RPOB_TRICV
ID RPOB_TRICV Reviewed; 1379 AA.
AC P49466;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 107.
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 Trieres chinensis (Marine centric diatom) (Odontella sinensis).
OG Plastid; Chloroplast.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta; Mediophyceae;
OC Biddulphiophycidae; Eupodiscales; Parodontellaceae; Trieres.
OX NCBI_TaxID=1514140;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kowallik K.V., Stoebe B., Schaffran I., Kroth-Pancic P., Freier U.;
RT "The chloroplast genome of a chlorophyll a+c-containing alga, Odontella
RT sinensis.";
RL Plant Mol. Biol. Rep. 13:336-342(1995).
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; Z67753; CAA91744.1; -; Genomic_DNA.
DR PIR; S78371; S78371.
DR AlphaFoldDB; P49466; -.
DR SMR; P49466; -.
DR PRIDE; P49466; -.
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 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..1379
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000048034"
SQ SEQUENCE 1379 AA; 159100 MW; 187AE76F29E3720B CRC64;
MNYSTALPDF IEMQRVSFCW FIAQGLNDEL TMFSRIHDFS YNTEYRLFGQ EYSLVKPVYT
IVRAKKLAAN YSVQLVIPLE VRNKKLNSVR YFGQFTIINL PLMTTTATFV INGCERVIVS
QIIRSPGIYF EKNKNHRKRK QFKSQVLGHA SKLGSFLPSG VPWIIPYDQP WKPWIIGKKL
GYSKYNSNKD TKLDFYFYSL KSFKIYQKIS KITNSPIKVQ RIKLFLQWLK LNQKEFNFKN
KLNLSELSFL LNYWNFIFKF IIKYQFLYKK NFEESYQIQE SEFKTIFKTW NNQPQLNDSF
SLKKIDQLTS NYEKKIQFYH NVIQQQFFDN LMLVPFITKE KKILNLESLA NRQKQKKISL
TLLTNESIKF AFYFSPSLKE VFKYRSPKKR KPKEAKIKQP ILYLRSPSKI VQFKDDHQVL
DSYKKKYDTK DFYTATLIPE SGSWIRFGFQ KNTKINRYQY PIRHQEDEVI IQIDKITQKP
ILYLLKEMGL TDWEICSNLK HADFFYFTKP FLTGSLTSKQ PLPRFDLHSD YYKNISEFSH
IFDARYYRLG KIGRFQINNR LNLKLNNRIY TITYEDIFAI LDCLVTLSIS KTTGDDIDHL
KNRRVRSVGE LLQNLFRVGF QRLVRKLGSQ INKRESGQIS SFNIIGATVR EFFGSSQLSQ
YMDQTNPLSS LTHRRRISGL GPGGLDRDRI SFAVRDIHPS HYGRICPIET PEGPNVGLIA
SLTTCARVNK LGFIETPFWR VINGKVIKTG NPIYLTADIE DFYKIAPADI STNSKNYLTQ
NLIPVRYKQD FITVSPFQVD FISISPIQVV SVATSLIPFF EHDDANRALM GSNMQRQSVP
LMLSQKPIVG TGLENQIAID SGMTINAQGA GIVHSVTADY IIVKEYSGRK LKYILQKYQR
SNQETCINHR PIVWKGEKIK SGQILTDGPG ITNNELALGQ NVLVAYMPWQ GYNFEDAILI
NERLVYEDVF TSIHIERYDI EIEQDDDVSE QITKNIPNLS FSEIQNLNDD GIVALGTFVK
PGDILVGKII AKNDSEQLPE AKLLRAIFGA KAKGVRDTSF RMPKGKYGRV VDRVTFNRKT
KLAYKFEKIQ VFIAQIRKIK VGDKIAGRHG NKGIISRILP RQDMPFLPDG TPVDIILNPL
GVPSRMNVGQ LYECLLGIAG HKLNRRFKIL PFDEMYGPEV SRILINKKLR QASIENDEAW
LFNPYSPGKM VLIDGRTGKE FENPITVGNA YMLKLIHLVD DKMHARATGP YSLITQQPLG
GKAQHGGQRF GEMEVWALEG FGAAFTLKEL LTIKSDDMQG RNETLNAIVK GQLIPKSGVP
ESFKVLLQEL RSIGLDMSTY KIENYNLNQH YELEVDLIET YDSLEKTFPP TSNLDDISF
