ID   RPOB_PHYMT              Reviewed;        1273 AA.
AC   B3QZH0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=ATP_00390;
OS   Phytoplasma mali (strain AT).
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC   Candidatus Phytoplasma; 16SrX (Apple proliferation group).
OX   NCBI_TaxID=482235;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AT;
RX   PubMed=18582369; DOI=10.1186/1471-2164-9-306;
RA   Kube M., Schneider B., Kuhl H., Dandekar T., Heitmann K., Migdoll A.M.,
RA   Reinhardt R., Seemueller E.;
RT   "The linear chromosome of the plant-pathogenic mycoplasma 'Candidatus
RT   Phytoplasma mali'.";
RL   BMC Genomics 9:306-306(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; CU469464; CAP18577.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3QZH0; -.
DR   SMR; B3QZH0; -.
DR   STRING; 37692.ATP_00390; -.
DR   EnsemblBacteria; CAP18577; CAP18577; ATP_00390.
DR   KEGG; pml:ATP_00390; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_3_14; -.
DR   OMA; FMTWEGY; -.
DR   BRENDA; 2.7.7.6; 14242.
DR   Proteomes; UP000002020; 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; 2.30.150.10; -; 1.
DR   Gene3D; 2.40.270.10; -; 3.
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; 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   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..1273
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_1000165815"
SQ   SEQUENCE   1273 AA;  144954 MW;  35E644676977E568 CRC64;
     MEYRNIKYGT KTERRNYSKM NYDIELPNLI EIQTKSFELF LKEGIKKILK DISPIESNNG
     DLKLYFDDFY LDKPKYNIEE AKNRDITYYA QLFAKARLEN VLTKEIKESN ILITELPLIT
     PSGTFIINGT ERVVISQIVR SSGIYFTKKF DSKIRYLAQL IPTRGAWIEY EQSNKDFLYA
     KLDRSKKIPL NKFICCLGFD TKEKIESTFG YNKFLDLSLK KDQILNINEA IIELHSKLHR
     GEKVPVDVAR EFIFSKLFYA KKYDLLAVGR YKFNQKLDVL KRIKNTYLAK DLIDPETNEI
     FLSKKTFLNE EIIEKLKNKR NCFTFELVNA DNNLENEINE EILTYANYNK DKILELYIKD
     NIINIKTGEI LVEKDTLITE QVMNIIRKNG QFIHDKVSKY FLCNKDLYQK HKERKGVFNE
     VLEVYILDNL GNPKPTIKVI GNIQSENNKQ HITVSDIIAS ISYYLNLYED IGKTDDIDHL
     GNRRLRLIGE LLTNQFRLGL IISEKNIKDK MSISKFNNIT VNSLVNFTSL SAIIKTFFNS
     SRLSHFMDQI NPLAELTQKR RVSALGTGGI DRDRAGIEIR DINNSHYAKL CPIETPEGPS
     IGLIASLSTY ARVDKYCFIQ TPYLKVIKNE QGQPKVSEHI DYLTADQEEK EVIASVTYLN
     SDNTFKEKKI IARKNGETGL HEIDKITYID VSPKQIVSVA TSSIPFLEHN DASRALMGAN
     MQRQAVPLLI PESPIVGTGI EHRIAKDSGC LILAKNSGYV TYADAQKIVI TEKPKKTITI
     NNEVIYKNEE EFNYEKAKIL HKKNVFSCQT EYKLINFAKS NQDTLILQKP LVLDGDFVNK
     NDIITDGPAT HKEELALGRN VTVAFMTWEG YNYEDAIIIS EDLVKNDIYT SVHIDKYEIQ
     TRELKKGAGV EQITREVPNV SAEAIKNLDE RGIIIPGSEV KEGDILVGKI TSQGMVEQTA
     YERLINVIIG EKSREHKDSS LRVPCGEGGI VQSVKYFSKE NNDILPPEVN ENIRVYIAKK
     RKIKEGDKIA GRHGNKGVIS LILPKEDLPY MKDGTTIDII LNPLGVPSRM NIGQILEMHL
     GIAAQKLNIK VATPVFDGVN NDDLRKIIKE AKLSLDGKMT LYDGRTGEPF DSSISVGVMY
     MIKLSHMVED KLHSRNIGPY TLMAQQPMGG RNQNGGQRFG EMEVWSLYAY GAANSLQEIL
     TIKSDDIIGR QKTYSAITNG LPLPKPSIPE SFRVFAKELQ ALGLYVELIN SKTKENEILK
     SLVENQKKGS NNR