ID   RPOB_FRATM              Reviewed;        1358 AA.
AC   B2SFD6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-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=FTM_0209;
OS   Francisella tularensis subsp. mediasiatica (strain FSC147).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=441952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSC147;
RX   PubMed=19521508; DOI=10.1371/journal.ppat.1000472;
RA   Larsson P., Elfsmark D., Svensson K., Wikstroem P., Forsman M., Brettin T.,
RA   Keim P., Johansson A.;
RT   "Molecular evolutionary consequences of niche restriction in Francisella
RT   tularensis, a facultative intracellular pathogen.";
RL   PLoS Pathog. 5:E1000472-E1000472(2009).
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; CP000915; ACD30289.1; -; Genomic_DNA.
DR   RefSeq; WP_012429130.1; NC_010677.1.
DR   AlphaFoldDB; B2SFD6; -.
DR   SMR; B2SFD6; -.
DR   PRIDE; B2SFD6; -.
DR   KEGG; ftm:FTM_0209; -.
DR   HOGENOM; CLU_000524_4_1_6; -.
DR   OMA; FMTWEGY; -.
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; -; 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; 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..1358
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_1000141698"
SQ   SEQUENCE   1358 AA;  151268 MW;  576D9205E1DE2266 CRC64;
     MSYSYAEKKR IRKEFGVLPH ILDVPYLLSI QTESYKKFLT ADAAKGRLHS GLEIVLKQSF
     PVESKNGQYE LHYVDYQIGE PTFDETECQV RGATYDAPLN VKLRLVVYNK DALPNEKIVE
     DIREEYVYMG DIPLMTTNGT FIINGTERVV VSQLHRSPGV FFSKDDSEEG AFSARIIPYR
     GSWLDFEFDS KGIIWARIDR KRKFCATVIL KALGYTQEQI LENFSESKTI TSNSKGFALR
     LDSLSNMKGE LLKFDIVDAQ DYVIVKKNKK LTSRDVKKIK DAGVDSVAID FDLVSTLRVA
     KDIVNEATGE VIAYANDDVT ESLLESCVEV GLLELEVIDF ITTERGRYIS DTLKYDLTRN
     TDEALVEIYK VLRPGDPPAA ASVKALFEGL FFIESRYSLS DIGRMKLNAR LGSDKVSKDI
     YTLENSDIVG VIEELINIRD GKGKVDDIDH LGNRRVRSVG EMVENQFRIG LYRVEKGIRE
     SMSLVHKDKL MPKDIVNSKP ITAAIKEFFT SGALSQFMDQ DNPLSEVTHK RRISALGPGG
     LSRDRAGFEV RDVHATHYGR LCPIETPEGP NIGLINSLAS YARVNDYGFL EAPYRKVVDG
     KVTDEIEYLS AIDEDNYVIA QASTKLDENN YFVEDLIQCR SGGEAIFTES SRVQYMDVSA
     KQMVSAAAAL IPFLEHDDAN RVLMGANMQR QAVPTLKSEK PLVGTGMEKI VARDSGNCII
     ARNAGEVAEV DSNRIVIKVD TEKSQTSNLV DIYSLTKFKR SNKNTCINQR PIVNVGDKVE
     AGDILADGFA ADFGELSLGH NLMVAFMPWN GYNFEDSILL SERIVKDDKY TSIHIEEFTC
     VARDTKLGPE EITADIPNVS ESSLAKLDES GIVHIGANVE AGDILVAKIT PKAEQQLTPE
     ERLLRAIFNE KASNVADSSL RMPSGTSGTV INVQVFENDK GGKSKRALKI EKELIDKARK
     DFDEEFAVIE SVVKSSIEQE VVGAKIQKAK GLKKGAILTK EFLATLPFSK WLEISFEDEK
     LEEKVQNARE YYEEAKIAID AKFEAKKKSI TQSNELSPGV LKTVKVFVAI KKRIQPGDKM
     AGRHGNKGVV SRVLPVEDMP YMEDGTPVDV CLNPLGIPSR MNIGQILEAH LGLASYGLGK
     KIEKTLEKTR KAAELRKTLE EIYNSVGDKK VNLEALNDEE ILTLCDNLKG GVPIATPVFD
     GAKEEDIKSL LKIGGFATNG QMKLFDGRTG KPFDRHVTVG YMYMLKLDHL VDDKMHARST
     GSYSLVTQQP LGGKAQFGGQ RFGEMEVWAL QAYGAAYTLR EMLTVKSDDI AGRSKMYKNI
     VDGKLTMNVD VPESFNVLRN EVRALGIDMD FDYSSEEE