RPOB_FRAT1
ID RPOB_FRAT1 Reviewed; 1358 AA.
AC Q14JT5;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=FTF0144;
OS Francisella tularensis subsp. tularensis (strain FSC 198).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=393115;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSC 198;
RX PubMed=17406676; DOI=10.1371/journal.pone.0000352;
RA Chaudhuri R.R., Ren C.-P., Desmond L., Vincent G.A., Silman N.J.,
RA Brehm J.K., Elmore M.J., Hudson M.J., Forsman M., Isherwood K.E.,
RA Gurycova D., Minton N.P., Titball R.W., Pallen M.J., Vipond R.;
RT "Genome sequencing shows that European isolates of Francisella tularensis
RT subspecies tularensis are almost identical to US laboratory strain Schu
RT S4.";
RL PLoS ONE 2:E352-E352(2007).
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; AM286280; CAL08160.1; -; Genomic_DNA.
DR RefSeq; WP_003019908.1; NC_008245.1.
DR AlphaFoldDB; Q14JT5; -.
DR SMR; Q14JT5; -.
DR KEGG; ftf:FTF0144; -.
DR HOGENOM; CLU_000524_4_3_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; 2.30.150.10; -; 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_0000300318"
SQ SEQUENCE 1358 AA; 151315 MW; 0F2A619B7BAC397F CRC64;
MSYSYAEKKR IRKEFGVLPH ILDVPYLLSI QTESYKKFLT ADAAKGRLHS 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 HFVEDLIQCR SGGEAIFTES SRVQYMDVSA
KQMVSAAAAL IPFLEHDDAN RVLMGANMQR QAVPTLKSEK PLVGTGMEKI VARDSGNCII
ARNAGEVAEV DSNRIVIKVD TEKSQTSNLV DIYSLTKFKR SNKNTCINQR PIVNVGDKVE
AGDILADGFA TDFGELSLGH 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 EVYNSVGDKK VNLEALNDEE ILTLCDNLKG GVPIATPVFD
GAKEEDIKSL LKIGGFATNG QMKLFDGRTG KPFDRHVTVG YMYMLKLDHL VDDKMHARST
GSYSLVTQQP LGGKAQFGGQ RFGEMEVWAL QAYGAAYTLR EMLTVKSDDI AGRSKMYKNI
VDGKLTMNVD VPESFNVLRN EVRALGIDMD FDYSSEEE
