RPOB_FRATO
ID RPOB_FRATO Reviewed; 1358 AA.
AC Q0BKC5;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=FTH_1683;
OS Francisella tularensis subsp. holarctica (strain OSU18).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=393011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OSU18;
RX PubMed=16980500; DOI=10.1128/jb.00506-06;
RA Petrosino J.F., Xiang Q., Karpathy S.E., Jiang H., Yerrapragada S., Liu Y.,
RA Gioia J., Hemphill L., Gonzalez A., Raghavan T.M., Uzman A., Fox G.E.,
RA Highlander S., Reichard M., Morton R.J., Clinkenbeard K.D., Weinstock G.M.;
RT "Chromosome rearrangement and diversification of Francisella tularensis
RT revealed by the type B (OSU18) genome sequence.";
RL J. Bacteriol. 188:6977-6985(2006).
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; CP000437; ABI83459.1; -; Genomic_DNA.
DR RefSeq; WP_011648780.1; NC_017463.1.
DR AlphaFoldDB; Q0BKC5; -.
DR SMR; Q0BKC5; -.
DR KEGG; fth:FTH_1683; -.
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; 2.30.150.10; -; 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..1358
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300316"
SQ SEQUENCE 1358 AA; 151365 MW; 80E448BCDA995D13 CRC64;
MSYSYAEKKR IRKEFGVLPH ILDVPYLLSI QTESYKKFLT VDAAKGRLHS GLEIVLKQSF
PVESKNGQYE LHYVDYQIGE PTFDETECQV RGATYDAPLN VKLRLVVYNK DALPNEKIVE
DIREEYVYMG DIPLMTTNGT FIINGTERVV VSQLHRSPGV FFSKDDSEEG AFSARIIPYR
GSWLDFEFDS KGIIWARIDR KRKFCATVIL KALGYTQEQI LENFSESKTI TFNSKGFALR
LDNLSNMKGE LLKFDIVDAQ DNVIVKKNKK LTSRDVKKIK DAGVDSVAID FDLVSTLRVA
KDIVNEATGE VIAYANDDVT ESLLESCVEV GMLELEVIDF 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 HFVEDIIQCR SGGEAIFTES SRVQYMDVSA
KQMVSAAAAL IPFLEHDDAN RVLMGANMQR QAVPTLKSEK PLVGTGMEKI VARDSGNCII
ARNVGEVAEV DSNRIVIKVD TEKSQTSNLV DIYSLTKFKR SNKNTCINQR PIVNVGDKVE
AGDILADGFA TDFGELSLGH NLMVAFMPWN GYNFEDSILL SERIVKDDKY TSIHIEEFTC
VARDTKLGPE EITADIPNVS ESSLAKLDES GIVHIGANVE AGDILVAKIT PKAEQQLTPE
ERLLRAIFNE KASNVVDSSL RMPSGTSGTV INVQVFENDK GGKSKRALKI EKELIDKARK
DFDEEFAVIE SVVKSSIEQE VVGAKIQKAK GLKKGAILTK EFLATLPLSK WLEISFEDEK
LEEKVQNARE YYEEAKIAID AKFEAKKKSI TQSNELSPGV LKTVKVFVAI KKRIQPGDKM
AGRHGNKGVV SRVLPVEDMP YMEDGTPVDV CLNPLGIPSR MNIGQILEAH LGLASYGLGK
KIEKTLEKTR KAAELRKTLE EVYNSVGDKK VNLEALNDEE ILTLCDNLKG GVPIATPVFD
GAKEEDIKSL LKIGGFATNG QMKLFDGRTG KPFDRHVTVG YMYMLKLDHL VDDKMHARST
GSYSLVTQQP LGGKAQFGGQ RFGEMEVWAL QAYGAAYTLR EMLTVKSDDI AGRSKMYKNI
VDGKLTMNVD VPESFNVLRN EVRALGIDMD FDYSSEEE
