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