDE
     RYEREASRKL VFSELNKAGE QTTNPWLFEL DNPGKSLLID GRTGEIFQQP ITIGKAYMLK
     LIHQVDDKIH ARSSGPYSLV TQQPLKGRSR MGGQRVGEME VWALEGFGAS YILQEMLTIK
     SDHIQARQKI INNIVAGEPV DKPETTPESF RLLARELRCL ALNLDHAVVK KDLIIDYKEL
 
 
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