ID   RPOB_ANAPH              Reviewed;        1394 AA.
AC   Q9AIU3;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 78.
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};
OS   Anaplasma phagocytophilum (Ehrlichia phagocytophila).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma; phagocytophilum group.
OX   NCBI_TaxID=948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Webster;
RX   PubMed=12710612; DOI=10.1099/ijs.0.02411-0;
RA   Taillardat-Bisch A.V., Raoult D., Drancourt M.;
RT   "RNA polymerase beta-subunit-based phylogeny of Ehrlichia spp., Anaplasma
RT   spp., Neorickettsia spp. and Wolbachia pipientis.";
RL   Int. J. Syst. Evol. Microbiol. 53:455-458(2003).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF237414; AAK15035.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9AIU3; -.
DR   SMR; Q9AIU3; -.
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; -; 2.
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; 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; Transcription;
KW   Transferase.
FT   CHAIN           1..1394
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000047853"
SQ   SEQUENCE   1394 AA;  155830 MW;  3460DB839D659804 CRC64;
     MVFGELMSSA GDSGPGYVLN DFDAVPRLSY ARSIDIRDSL SDLIRIQRDS YDAFIGIDEG
     SSGGIQSIFQ SMFPIRDPLG RAVLEFVSCN IGEPQYDEYE CIKRGITFSV PMRITLRFVV
     WKVQEVSFKE VKYVVDEGTL ERSVKYMKEQ EVSIGDLPMM TSYGTFIING IERVIVSQMH
     RSPGVFFDSD KGKTYSSGKL IYSARIIPYR GSWLDFEFDI KDIIYFRIDK KRKLPVTYLL
     KALGMSNNDI LDTFYDKVLY VRSDKGWKVP FVVDRFKGVR LSYDLMDVDG NVLIKANTRI
     TLRIAKKLYA DGLREYLVPF AGISGLFVAT DLVDPASGAV IVSAGEAIAA EHIVKLELFD
     ISEIAFLNID FLTVGPYVLN TLFLDRHITQ EDALFEIYRV LRSGESPNLE AVKSFFKGLF
     FEPDRYDLSV VGRIKLNSHL RLDIDENLTV LTKDDIVHVI KKLVLLRDGE GVVDDIDHLG
     NRRVRSVGEF IENQFRVGIL RLERMIMDYM SSVNFDNAVP CDFVNPKILA TVLKDFFSSS
     QLSQFMDQTN PLSEVTHKRR LSALGPGGLT RERAGFEVRD VHPTHYGRIC PIETPEGQNI
     GLISSLAIYA KINKYGFIES PYRKVIDGVV TDSVEYLLAT QESDYYIADA GAALDENNRF
     VDDMLYCRHG GNFVMVKRED VNYIDVSPKQ IVSVAASLIP FLENNDANRA LMGSNMQRQA
     VPLLKAEAPL VGTGMESVVA AGSGAVVLAK RDGVLHRVDR VLYPVIRAFD KNKDSILVLI
     YTTEKVQRSN HNTCINQRPI VKIGDYVRTN DVIADGAAID RGELALGKNV LVAFMSWQGC
     NFEDSIVISS DVVKRDVFTS IHIEEFECVV RDTPLGPEKI MRSVPDVNEE SLSHLDDVGI
     VNIGAEVSAG SVLVGKVTPR PPVSLPPETK LLVTIFGEKV FDCVDSSLYL PPDVEGTVID
     VHVFVRRGVE ENDRSLLIKQ SEVNSFRKER DYEIDVVSEY FYDELKKLLC SADLPLNGHA
     DVESLLAAKS LEALWEIGLS NPKISAKVAD MKGKFDELIT EAHSKFDQKI DKLNYGYDLP
     QGVLTIVKVF VAVKHNLQPG DKMAGRHGNK GVISRIVPVE DMPHLEDGTP VDIILNSLGV
     PSRMNIGQIL ETHLGWAAVN LGHRVGRMLD SGEEEGPVVE RIRSFLSEVY EGQKLKEDVA
     SMSDEALLKF ANRLRRGVPM AAPVFEGPKD AQISRLLELA DVDPSGQVDL YDGRSGQKFD
     RKVTVGYIYM LKLHHLVDDK IHARSVGPYG LVTQQPLGGK SHFGGQRFGE MECWALQAYG
     AAYTLQEMLT VKSDDTSPGR RPRVPYSESY YIKGDSNFEC GIPESFNVMV KELRSLCLDV
     VLKHDKEFTS SNVE