RPOB_ACIC1
ID RPOB_ACIC1 Reviewed; 1169 AA.
AC A0LRL3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=Acel_0299;
OS Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC Bacteria; Actinobacteria; Acidothermales; Acidothermaceae; Acidothermus.
OX NCBI_TaxID=351607;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43068 / DSM 8971 / 11B;
RX PubMed=19270083; DOI=10.1101/gr.084848.108;
RA Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT "Complete genome of the cellulolytic thermophile Acidothermus
RT cellulolyticus 11B provides insights into its ecophysiological and
RT evolutionary adaptations.";
RL Genome Res. 19:1033-1043(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; CP000481; ABK52073.1; -; Genomic_DNA.
DR AlphaFoldDB; A0LRL3; -.
DR SMR; A0LRL3; -.
DR STRING; 351607.Acel_0299; -.
DR PRIDE; A0LRL3; -.
DR EnsemblBacteria; ABK52073; ABK52073; Acel_0299.
DR KEGG; ace:Acel_0299; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_11; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000008221; 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; 1.
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; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..1169
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300268"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1169 AA; 129702 MW; AFB6F075C1409A16 CRC64;
MVDREPWKEP HLAASGSTSM INGPLAPHRV SFAKIHEPLD LPNLLALQIE SFDWLVGNDA
WKARVEAALA AGRTDVNTSS GLEEIFEEIS PIEDISGTMS LSFRDHRFEP PKNTPDECRE
RDFTYSAPLF VTAEFVNNTT GEIKSQTVFM GDFPLMTEKG TFIINGTERV VVSQLVRSPG
VYFDRTVDKT SDRDIYGCKI IPSRGAWLEL EIDKRDNVGV RIDRKRKQSV TVLLKALGWD
DARILERFGE FEAIRATLEK DHVHTQEEAL LDIYRKLRPG EPPTYEAAQT LLNNLYFNPK
RYDLAKVGRY KVNKKLGLDL PYTQNTLTEE DIVATIDYLV RLHAGQTETT RNGRTVIIET
DDIDHFGNRR LRTVGELIQN QIRLGLARME RVVRERMTTQ DIVAITPQTL INIRPVVASI
KEFFGTSQLS QFMDQTNPLA GLTHKRRLNA LGPGGLSRER AGFEVRDVHP SHYGRMCPIE
TPEGPNIGLI GSLATHGRVN AFGFVETPYR KVINGRVTDQ VDYLTADEED RHVIAQANAP
LNEDGSFAEE RVLVRRRGGE VDYVHPSTVD YMDVSPRQMV SVATALIPFL EHDDANRALM
GSNMQRQAVP LLRAEAPLVG TGMEFRAAVD AGDVVIASKA GVVEEVSADA ITIAADDGTR
QTYRLAKFRR SNQGTCINQK PIVDEGQRVE AGQPIADGPC TQGGELALGR NLLVAFMSWE
GHNYEDAIII SERLVKEDIL SSIHIEEHEV DARDTKLGPE EITRDIPNVS EEILADLDER
GIIRIGADVV PGDILVGKVT PKGETELTPE ERLLRAIFGE KAREVRDTSL KVPHGESGKV
IDVKVFTRDD AELPPGVNEL VRVYVAQKRK ITDGDKLAGR HGNKGVIAKI LPEEDMPFLE
DGTPVDIILN PLGVPGRMNV GQVLETHLGW AAKSGWKVEL NGQPEGWRKR LADIGALDAP
PNTLVATPVF DGAKEDEIRG LLENALPNSD GLRMVGPDGK ARLFDGRTGE PYPEPISVGY
IYIMKLHHLV DDKLHARSTG PYSMITQQPL GGKAQFGGQR FGEMEVWALE AYGAAYALQE
LLTIKSDDVL GRVKVYEAIV KGENIPEPGI PESFKVLVKE MQALCLNVEV LSSDGMTVEM
RETDDEVFRA AEELGIDLSR REPSSVEEI
