RPOB_OLTVI
ID RPOB_OLTVI Reviewed; 1416 AA.
AC Q20EX1;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 61.
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 Oltmannsiellopsis viridis (Marine flagellate) (Oltmannsiella viridis).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; Ulvophyceae; Oltmannsiellopsidales;
OC Oltmannsiellopsidaceae; Oltmannsiellopsis.
OX NCBI_TaxID=51324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16472375; DOI=10.1186/1741-7007-4-3;
RA Pombert J.-F., Lemieux C., Turmel M.;
RT "The complete chloroplast DNA sequence of the green alga Oltmannsiellopsis
RT viridis reveals a distinctive quadripartite architecture in the chloroplast
RT genome of early diverging ulvophytes.";
RL BMC Biol. 4:3-3(2006).
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; DQ291132; ABB81942.1; -; Genomic_DNA.
DR RefSeq; YP_635874.1; NC_008099.1.
DR AlphaFoldDB; Q20EX1; -.
DR SMR; Q20EX1; -.
DR PRIDE; Q20EX1; -.
DR GeneID; 4100134; -.
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; -; 2.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 2.
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; 2.
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..1416
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000237327"
SQ SEQUENCE 1416 AA; 158293 MW; 80FBC4EE453C0D25 CRC64;
MNIYLRQNSF LVPDFIAVQR NSFSQFLESG LIQEISKRNP ITNSTKELEL CFYPQYYKLS
PPELNAKQSI LKNKTYSCRL YIPVKLTNKR TKTLKLQWVV LGNLPLMTKR GHFIINGSPR
VIINQMVRSP GVYFKEVSHA DQKLTYYADL IAYRGAWLRI ELDKKADIWA RMKKTPKLPM
LILLQALGLN LPTILKSLNY PKFFENLGHD GNFMKQLKKG RVSSRSSSQE LSGSFNLSED
VSLRLDDSSK NMGAENVQRA PLQKSTKKAT LFGDFSRSSV YCKTQEEALW ALYALTHPLK
NPDEVTANLG KSFLYRKFMN SRVYDLSPLG RLRLNQKLNL SVNENITTIT AQDLLFITNT
LINLNYGVGK VDDIDNLKNR RIRTAGELVQ NQFGIGLLRL EKIIREKLKQ QQTKLSIGSL
INTKPINGAL REFFGSSPLS QFMDQTNPLA EITHKRRLSS LGPGGVNRET AGMAIRGIHP
THYGRICPIE TPEGQNAGLV NSLTIYSRVN PYGFIETPFY KVVKGQVQNS TRPIFFSAYQ
EEKKLLAPGD IYANKLKYLP KSELPIRKLA EFTRTTREKI DYISVSPLQM ISIATSLIPF
LEHDDANRAL MGSNMQRQAV PLMTAEAPVV GTGLECRVAS DSGHVLQAKK SGFVTYSSAE
KITILSPVDS TPAVPKLSKG NNSPQHFHES VGGSCKESQS LQAAAEGYLS GVASSSSSKF
TGSSFSTISA LNDGVLRRAL TQKVLTTGTN CSSMLKNQRF FVEPKAQLYT GAQTPVGRVE
TILQPNHAEG YLSEVETIQQ TQNKLPLQVR FGVEAPKSSF DSEATKISST LNSIPQHPVL
GEDSPSKQVG WALKDPQIQT MLKPKWHHSA QTMSRENWYQ NLKGQNVKTF TQVESGRLVT
KPTNTKMPMS SLAGTANSKK TGEALYKLAS SESATKSMDF STKTQLKPIT YELQKLFRSN
QDTSIMHRPV VREGEWVNRG DLLADNSTTV GGELSLGKNL LLAYMPWEGY NFEDAILISE
RLVSDDAYTS LHIERYEVEI RETKFGLEQI TSQIPDEGKL SHLDHFGIAK PGTWVEEGDI
LIGKVAPMPQ KNLSRYEKLL YDVVGKKIST TRDTSLRVPR GVSGRVIHVE ILNAENLPPE
FVFEGPSRVN LYIAEKRKIH VGDKMAGRHG NKGIISNILP RQDMPYLPDG TPLDMVLNPL
GVPSRMNVGQ IYECLLGLAG RYLGQKFKVR PFDEIYGPQT SRSLVYSKLY EARLRTGQRW
LFNPASPGKT RLFDGRTGEC FSQPVTVGQA YMLKLIHLVD EKIHARSIGP YSLVTQQPLR
GRSKHGGQRL GEMEVWALEG FGAAYTLQEL LTVKSDDIKG REQVMESIQK NKTISLGTPE
SFKVLIRELQ SLCLDVGVYA VDGSGKIKQV DTMKLP
