ID   RPOB_PHYAS              Reviewed;        1240 AA.
AC   B1VAM6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, 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            Short=RNAP subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01321};
DE   AltName: Full=RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE   AltName: Full=Transcriptase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
GN   Name=rpoB {ECO:0000255|HAMAP-Rule:MF_01321}; OrderedLocusNames=PA0665;
OS   Phytoplasma australiense.
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC   Candidatus Phytoplasma; 16SrXII (Stolbur group).
OX   NCBI_TaxID=59748;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18359806; DOI=10.1128/jb.01301-07;
RA   Tran-Nguyen L.T., Kube M., Schneider B., Reinhardt R., Gibb K.S.;
RT   "Comparative genome analysis of 'Candidatus Phytoplasma australiense'
RT   (subgroup tuf-Australia I; rp-A) and 'Ca. Phytoplasma asteris' strains OY-M
RT   and AY-WB.";
RL   J. Bacteriol. 190:3979-3991(2008).
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: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta'
CC       and 1 omega subunit. When a sigma factor is associated with the core
CC       the holoenzyme is formed, which can initiate transcription.
CC       {ECO:0000255|HAMAP-Rule:MF_01321}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_01321}.
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DR   EMBL; AM422018; CAM11999.1; -; Genomic_DNA.
DR   RefSeq; WP_012359127.1; NC_010544.1.
DR   AlphaFoldDB; B1VAM6; -.
DR   SMR; B1VAM6; -.
DR   STRING; 59748.PA0665; -.
DR   PRIDE; B1VAM6; -.
DR   EnsemblBacteria; CAM11999; CAM11999; PA0665.
DR   KEGG; pal:PA0665; -.
DR   eggNOG; COG0085; Bacteria.
DR   OMA; FMTWEGY; -.
DR   BRENDA; 2.7.7.6; 28560.
DR   Proteomes; UP000008323; Chromosome.
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; 2.40.270.10; -; 3.
DR   Gene3D; 3.90.1110.10; -; 1.
DR   HAMAP; MF_01321; RNApol_bact_RpoB; 1.
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   PANTHER; PTHR20856; PTHR20856; 1.
DR   Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR   Pfam; PF04561; RNA_pol_Rpb2_2; 2.
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   DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome;
KW   Transcription; Transferase.
FT   CHAIN           1..1240
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_1000141717"
SQ   SEQUENCE   1240 AA;  140223 MW;  9B9C48132A0058D0 CRC64;
     MAYRNVKYGK KVERRNYSKI IYDVDLPNLI EIQNKSFNWF LKDGIEELLQ DFCPIESYNG
     DLKIYFGECY STGPKYSVEE SKTKDASYVI QLFVKATLEN TLTGETKKSS VLLTELPLIT
     DTGTFIINGK ERVAVSQIVR SSSVYYSSTF DVKLNKNLYS GQVIPARGAW IEYEEGSKEI
     LYVKLDRSKK IPLSNFIYAL GFNNREIIEK VFGKSPLLNS SFVKEEDMDT GNALIELYSK
     IRQGEKVPVD TARDFIRKRL FDQKKYDLTT VGRYKFNKKL DVLARAEKTY LVHDFVNLET
     KEIILPKHTF LTKDKIEILR KNRHFLLQEL FDAQHNLENE TDEEILTYKK DPQSRELYIK
     TNILNFRTGE IIFPKDTLVT DEVIKRLRKS IQLLDGKVIE FFLRSKDVYQ KDLERTGVFN
     EILEVYLSKD EHDNLQHKVQ IVGNNQKETK KHITLSDIIA SISYYLNLYE GIGNVDDIDH
     LGNRRLRLIG ELLKNQFRIG LTRAEKHIKD MISVSKFSEV GPGELVNFGF LNGVIKTFFA
     NSRLSQFMDQ INPLAELTQK RRVSALGVGG INRDRAGVEV RDVHNSHYGR LCPIETPEGP
     SIGLIASLAI YAKVDDYGFI QTPFFKVFVQ NGASYVSNQI EYLTADQEKE EIIASSGYEL
     NSDATFQKDK VIARKNGEIG IYPKEQVTYA DISPKQIVSI ATASIPFLEH NDSSRALMGS
     NMQRQAVPLL VTESPIVGTG IEYRAAKDSG SLIIASQPGI VTYVDAKKIV TSDQEGNKKE
     YQLTTFEKSN QDTLILQKPI VSLGDNIQKG DILVDGPSTN QGELALGRNI LVAFMTWEGY
     NYEDAIIISE ELVKNDVYTS VHINKYSVQT RELKKGSGKE EITREVPNVG ADAIKNLDER
     GIIIPGSEVK EGDILVGKIT PQGNVDPTPQ EKLIQIVIGE KAREYKDSSL RVPYGEGGIV
     QSVQYFSRKN GDILPPGVNE NIRVFIAKKR KISEGDKMAG RHGNKGVISR ILPKEDLPFM
     EDGTTIDVML NPLGVPSRMN IGQILEIHLG MSAKNLNIKV ATPVFDGVND QDLKEISQEA
     NLELDGKKVL YDGRTGEPYE NRISVGVMYM IKLSHMVDDK LHARNVGPYT LVTQQPMRGK
     IREGGQRYGE MENWAVHAHG AAYTLQEFLT IKSDDIIGRN QTYSAIVQGK QLPKPNIPES
     FRVLIKELQA LGLYVELIKT DTKENEVNKS LIDYKKEGYN