RPOB_BACCQ
ID RPOB_BACCQ Reviewed; 1177 AA.
AC B9IZI6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, 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=BCQ_0115;
OS Bacillus cereus (strain Q1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=361100;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Q1;
RX PubMed=19060151; DOI=10.1128/jb.01629-08;
RA Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X.,
RA Xue Y., Zhu Y., Jin Q.;
RT "Complete genome sequence of the extremophilic Bacillus cereus strain Q1
RT with industrial applications.";
RL J. Bacteriol. 191:1120-1121(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; CP000227; ACM10630.1; -; Genomic_DNA.
DR RefSeq; WP_000147554.1; NC_011969.1.
DR AlphaFoldDB; B9IZI6; -.
DR SMR; B9IZI6; -.
DR EnsemblBacteria; ACM10630; ACM10630; BCQ_0115.
DR GeneID; 59159718; -.
DR GeneID; 64202511; -.
DR KEGG; bcq:BCQ_0115; -.
DR HOGENOM; CLU_000524_4_1_9; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000000441; 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; -; 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; 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..1177
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000165789"
FT REGION 1147..1177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1158..1177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1177 AA; 131893 MW; 09E58093161E230E CRC64;
MTGQLVQYGR HRQRRSYARI SEVLELPNLI EIQTSSYQWF LDEGLREMFQ DISPIEDFTG
NLSLEFIDYS LGEPKYSVDE CKERDVTYAA PLRVKVRLIN KETGEVKEQD VFMGDFPLMT
ETGTFVINGA ERVIVSQLVR SPSVYYSGKV DKNGKRGFTA TVIPNRGAWL EYETDAKDVV
YVRIDRTRKL PVTVLLRALG FGSDQEITEL LGDNEYLSNT LEKDNTDSTE KALLEIYERL
RPGEPPTVEN AKSLLVSRFF DPKRYDLANV GRYKINKKLH IKNRLFNQRL AETLVDPETG
EILAAEGTIL DRRTLDRILP YLEKNIGFKT AKPMGGVVEG DVELQSIKIY APESEGERVI
NVIGNANITR DVKHITPGDI LASISYFFNL LYKVGDTDDI DHLGNRRLRS VGELLQNQFR
IGLSRMERVV RERMSIQDTN AITPQALINI RPVIASIKEF FGSSQLSQFM DQTNPLAELT
HKRRLSALGP GGLTRERAGF EVRDVHYSHY GRMCPIETPE GPNIGLINSL SSFAKVNEFG
FIETPYRRVD PETGLVTGHV DYLTADEEDN YVVAQANMKL SEEGEFLDED IVARFRGENI
VTNKERIDYM DVSPKQVVSA ATACIPFLEN DDSNRALMGA NMQRQAVPLM NPESPIVGTG
MEYVSAKDSG AAVICKHPGI VERVEAREVW VRRYVEVDGQ TVKGDLDRYK MQKFIRSNQG
TCYNQRPIVS VGNEVVKGEI LADGPSMELG ELALGRNVLV GFMTWDGYNY EDAIIMSERL
VKDDVYTSIH IEEYESEARD TKLGPEEITR DIPNVGEDAL RNLDERGIIR VGAEVKDGDL
LVGKVTPKGV TELTAEERLL HAIFGEKARE VRDTSLRVPH GGGGIILDVK VFNREDGDEL
PPGVNQLVRA YIVQKRKISE GDKMAGRHGN KGVISRILPE EDMPYLPDGT PIDIMLNPLG
VPSRMNIGQV LELHLGMAAR YLGIHIATPV FDGAREEDVW GTIEEAGMAN DAKTILYDGR
TGEPFDNRVS VGVMYMIKLA HMVDDKLHAR STGPYSLVTQ QPLGGKAQFG GQRFGEMEVW
ALEAYGAAYT LQEILTVKSD DVVGRVKTYE AIVKGENVPE PGVPESFKVL IKELQSLGMD
VKMMSSDDTE IEMRDTEDDD DHQSADKLNV EVETTKE
