RPOB_VITVI
ID RPOB_VITVI Reviewed; 1070 AA.
AC Q0ZJ28;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 78.
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 Vitis vinifera (Grape).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Maxxa;
RX PubMed=16603088; DOI=10.1186/1471-2148-6-32;
RA Jansen R.K., Kaittanis C., Lee S.-B., Saski C., Tomkins J., Alverson A.J.,
RA Daniell H.;
RT "Phylogenetic analyses of Vitis (Vitaceae) based on complete chloroplast
RT genome sequences: effects of taxon sampling and phylogenetic methods on
RT resolving relationships among rosids.";
RL BMC Evol. Biol. 6:32-32(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; DQ424856; ABE47526.1; -; Genomic_DNA.
DR RefSeq; YP_567068.1; NC_007957.1.
DR AlphaFoldDB; Q0ZJ28; -.
DR SMR; Q0ZJ28; -.
DR STRING; 29760.VIT_04s0079g00620.t01; -.
DR PRIDE; Q0ZJ28; -.
DR GeneID; 4025099; -.
DR KEGG; vvi:4025099; -.
DR eggNOG; KOG0214; Eukaryota.
DR InParanoid; Q0ZJ28; -.
DR OrthoDB; 944344at2759; -.
DR Proteomes; UP000009183; Chloroplast.
DR ExpressionAtlas; Q0ZJ28; baseline and differential.
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; 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 Reference proteome; Transcription; Transferase.
FT CHAIN 1..1070
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000276598"
SQ SEQUENCE 1070 AA; 120544 MW; 4A6C8A690216D240 CRC64;
MFRGGNEGMS TIPGFNQIQF EGFCRFIDQG LTEELYKFPK IEDTDQEIEF QLFVETYQLV
EPLIKERDAV YESLTYSSEL YVSAGLIWKT SRDMQEQTIF IGNIPLMNSL GTSIVNGLYR
IVINQILQSP GIYYRSELDH NGISVYTGTI VSDWGGRLEL EIDRKARIWA RVSRKQKISI
LVLSSAMGSN LREILENVCY PEIFLSFLND KEKKKIGSKE SAILEFYQQF ACVGGDPVFS
ESLCKELQKK FFQQRCELGR IGRRNINRRL NLDIPQNNTF LLPQDILAAA DHLIGMKFGM
GILDDMNHLK NKRIRSVADL LQDQFGLALI RLENVVRGTI CGAIRHKLIP TPQNLVTSTP
VTTTYESFFG LHPLSQVLDR TNPLTQIVHG RKSSYLGPGG LTGRTASFRI RDIHPSHYGR
ICPIDTSEGI NVGLIGSLAI HARIGHWGSL ESPFYEISER SKKVRMLYLS PSRDEYYMVA
AGNSLALNQG IQEEQVVPAR YRQEFLTIAW EQVHLRSIFP FQYFSIGASL IPFIEHNDAN
RALMSSNMQR QAVPLSRSEK CIVGTGLERQ AALDSGVPVI AEHEGKIVYT DTDKIILSGN
GDTLSIPLVM YQRSNKNTCM HQKAQVRRGK CIKKGQILAD GAATVGGELA LGKNVLVAYM
PWEGYNSEDA VLISERLVYG DIYTSFHIRK YEIQTHVTSQ GPERITNKIP HLEAHLLRNL
DKNGIVILGS WVETGDILVG KLTPQMAKES SYAPEDRLLR AILGIQVSTS KETCLKLPIG
GRGRVIDVRW IQKKGGSSYN PETIRVYISQ KREIKVGDKV AGRHGNKGII SKILPRQDMP
YLQDGRPVDM VFNPLGVPSR MNVGQIFECS LGLAGGLLDR HYRIAPFDEK YEQEASRKLV
FSELYEASKQ TANPWVFEPE YPGKSRIFDG RTGDPFEQPV IIGKPYILKL IHQVDDKIHG
RSSGHYALVT QQPLRGRAKQ GGQRVGEMEV WALEGFGVAH ILQEMLTYKS DHIRARQEVL
GTTIIGGTIP NPEDAPESFR LLVRELRSLA LELNHFLVSE KNFQINRKEA
