ID   RPOB_XANAC              Reviewed;        1383 AA.
AC   Q8PNT0;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 111.
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=XAC0965;
OS   Xanthomonas axonopodis pv. citri (strain 306).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190486;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=306;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
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; AE008923; AAM35848.1; -; Genomic_DNA.
DR   RefSeq; WP_003486738.1; NC_003919.1.
DR   AlphaFoldDB; Q8PNT0; -.
DR   SMR; Q8PNT0; -.
DR   STRING; 190486.XAC0965; -.
DR   EnsemblBacteria; AAM35848; AAM35848; XAC0965.
DR   GeneID; 66910151; -.
DR   KEGG; xac:XAC0965; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_3_6; -.
DR   OMA; FMTWEGY; -.
DR   Proteomes; UP000000576; 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; -; 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; 3.
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..1383
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000047998"
SQ   SEQUENCE   1383 AA;  154198 MW;  448B3DB75AA5955A CRC64;
     MTSYSFTEKK RIRKDFGKQR SILEVPFLLA IQVDSYREFL QEDVEPNKRK DLGLHAALKS
     VFPISSYSGN AALEYVGYKL GQPVFDEREC RQRGMSYGAP LRVTVRLVIY DRESSTKAIK
     YVKEQEVYLG EIPLMTGNGT FIVNGTERVI VSQLHRSPGV FFDHDRGKTH SSGKLLYSAR
     IIPYRGSWLD FEFDPKDALF TRIDRRRKLP VSILLRALGY SNEEMLAEFF EINTFHINPD
     EGVQLELVPE RLRGETLNFD LADGDKVIVE AGKRITARHV KQLEAAGVAA LAVPDDYLVG
     RILSHDVVDG STGELLANAN DEINEDQLAA FRKAGVDAVG TLWVNDLDRG PYLSNTLRID
     PTKTQLEALV EIYRMMRPGE PPTKEAAQNL FHNLFFTFER YDLSTVGRMK FNRRVGRKDV
     LGESVLYDKK YFAERNDEES KRLVAEHADT SDILEVIKVL TEIRNGRGVV DDIDHLGNRR
     VRSVGEMAEN VFRVGLVRVE RAVKERLSMA ESEGLTPQEL INAKPVAAAI KEFFGSSQLS
     QFMDQNNPLS EVTHKRRVSA LGPGGLTRER AGFEVRDVHP THYGRVCTIE TPEGPNIGLI
     NSLAVFARTN QYGFLETPYR KVLDGKVSDD VEYLSAIEEN EYVIAQANAL TDAKNMLTEQ
     FVPCRFQGES LLKPPSEVHF MDVSPMQTVS VAAALVPFLE HDDANRALMG ANMQRQAVPT
     LRSQKPLVGT GIERAVARDS GVTVNALRGG VIEQIDAARI VVKVNEAEIG GGTDAGVDIY
     NLIKYTRSNQ NTCINQRPLV NVGDVIARGD VLADGPSTDI GELALGQNML IAFMPWNGYN
     FEDSILLSER VVEEDRYTTI HIEELTCVAR DTKLGPEEIS ADIPNVSEQA LNRLDESGVV
     YIGAEVRAGD IMVGKVTPKG ESQLTPEEKL LRAIFGEKAS DVKDSSLRVP PGMDGTVIDV
     QVFTRDGIEK DKRARQIEES EIKRVKKDFD DQFRILEAAI YARLRSQIVG KVANGGANLK
     KGDTVTDAYL DGLKKSDWFQ LRMKDEDAAD AIERAQKQIQ AHEKEFEARF ADKRGKITQG
     DDLAPGVLKM VKVFLAVKRR IQPGDKMAGR HGNKGVVSNV VPVEDMPYMA TGESVDIVLN
     PLGVPSRMNI GQILEVHLGW AAKGLGRKIQ RMLEAQAAVS ELRKFLNDIY NHDNAINAQR
     VDLSQFSDEE LLNLGKNLID GVPMATPVFD GASEAEIKRM LELADLPQSG QTQLYDGRTG
     EAFDRKTTVG YMHYLKLNHL VDDKMHARST GPYSLVTQQP LGGKAQFGGQ RFGEMEVWAL
     EAYGAAYTLQ EMLTVKSDDV QGRNQMYKNI VDGEHEMVAG MPESFNVLVK EIRSLAINME
     LEE