RPOB_GRATL
ID RPOB_GRATL Reviewed; 1120 AA.
AC Q6B8R8;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
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}; OrderedLocusNames=Grc000136;
OS Gracilaria tenuistipitata var. liui (Red alga).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gracilariales;
OC Gracilariaceae; Agarophyton; Agarophyton tenuistipitatum.
OX NCBI_TaxID=285951;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15638458; DOI=10.1007/s00239-004-2638-3;
RA Hagopian J.C., Reis M., Kitajima J.P., Bhattacharya D., de Oliveira M.C.;
RT "Comparative analysis of the complete plastid genome sequence of the red
RT alga Gracilaria tenuistipitata var. liui provides insights into the
RT evolution of rhodoplasts and their relationship to other plastids.";
RL J. Mol. Evol. 59:464-477(2004).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY673996; AAT79717.1; -; Genomic_DNA.
DR RefSeq; YP_063642.1; NC_006137.1.
DR AlphaFoldDB; Q6B8R8; -.
DR SMR; Q6B8R8; -.
DR PRIDE; Q6B8R8; -.
DR GeneID; 2944076; -.
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; IPR019462; DNA-dir_RNA_pol_bsu_external_1.
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; PF10385; RNA_pol_Rpb2_45; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR TIGRFAMs; TIGR02013; rpoB; 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..1120
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000048023"
SQ SEQUENCE 1120 AA; 126423 MW; 53A3AECDFBE81E64 CRC64;
MRLLMSQEIM FKYIFPDLAA IQKESFKSFL LEGLSEVLDS FPIIVDPTGK LELQFFGKDY
KLKFPRYSVR KAKSRDKTYS AQIYIPAKLT RRDIEVIKEN ISTSKDLSYF FNSQDINKKY
RKRPVFIGDL PLMTNRGTFV ISGTERIIIN QIVRSPGVYY KKELDKNNKQ IYSCSIISNR
GSWLKFEIDS KAQIWAKIDK NHKVSAYIFL RSIGLNNEDI RKRLTKYNYL INSSLTYYKK
EFSKDVNNVD IEKITEEEAL VIVYSKLRPN EPATLAVAKQ MLYTRFFDPK RYDLGAVGRH
KINQKLNLKV PTHFRVLSPE DILVSLDYLL NIKEQNIGTF DDIDHLGNRR VRSVGELLQN
QVRIGLNRLE RIIRERMIIC DLDSLSLSNL VNPKPLMASV REFFSSSQLS QFMDQTNPLS
ELTHKRRISA LGPGGLNKDR AGFAVRDLHP SHYGRICPIE TPEGPNAGLI GSLSIYAKVN
RYGFIETPCY KVTDGQVLKK DKLYYITADQ EDYLRIAPAD ISLDVNDFIQ DKIIAVRYKQ
EFITATISQV DYMAVSPIQF ISAATSLIPF LEHDDANRAL MGSNMQRQAV PLLFPEKSIV
GTGLEAKIAK DSGMTIISRT NGTVSYVSGT KIGIQNKEGY TIHYRLKKYY RSNQDTCINQ
RPIVWPGENI RIGQTIADGA STDGGEIALG RNIIVAYMPW EGYNYEDAFL ISERLVYEDL
YTSIHIERYE LECRQTKLGS EEITRDIPNV SEASIGLLDK NGIISIGSWV DAGDILVGKV
TPKGESDQLP EGKLLRAIFG EKARDVRDTS LRLPNATKGR VVNVKIFKRQ KGDELPPGTN
EIIRVYVAQK RKIQVGDKMA GRHGNKGIIS RILSLQDMPF LPDGTPVDII LNPLGVPSRM
NVGQLFECLL GLAGEYSSKR FKIIPFDEMY GSEASRALVY NKLKQASSMN DKSWLFNALH
PGKVMLVDGR TGEFFDNPVT VGKAYILKLV HLVDDKIHAR STGPYSLVTQ QPLGGRAQHG
GQRLGEMEVW ALEAFGAAYT LQELLTVKSD DMQGRNDALN AIVKGKPIPK PGTPESFKVL
MRELQSLALD IAVHKLELLD NGNKASIEID LMSDEQVSAI
