RPOB_AQUAE
ID RPOB_AQUAE Reviewed; 1468 AA.
AC O67762;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 120.
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=aq_1939;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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; AE000657; AAC07723.1; -; Genomic_DNA.
DR PIR; F70466; F70466.
DR RefSeq; NP_214331.1; NC_000918.1.
DR RefSeq; WP_010881267.1; NC_000918.1.
DR AlphaFoldDB; O67762; -.
DR SMR; O67762; -.
DR STRING; 224324.aq_1939; -.
DR EnsemblBacteria; AAC07723; AAC07723; aq_1939.
DR KEGG; aae:aq_1939; -.
DR PATRIC; fig|224324.8.peg.1501; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_0; -.
DR InParanoid; O67762; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000000798; 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..1468
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000047855"
SQ SEQUENCE 1468 AA; 167388 MW; 9182372EA417930E CRC64;
MAKIALPRKF FGRRFEVLEP PYLLSIPKNS FENFVQLKVN PYKRKNVGLE HIFRTSFPFK
DPDENFILEY LGYEIGDWEC NRCGYKPKDD LLGGWDVDCP QCGAKLVYKE KFTPEECKLK
GLTYSAPLRV MLQLKAKTKN GYREFPPKKV YFGEIPLMTE TGSFIINGTE RIIINQLIRS
SGVFFDEKEE KQKDATITRI LYRGSIIPDK GSRVEFELSG ATDLISARID RKKLSATAVL
RAFGLETAYD ILKYFYEDVR KFIVKDKYLY DAQTGEEFTP EDLEHHYIFA IIKFRGKLVG
FASSKERDFI EERYIEEWED LVRLLDDDRI EVLSVTAVPR DVVIKSPYGK SLIDTLANDT
SPKDVDKRSP VKVPAEYTLR DYGLMEMYKR LRHIEAITME IDSVIERARI FFNVFFRDLK
RYDLSRVGRV KINAKVHRIP KVLKPADVDL LDQLPPLALA EDYGEYKAGT RVTKDLLKEL
FKQYKEIKVK DYTEDEARFI LPIDLVNILK YLIDLRHGRV KKDDIAHLGN RRVRSVGELL
ENQARLGIAK MEKVFRDRSA VINPEQPDLK PQDFINPRYV TTAITDFLKT GQLSQYLDNT
NPLSELTHKR RLSALGPGGL TRESAKFEIR DVHPSHYGRI CPIETPEGQN IGLVTSPTVY
ARVNEYGFLI TPYRKVENGK VTDKIEWLAA YEEENYVIAQ STPTDEEGRL KAEFILARHK
NDIRLVKPEQ VEYIDVSPRQ VISPSSSLIP FLEHDDANRA LMGSNMQRQA VPLIFTQAPL
IGTGMEKKIA RDSHAVVVAK RGGVVEEVDS SKIIIRVNPE EINFDDPLDI GIDIYELRKF
QRTNQKTCVN QRPIVRKGEK VEKGQIIADG HSTDRGELAL GKDVLVAFMP WRGYNFEDAI
VISERLVKED VYTSIHIEEL EVEARETKVG EEEITRQIPG VPERALAHLD EHGIVRVGTY
VKPGDILVGK VTPKGETRLT PEEKLLQAIF GEKTRDVKDA SLRCPPGVEG IVIDVQVFTR
KGTGKKDMLA EKVEREELEA LEQELEKKKN LIITGRDKVL KGLVLGRKVE KDAKVGRKTV
KKGTVIDEKV FEEFVNYILG RPENFFEDED LIRKIREIAE RTRTQIEMLN KVYEEKKETL
LKRRDLPPGV ITLVKVFIAN KRKIKVGDKM AGRHGNKGVI SVVLPVEDMP FLPDGTPVDI
VLNPLGVPSR MNVGQILETH LGWAAKELGK KIGEMIEKGR DRKAITEYLK EIFAIGDKDG
ENAKFIEEFL NSLSEEEFWS VVRDYAERGI PMATPAFEGA EEDAIKELLK KAGLPENGKT
TLYDGRTGEP FDFEVTVGYM HMLKLIHMVD DKIHARATGP YSLVTQQPLG GRAQFGGQRL
GEMEVWALEA HGAAYTLQEM LTVKSDDVEG RTKVYEAIVK GKYTYTPGIP ESFKVLVREL
KALGLNVKCL NGEEKPCDEV EVKEEEEK