ID   RPOB_AQUPY              Reviewed;        1469 AA.
AC   Q9X6Y1;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 84.
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};
OS   Aquifex pyrophilus.
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=2714;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 6858 / JCM 9492 / Kol5A;
RX   PubMed=10198119; DOI=10.1007/pl00006496;
RA   Klenk H.-P., Meier T.D., Durovic P., Schwass V., Lottspeich F.,
RA   Dennis P.P., Zillig W.;
RT   "RNA polymerase of Aquifex pyrophilus: implications for the evolution of
RT   the bacterial rpoBC operon and extremely thermophilic bacteria.";
RL   J. Mol. Evol. 48:528-541(1999).
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; X75046; CAA52957.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9X6Y1; -.
DR   SMR; Q9X6Y1; -.
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; -; 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; Transcription;
KW   Transferase.
FT   CHAIN           1..1469
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000047856"
SQ   SEQUENCE   1469 AA;  167302 MW;  F83D2B663E93E9E4 CRC64;
     MAKIALPRKF FGRRTEILEP PYLLSIPKNS FENFVQLKVN PYKRKNVGLE HIFRTSFPFK
     DPDENFILEY LGYEIGDWEC NRCGYKPKDD LLGGWDVDCP ECGAKLVYKE KFTPEECKLK
     GLTYSAPLRV MLQLKAKTKN GYRTFPPRKV YFGEVPLMTD NGSFIINGTE RIIINQLIRS
     SGVFFDEKEE KQKDATITRI LYRASIIPDK GSRVEFELSG ATDLISARID RKKLSAISVL
     RAFGLETAYD ILKPFYEGVR KYIVKDKYLY DAETGEEFTP EDLEHHYIFA ILKFKAKIAG
     FGTSKEREII EERYIEEWEE LVRILDDERI EVLSVTSVPR ENVIKSPYGK SLVDTLATDT
     SPRDADRRSP VKVPAEYTLR DYGLMEMYKK LRHIEALTME IDSIIERARV YFNVFFRDLK
     RYDLSRVGRV KINAKVHNIP KVLKPTDIDL LDNLPPLALA EDYGEYKAGT RITKELLKEL
     FKNYKEIKVK DYTEDEARFL LPIDLINILK YLIDLRHGRV KKDDIAHLGN RRVRSVGELL
     ENQARLGIAK MEKVFRDRSA TIHPEQPDLK PQDFINPRYV TNAIADFLKT GQLSQYLDNT
     NPLSELTHKR RLSALGPGGL TRESAKFEIR DVHPSHYGRI CPIETPEGQN IGLVTSPTVY
     ARVNEYGFLI TPYRKVENGR VTDKIEWLAA YEEENYVIAQ STPTDEEGRI KAEFVLARHK
     NDIRLVKPEQ VDYIDVSPRQ VISPSSSLIP FLEHDDANRA LMGSNMQRQA VPLIFTQAPL
     VGTGMEKKIA RDSHAVVVAK RGGVVEEVDG SKIIVRVNPE EINLEDPLDI GIDIYELRKF
     ERTNQKTCVN QRPIVKKGER VEKGQIIADG HSTDRGELAL GKDVLVAFMP WRGYNFEDAI
     VISERLVKED VYTSIHIEEL EVEARETKVG DEEITRQIPG VPERALAHLD EHGIVRVGTY
     VKPGDILVGK VTPKGETRLT PEEKLLQAIF GEKTKDVKDA SLRCPPGVEG IVIDVQVFTR
     KGGKAAKDML AQKVEREELE ALERELEKKK NLLMSGVEKV LKGLILGKKT DKDVKIGKKE
     IKKGTEITEE IFKEYSQYIL ARPENFFTDE ELIKKIREIY TRSRTQIDML QKVYQEKKET
     LLKRRDLPPG VITLVKVFIA NKRKIKVGDK MAGRHGNKGV ISVVLPVEDM PFLPDGTPVD
     IVLNPLGVPS RMNVGQILET HLGWAAKELG KKIGEMIEKG RDRKAITEYL KEIYAVGDEN
     GENAKFIEEF LNSLSEEEFW SVVRDYAQRG IPMATPAFEG ADEKAVKELL KKAGLPESGK
     TTLYDGRTGE PFDFEVTVGY MHMLKLIHMV DDKIHARATG PYSLVTQQPL GGRAQFGGQR
     LGEMEVWALE AHGAAYTLQE MLTVKSDDVE GRSKVYEAIV KGKYTYTPGI PESFKVLVRE
     LKGLSLNVKC MNGEEKPCDQ VEIKEEEEK