RPOB_SINAL
ID RPOB_SINAL Reviewed; 1078 AA.
AC P46818; Q9THV7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=DNA-directed RNA polymerase subunit beta;
DE EC=2.7.7.6;
DE AltName: Full=PEP;
DE AltName: Full=Plastid-encoded RNA polymerase subunit beta;
DE Short=RNA polymerase subunit beta;
GN Name=rpoB;
OS Sinapis alba (White mustard) (Brassica hirta).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Sinapis.
OX NCBI_TaxID=3728;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-8,
RP CHARACTERIZATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=cv. Albatros; TISSUE=Cotyledon;
RX PubMed=10601874; DOI=10.1046/j.1432-1327.2000.00991.x;
RA Pfannschmidt T., Ogrzewalla K., Baginsky S., Sickmann A., Meyer H.E.,
RA Link G.;
RT "The multisubunit chloroplast RNA polymerase A from mustard (Sinapis alba
RT L.). Integration of a prokaryotic core into a larger complex with
RT organelle-specific functions.";
RL Eur. J. Biochem. 267:253-261(2000).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
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;
CC -!- SUBUNIT: The minimal PEP RNA polymerase found in etioplasts (PEP-B) is
CC composed of four subunits: alpha, beta, beta', and beta''. Following
CC differentiation into chloroplasts the PEP-A RNA polymerase in this
CC organism has been shown to be composed of at least 13 subunits,
CC including the PEP-B subunits. When a (nuclear-encoded) sigma factor is
CC associated with the core the holoenzyme is formed, which can initiate
CC transcription (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- MISCELLANEOUS: A second beta-like protein with a slightly lower
CC molecular weight has been purified with the PEP-A polymerase as
CC identified by mass spectrometry.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000305}.
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DR EMBL; X82417; CAA57814.1; -; Genomic_DNA.
DR EMBL; AJ243754; CAB48411.1; -; Genomic_DNA.
DR PIR; S48842; S48842.
DR AlphaFoldDB; P46818; -.
DR SMR; P46818; -.
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 1: Evidence at protein level;
KW Chloroplast; Direct protein sequencing; DNA-directed RNA polymerase;
KW Nucleotidyltransferase; Plastid; Transcription; Transferase.
FT CHAIN 1..1078
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000048048"
FT CONFLICT 4
FT /note="A -> S (in Ref. 1; CAA57814)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1078 AA; 121654 MW; B0C0F2367526DBF8 CRC64;
MINAKKMLGD GKEGTSTIPG FNQIQFEGFY RFIDQGLIEE LSKFPKIEDI DHEIEFQLFV
ETYQLVEPLI KERDAVYESL TYSSELYVSA GLIWKTNRNM QEQRIFIGNI PLMNSLGTSI
VNGIYRVVIN QILQSPGIYY QSELDHNGIS VYTGTIISDW GGRLELEIDK KARIWARVSR
KQKISILVLS SAMGSNLREI LENVCYPEIF LSFLTDKEKK KIGSKENAIL EFYQQFSCVG
GDPIFSESLC KELQKKFFHQ RCELGRIGRR NINWRLNLNI PQNNIFLLPR DILAAADHLI
GMKFGMGTLD DMNHLKNKRI RSVADLLQDQ LGLALARLEN VVKGTIGGAI RHKLIPPTQN
LVTSTPLTTT YESFFGFHPL SQVLDRTNPL TQIVHGRKLS YLGPGGLTGR TANFRIRDIH
PSHYGRICPI DTSEGINVGL IGSLSIHARI GDWGSLESPF YELVEKSKKA QIRMLFLSPS
QDEYYMIAAG NSLALNRGIQ EEQVVPARYR QEFLTIAWEE VHLRSIFPFQ YFSIGASLIP
FIEHNDANRA LMSSNMQRQA VPLSRSEKCI VGTGLERQVA LDSGVPAIAE HEGKILYTDT
EKIILSGNEN TLSIPLIMYQ RSNKNTCMHQ KPQVPRGKCI KKGQILADGA ATVGGELALG
KNVLVAYMPW EGYNFEDAVL ISECLVYGDI YTSFHIRKYE IQTHVTTQGP ERITKEIPHL
EGRLLRNLDK NGIVMLGSWV ETGDILVGKL TPQVAKESSY APEDRLLRAI LGIQVSTSKE
TCLKLPIGGR GRVIDVRWVQ KKGGSSYNPE IIRVYISQKR EIKVGDKVAG RHGNKGIISK
ILPRQDMPYL QDGRPVDMVF NPLGVPSRMN VGQIFECSLG LAGSLLDRHY RIAPFDERYE
QEASRKLVFS ELYEASKQTA NPWVFEPEYP GKSRIFDGRT GDPFEQPVII GKPYILKLIH
QVDDKIHGRS SGHYALVTQQ PLRGRSKQGG QRVGEMEVWA LEGFGVAHIL QEMLTYKSDH
IRARQEVLGT TIIGGTIPKP EDAPESFRLL VRELRSLALE LNHFLVSEKN FQINRKEV
