RPOB_LYSSC
ID RPOB_LYSSC Reviewed; 1191 AA.
AC B1HMZ6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=Bsph_4630;
OS Lysinibacillus sphaericus (strain C3-41).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=444177;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C3-41;
RX PubMed=18296527; DOI=10.1128/jb.01652-07;
RA Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M.,
RA Berry C., Yuan Z.;
RT "Complete genome sequence of the mosquitocidal bacterium Bacillus
RT sphaericus C3-41 and comparison with those of closely related Bacillus
RT species.";
RL J. Bacteriol. 190:2892-2902(2008).
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; CP000817; ACA42074.1; -; Genomic_DNA.
DR AlphaFoldDB; B1HMZ6; -.
DR SMR; B1HMZ6; -.
DR PRIDE; B1HMZ6; -.
DR EnsemblBacteria; ACA42074; ACA42074; Bsph_4630.
DR KEGG; lsp:Bsph_4630; -.
DR HOGENOM; CLU_000524_4_1_9; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000002164; 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; 2.40.270.10; -; 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..1191
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000141708"
FT REGION 1164..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1191 AA; 133879 MW; DC807F566F7C6CB9 CRC64;
MNELTGQLVQ YGQHRQRRSF ARIKEVLELP NLIEIQTASY EWFLEEGLRE MFRDISPIED
FTGNLSLEFI DYSLGDPKYD VDECKERDVT YAAPLRVKVR LYNKETDEVK EQDVFMGDFP
LMTETGTFII NGAERVIVSQ LVRSPSVYFH DKTDKNGKKG FGATVIPNRG AWLEYETDAK
DVVYVRIDRT RKLPVTVLLR ALGFGSDQEI IDIIGDNEYL RNTLEKDNSE STEKALLEIY
ERLRPGEPPT VESAKSLLYS RFFDAKRYDL ANVGRYKMNK KLHIKNRLFN QTIAETLVDP
ETGEILVEKG TVLDRRTLDK ILPYLEDSSK GIGFRTLSQV GGVLEDDVTI QSIKIYAPKD
EAQKEINIIS NAYIDEEVKN ITPADVLSSV SYFFNLLYQV GATDDIDHLG NRRLRSVGEL
LQNQFRIGLS RMERVVRERM SINDTAAIVP QQLINIRPVI ASIKEFFGSS QLSQFMDQTN
PLAELTHKRR LSALGPGGLT RERAGFEVRD VHYSHYGRMC PIETPEGPNI GLINSLSSFA
KVNKFGFIET PYRRIDHETG QVTDQIDYLT ADEEDNYYVA QANSPLNPDG SFANDEVVGR
FRGDNTVFNK AQMDYMDVSP KQVVSAATAC IPFLENDDSN RALMGANMQR QAVPLLNPEA
PFVGTGMEHV DARDSGAAVV AKYDGIVEHV EARSIHVRRI EVVDGKEVKG DLTKYKLQKF
IRSNQGTSYN QRPLVKVGER VKPRDILADG PSMEKGELAL GRNVLVAFMT WNGFNYEDAV
IMSERLVKDD VYTSVHIEEY ESESRDTKLG PEEITRDIPN VGEDALRNLD ERGIIRIGAE
VRDGDILVGK VTPKGVTELT AEERLLHAIF GEKAREVRDT SLRVPHGAGG IILDVKVFNR
EDGDELPPGV NQLVRAYIVQ KRKIRVGDKM AGRHGNKGVI SRILPEEDMP FMPDGTPVDI
MLNPLGVPSR MNIGQVLELH LGMASRYLGV HMATPVFDGA NEEDVWETME EAGMNRDGKT
ILYDGRSGEP FDNRVSVGIM YMIKLAHMVD DKLHARSTGP YSLVTQQPLG GKAQFGGQRF
GEMEVWALEA YGAAYTLQEI LTVKSDDVVG RVKTYEAIVK GESVPEPGVP ESFKVLIKEL
QSLGMDVKML TVNDEEVELR DLDEEEDLQP ADALNIAPQP DTEEEPVESF E