ID   RPOB_PORCN              Reviewed;        1270 AA.
AC   Q9F3X8;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 86.
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   Porphyromonas cangingivalis.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=36874;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 700135 / JCM 15983 / NCTC 12856 / VPB 4874;
RX   PubMed=12361249; DOI=10.1099/00207713-52-5-1477;
RA   Morse R., O'Hanlon K., Collins M.D.;
RT   "Phylogenetic, amino acid content and indel analyses of the beta subunit of
RT   DNA-dependent RNA polymerase of Gram-positive and Gram-negative bacteria.";
RL   Int. J. Syst. Evol. Microbiol. 52:1477-1484(2002).
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; Y16470; CAC10563.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9F3X8; -.
DR   SMR; Q9F3X8; -.
DR   STRING; 36874.HQ34_00335; -.
DR   eggNOG; COG0085; Bacteria.
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; -; 3.
DR   Gene3D; 2.40.50.150; -; 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; 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..1270
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000047935"
SQ   SEQUENCE   1270 AA;  142623 MW;  0B07E9144FB9E3C4 CRC64;
     MSSHNPTQRV NFASIKNPME YADFLDVQLK SFKDFLQLDT PPEKRKKEGL YKVFAENFPI
     HDTRNNFVLE FLDYYIDPPR YTLDECISRG LTYNVPLKAK MKLYCTDPEH EDFETVIQDV
     YLGPIPYMTE SGTFIINGAE RVVVSQMHRS PGVFFSESVH PNGTKLFSAR IIPFKGSWIE
     FATDINNVMY AYIDRKKKLP VTTLLRAIGF ETDKDILNLF GIAEEVKVSK STLKKYYGRK
     IAARVLNSWI EDLVDEETGE VVSMERYDVI VDRDELLTED NVDQIIESGA KNILITKDDS
     ELGLDYSVTT NTLQKDPSNS EKEAVYHIYK QLRNQDPVDD ASAREVINSL FFSEKRYDLG
     DVGRYRINKK LGINIDEETK VLTTEDITAI IAHLVELMNS KQVVDDIDHL SNRRVRTVGE
     QLYNQFGIGL ARMARTVRER MNVRDNEVFT PIDLINAKTI SSVVNSFFGT NALSQFMDRT
     NPLAEITHKR RLSSLGPGGL SRDRAGFEVR DVHYTHYGRL CPIETPEGPN IGLISSLCVY
     AKINDLGFIS TPYRKVVDGK VDFSENGVEY YTAEAEDDKT VAQGNAPLDE NGKFIKDAVY
     ARYGSDFPVV SPSEIDLMDV SPIQIASIAA SLIPFLEHDD ANRALMGSNM MRQAVPLIHS
     DAPIVGTGVE QKLVHDSRTQ IVAEGAGTVE FVDASVIKIR YDRSEDDTFV SFEDNLKIYN
     LPKFRKTNQS TTIDLRPICR KGDRVEKGDI LTEGYSTENG ELALGRNVQV AYMPWKGYNY
     EDAIVLNERM VREDIFTSVH VDEYILEVRE TKRGLEELTS DIPNVSEEAT KDLDDRGIIR
     VGARVHPGDI LIGKITPKGE SDPTPEEKLL HAIFGDKAGD VKDASLKANP SLSGVVIKTH
     LFSKAMHSKK DKGGVREIVK KLDEEMEEKL AELRELMLKK LIQLTDNKLS NGIRNFEDTE
     IVPKGVKLTP AVCSKIEFGE VAIFNWTGDE HTDELVAKLI SNYLRKAKEI ESEYRRKKFD
     ATIGDELPNG IIQIAKVLIA KKRKIQVGDK MAGRHGNKGI VSKIVRQEDM PFMEDGTPMD
     LCLNPLGVPS RMNLGQIFEL SSMGSRRLDV KFATPIFDGA SLDDLDQWTD KAGIPRYGKT
     YLYDGGTGEQ FDQPATVGVT YFLKLGHMVD DKMHARSIGP YSLITQQPLG GKAQFGGQRF
     GEMEVWALEA YGAAHVLQEM LTIKSDDVVG RSKAYEAIVK GAPMPTPGIP ESLNVLLHEL
     KGLGLSFCME