ID   RPOB_WOLPI              Reviewed;        1436 AA.
AC   Q93MK7;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 79.
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   Wolbachia pipientis.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia.
OX   NCBI_TaxID=955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=O'Neill;
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}.
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DR   EMBL; AF401090; AAK83926.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q93MK7; -.
DR   SMR; Q93MK7; -.
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; 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..1436
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000047997"
SQ   SEQUENCE   1436 AA;  161619 MW;  FD371036E3EAF22F CRC64;
     MSSAGDSGPG YVLNDFDAVP RGTRGRRPGL VKDSLLDLVK VQKGSYNSFT PNNESNERLE
     AIFHTIFPIS DPLHRATIEF LNCRVDDLKY SESECIKRGI TFSAQVIASI RLVIMQDGVS
     LEKYQEIKEY DDHSKLATVI KSAEEQEVRF CELPMMTDKG TFIINGVEKV IVSQMHRSPG
     VFFDSDKGKT YNSGKLIYSA RVIPYRGSWL DIEFDVKDHL YFRIDRKRKL PISVLLKALG
     LSNNDILNKF MKNRVYKHKS GWKVPFFPDK FKGVRLPFDL KNVEGNVLLK ANVRITSKLA
     KNLYDNGLKE YLIPYDSICG LFLAEDLIDS ASSTKILSAG ESIKLEDIKK LELLSIDKIS
     VLNIDNVSVG PYILNTLFLD ENMSYENALY EIYKVLRPGE VPVLKIVEEF FRNLFFSPEY
     YDLSNIGRLK LNSCLGLNYE ENLTTLTHED IIEIIRKIVL LRDGQGSVDD DIDHLANRRV
     RSVGEFIENQ FRTGLLKLGR AVVDSMSTSS LDKVSPSDFI NPKVLTNVLR DFFNSSQLSQ
     FMDQTNPLSE ITHKRRLSAL GPGGLTRERA GFEVRDVHPT HYGRICPIET PEQNIAYNSL
     AIYARINKYG FIESPYRKVV NKVVTDQIEY LSAIDEGLYY IADTSAKLDE NNCFVDDMLY
     CRYAGTFVMV NSNQVSYIDL SPKQVISVAA SLIPFLENDD ANRALMGSNM QRQAVPLLKP
     TAPLVATGME SFVASGSGAV VLAKRGGIVD SSDSNSIVIR AFDKGGINYL DVDIYHLRKF
     QRSNHNTCIN QKPLVHVGDC VKEGDVIADG PAINNGELAL GQNLLVAFMS WQGYNFEDSI
     IISSEVVKKD LFTSIHIEEF ECVVHDTPLG SEKITRAIPG VNEENLYHLD DSGIVKVGTR
     VGPGYILVGK VTPRHSLSLP PETKLLMTIF GEKSFDCVDS SLYTSPDIEG IVIDVQVFTR
     RGEEENERAF LIKQKEANDF EKERDHIINV INQYFYDELR KILINSGSQD RESINFIERE
     GWWDIGLKNQ SISKQVESLK KDFDEKVSHA ITNFKRKVEK LHEGYDLPQG VSMSVKVFIA
     VKHSLQPGDK MAGRHGNKGV ISRVVPVEDM PYLEDGTPID IILNPLGVPS RMNVGQMLET
     HVGWACKKLG EKVGNILDEI NKIKRAFCEA IRSLSDDDFE KFAALYLDNK KFEDINDDEI
     TASILDTPNK DELNNELTTL VENYFNSCKD AHSSLRHFLI EVYSCGSNLS ICNNIRDIND
     NHLIEFAYKL RDGIPVTAPV FEGPKDEQIV KLFELAGLDN SGQVVLYDGC SGEKFDRKVT
     VGYMYMLKLH HLVDGKIHAR SVGPYSLVTQ QPLGGKSHFG GQRFGEMECW ALQAYGAAYT
     LQEMLTVKSD DINGRVKIYE SVIKGDSNFE CGIPESFNVM IKELRSLCFN VDLNAK