RPOB_RHDSA
ID RPOB_RHDSA Reviewed; 1097 AA.
AC A6MVX4;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 58.
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 Rhodomonas salina (Cryptomonas salina).
OG Plastid; Chloroplast.
OC Eukaryota; Cryptophyceae; Pyrenomonadales; Pyrenomonadaceae; Rhodomonas.
OX NCBI_TaxID=52970;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1319 / NEPCC76 / CS-174;
RX PubMed=17522086; DOI=10.1093/molbev/msm101;
RA Khan H., Parks N., Kozera C., Curtis B.A., Parsons B.J., Bowman S.,
RA Archibald J.M.;
RT "Plastid genome sequence of the cryptophyte alga Rhodomonas salina
RT CCMP1319: lateral transfer of putative DNA replication machinery and a test
RT of chromist plastid phylogeny.";
RL Mol. Biol. Evol. 24:1832-1842(2007).
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; EF508371; ABO70811.1; -; Genomic_DNA.
DR RefSeq; YP_001293553.1; NC_009573.1.
DR AlphaFoldDB; A6MVX4; -.
DR SMR; A6MVX4; -.
DR GeneID; 5228507; -.
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..1097
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300457"
SQ SEQUENCE 1097 AA; 123025 MW; 2B235B393DC8647F CRC64;
MSSTKLSTSI LPDLVEIQRA SFCWFLEEGL AEEIKSFSPI TDYTGNLELH FFGDQFKLKC
PKYNLLESKR RDATYSVQVY VPARLINRDT GIIKEQEVFI GDLPLMTDRG TFIINGAERV
IVNQIVRSPG IYYKSETDRQ GRRTYSGSLI SNRGAWVKFE TDRNDLVWVR IDKTRKIPAH
VFLKAMGLSD SDIYNGLRHP EYLKKSFRVE GNYTTEEALI QMYTKLRPGE PATVNGGQQI
LYSRFFDPKR YDLGKVGRYK INKKLALSIP ENIKVLTPQD TLSAIDYLIN LKFNIGETDD
IDHLGNRRVR SVGELLQNQV RVGLNRLERI IRERMTICDS ESLAPNTLVN PKPIIAAIRE
FFGSSQLSQF MDQTNPLAEL THKRRISALG PGGLNRDRAG FAVRDIHPSH YGRICPIETP
EGPNAGLIGV LATHARINSY GFIETPFYQV INGKVVSDGN PVYLTADQED NFRIAPGDIA
IDENNAINND IVPVRYRQEF TITKPEQIDY IQVSPIQVIS IATSLIPFLE HDDANRALMG
SNMQRQAVPL LYPESPLIGT GIEAQAARDS GMVVVSYQDG RVTYVSANKI CITDDEGKEV
VYYLQKYQRS NQDTCINQRP SVWLGEKVVA GQVIADGAAT EGGELALGQN ILIAYLPWEG
YNYEDAFLIS ERLVYNDVYT SVHIEKYEIE ARQTKLGSEE ITRELPNIGE YSLRKLDDNG
IIVIGSWVEV GDILVGKVTP KGESDQPPEG KLLRAIFGEK ARDVRDTSLR VPNGGRGRVL
DVRIFTREKG DELPTGANIV IRVYVAQTRK IQVGDKMAGR HGNKGIISRI LPRQDMPYLP
DGTPVDLVLN PLGVPSRMNV GQIFECLLGL AAENLDKRFK IIPFDEMNGA EASRVLVNEK
LMEARTLTEK DWIFDLRHPG KTQLFDGRTG EAFDNPVTVG ISYMLKLVHL VDDKIHARST
GPYSLVTQQP LGGKAQHGGQ RLGEMEVWAL EAFGASYTLQ ELLTVKSDDM QGRNETLNAI
VKGKPIPRPG TPESFKVLMR ELQSLGLDIG AYKIENLPDG QTRGIEVDLM SNLHNRRVPS
RPTYESITRE DLENSFA