RPOB_ACOAM
ID RPOB_ACOAM Reviewed; 1083 AA.
AC A9LYH7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 52.
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 Acorus americanus (Sweetflag) (Acorus calamus var. americanus).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Acoraceae; Acorus.
OX NCBI_TaxID=263995;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Peery R.M., Chumley T.W., Kuehl J.V., Boore J.L., Raubeson L.A.;
RT "The complete chloroplast genome of Acorus americanus.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; EU273602; ABX38736.1; -; Genomic_DNA.
DR RefSeq; YP_001586174.1; NC_010093.1.
DR AlphaFoldDB; A9LYH7; -.
DR SMR; A9LYH7; -.
DR GeneID; 5777712; -.
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; -; 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; 3.
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..1083
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000329197"
SQ SEQUENCE 1083 AA; 122370 MW; 8F22C50244A37BC8 CRC64;
MGFLFSINRK LKMPRDGNEG MFTIPGFSQI QFEGFCRFID QGLMEEFHKF PKIEDTDQEI
EFQLFVERYQ LVEPLIKERD AVYESLTYSS ELYVPAGLIW KTGRDMQEQT IFIGNIPLMN
SLGTFIVNGI YRIVINQILQ SPGIYYRSEL DHNGISVYTS TIISDWGGRS ELEIDRKSRI
WARVSRKQKI SILVLSSAMG SNLREILDNV CYPEIFLSFL NDREKKKIGS KENAILEFYQ
QFACVGGDPV FSESLCKELQ KKFFQQRCEL GRIGRRNMNR RLNLDIPQSN TFLLPRDVLA
AADHLIGMKF GMGTLDDMNH LKNKRIRSVA DLLQDQFGLA LVRLENAVRG TICGAIRHKL
ILTPQNLVSS TSLTTTYESF FGLHPLSQVL DRTNPLTQIV HGRKLSYLGP GGLTGRTASF
RIRDIHPSHY GRICPIDTSE GINVGLIGSL AIHARIGHWG SIESPFYEVY QRSKETKMVF
LSPSRDEYYT VATGNSLALN RGGIQEEQIV PARYRQEFLT IAWEQIHLRS IFPFQYFSIG
ASLIPFIEHN DANRALMSSN MQRQAVPLSR SEKCIVGTGL ERQAALDSGV SAIAECEGKI
IHTDTHKIVL SGHGDTISIP LVMYQRSNKN TCMHQNPQVR RGKCIKKGQI LADGAATVGG
ELALGKNVLV AYMPWEGYNF EDAVLISERL VYEDIYTSFH IRKYEIQTHV TSQGPERITH
EIPHLEAHLL RNLDRNGIVA LGSWVETGDI LVGKLTPQTA NESSYAPEDR LLRAILGIQV
STAKETCLKL PIGGRGRVID VRWIQKKGGS SYNPETIRVY ISQKREIKVG DKVAGRHGNK
GIISKILSRQ DMPYLQDGTP VDMVFNPLGV PSRMNVGQIF ECSLGLAGDL LDRHYRIAPF
DERYEQEASR KLVFSELYEA SKQTANPWVF EPEYPGKSRI FDGRTGDPFE QPVLIGKSYI
LKLIHQVDDK IHGRSSGHYA LVTQQPLRGR AKQGGQRVGE MEVWALEGFG VAHILQEMLT
YKSDHIRARQ EVLGTTIIGG TIPTPEDAPE SFRLLVRELR SLALELNHFL VSEKNFQINR
KEA