RPOB_NEPOL
ID RPOB_NEPOL Reviewed; 1109 AA.
AC Q9TL06;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 96.
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 Nephroselmis olivacea (Green alga).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; Nephroselmidophyceae;
OC Nephroselmidales; Nephroselmidaceae; Nephroselmis.
OX NCBI_TaxID=31312;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-484 / S-N-5-8;
RX PubMed=10468594; DOI=10.1073/pnas.96.18.10248;
RA Turmel M., Otis C., Lemieux C.;
RT "The complete chloroplast DNA sequence of the green alga Nephroselmis
RT olivacea: insights into the architecture of ancestral chloroplast
RT genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:10248-10253(1999).
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; AF137379; AAD54810.1; -; Genomic_DNA.
DR RefSeq; NP_050839.1; NC_000927.1.
DR AlphaFoldDB; Q9TL06; -.
DR SMR; Q9TL06; -.
DR PRIDE; Q9TL06; -.
DR GeneID; 801913; -.
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..1109
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000048032"
SQ SEQUENCE 1109 AA; 124886 MW; C8118702BD4A5849 CRC64;
MIQNLQRKDS QWTPFILPDL ISIQRDSFLL FLERGLATEL SHVTPLTGSH FRITLCSHGY
RLKRPKVSIQ EAVYQATSYS AALYVNVETN QSNLGTQETQ IQSVWMGDIP LMTSRGHFII
NGSSRVVVNQ IVRSPGIYFK EMIDQKHRRM FQASIISNRG SWVRLETDVD GMIWVRMDKA
KKISILIVLE AMGLSKKTIF RSLKSPEFLF KALQQLLAKK RWQDKVYELI PQSTTDALFH
LYTKLSPDKP GNTLTARRVL YEKLMDAKRY DVGLVGRVKL NKKLKLPVPE HVHTLRPVDF
LAATDYLIGL EYGRGQVDDI DHLKNRRVRC AGELIQSQLR IGLNRLERTM QGRISRPGEL
PGMSSLMNPK PVMAALREFF GSNPLSQFMD QTNPLAELTH KRRLSSLGPG GLSQDRAGMA
VREIHPSQYG RICPIETPEG PNAGLIGSMA TYARLNQYGG LECPFYQVVE GKVLYEFGPI
FLTAEQEDQV TVVAGDILDQ RKLMVAVAEG RDPLDPAVRP TLPDRPLILR SRQEFHTGSF
RDVNYVGIAP TQMISVATSL IPFLEHDDAN RALMGSNMQR QAVPLLKTEA PIIGTGLEAQ
VAADAGGVVQ SPFEGIVVYV DATRIVVSTS KSKLALSKKR KIHESNVFLQ VYQRSNQGTC
IHQRPIIPLH TPVIRGDLLA DGSSTSGGQI ALGKNLLVAY MPWEGYNFED AILISERLIY
DDLYTSLHIE RYEVETQHTK LGPEEITKSI VHETDDKLPY RWLDERGIVM RGAWVEPGDV
LIGKITPKEE KELTPELRLV YAIFGKRPKG FRDTSLRVPQ GVRGRVVDVR MIRDEDTKVV
HVYVCQQRQI QVGDKMAGRH GNKGIVSRIV PRQDMPYLQD GTPVDMVLNP LGVPSRMNVG
QVFECLLGLA GQRLGQQLKV RAFDEMYGAE ASRHLVYNKL HEASEVTGHH WLFDPNHPGK
SRLIDGRTGD MFDQAVTIGQ AYMLKLIHQV DDKIHARATG PYSLITQQPL GGRSKRGGQR
LGEMEVWAFE GFGAAYTLQE LLTVKSDDMQ GRNEIMSAMV QGRQLPEMGT PESFKVMIRE
LQALCLDIGI YHRSKMTFKT EEIDLMQMR