RPOB_NEOYE
ID RPOB_NEOYE Reviewed; 1143 AA.
AC Q1XDN5;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 67.
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 Neopyropia yezoensis (Susabi-nori) (Pyropia yezoensis).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Neopyropia.
OX NCBI_TaxID=2788;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U-51;
RA Kunimoto M., Morishima K., Yoshikawa M., Fukuda S., Kobayashi T.,
RA Kobayashi M., Okazaki T., Ohara I., Nakayama I.;
RT "Whole genome sequence of Porphyra yezoensis chloroplast.";
RL Submitted (NOV-2003) 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; AP006715; BAE92376.1; -; Genomic_DNA.
DR RefSeq; YP_536933.1; NC_007932.1.
DR AlphaFoldDB; Q1XDN5; -.
DR SMR; Q1XDN5; -.
DR GeneID; 3978929; -.
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..1143
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000237328"
SQ SEQUENCE 1143 AA; 128775 MW; C83C9F7ECA68AA84 CRC64;
MVQRISLKNK LLPDLVEIQR ASFKWFLLEG LTEVLEIFPK ISDPTSRLEL QLFGNEYKIK
FPRYSVRQAK NRDKTYSAQI YVPAKLTRKD IDLPSKNQEK NIKSLDLSST HLQLSAEKQI
KNKKYKKRLV FIGDLPIMTN RGTFIVSGTE RVIINQIIRS PGIYYKQEID KNGKQIYSAS
LISNRGSWLK FEIDPKGEIW IRIDKTHKVN AYIFLRAIGL NKDEIEKGLS KYAFLISASQ
IYSVKELAKE IGKNNIEEVT DEEALLIVYS KLRPNEPATV AVAKQMLYSR FFDPKRYDLG
EVGRYKINKK LGLNIPKTFR VLSPQDILSS IDYLINIKDK NSGNLDDIDH LGNRRVRSVG
ELLQNQFRVG LNRLERIIRE RMMICDIDSL SLSNLINPKP LIASVREFFG SSQLSQFMDQ
TNPVAELTHK RRISALGPGG FNKDRAGFAV RDLHPSHYGR ICPIETPEGP NAGLIGSLAT
CARVNVFGFI ETPFYPVNQG QVIYHNSPVY LTADEEDDFR VAPGDVKVSK QHYIEGDIIP
VRYRQEFITT TPTQVDYIAI SPIQVISAAT SLIPFLEHDD ANRALMGSNM QRQAVPLLYP
EKPIIGTGLE TKIARDSGMV VISRTSGHVN YVSANKIGIQ DNSGRTVHYR LKKYYRSNQD
TCINQRPIVW VGEKIVVGQT LADGASTDGG EIALGRNILV AYMPWEGYNY EDAFLISERL
VYDDLYTSIH IEKYEVECRQ TKLGPEEITR EIPNVSDNSL KDLDRNGIVV GGSWVEAGDI
LVGKITPKGE ADQLPEGKLL RAIFGEKARD VRDTSLRLPN AAKGRVVKVR VFTRQKGDEL
PPGTNAMIRV YVAQKRKIQV GDKMAGRHGN KGIISRILPK QDMPYLSDGT PVDIVLNPLG
VPSRMNVGQV FECLLGLAGG YLGKRFKIIP FDEMYGAEAS RALVNRKLKE ASLITSNKWL
FNDQHPGKMQ VFDGRTGEPF DNPVTVGRAY MLKLVHLVDD KIHARSTGPY SLVTQQPLGG
RAQHGGQRLG EMEVWALEAF GAAYTLQELL TVKSDDMQAR NEALNAIVKG KPIPKPGTPE
SFKVLMRELQ SLGLDIAVHK LKLFEDGQRR TVEVDLMSDS KDNRVDRSNY DTPPVDDFEQ
FLY