ID   RPOB_COXBR              Reviewed;        1375 AA.
AC   A9NAL4;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
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};
GN   OrderedLocusNames=COXBURSA331_A0328;
OS   Coxiella burnetii (strain RSA 331 / Henzerling II).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=360115;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSA 331 / Henzerling II;
RA   Seshadri R., Samuel J.E.;
RT   "Genome sequencing of phylogenetically and phenotypically diverse Coxiella
RT   burnetii isolates.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000890; ABX78812.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9NAL4; -.
DR   SMR; A9NAL4; -.
DR   PRIDE; A9NAL4; -.
DR   KEGG; cbs:COXBURSA331_A0328; -.
DR   HOGENOM; CLU_000524_4_0_6; -.
DR   OMA; FMTWEGY; -.
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..1375
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000329173"
SQ   SEQUENCE   1375 AA;  153570 MW;  94BCE5E7DFFF823F CRC64;
     MAQANSRSRN SATISYPEKR RARVNLGKRE VEILKTPYLL ETQIESYRKF LQKDIAAEKR
     EDNGLHAAFK SVFPITSYSG YAVLEYVGYS LGGESTLFDV EECKLRGLTY AAPLKVNMRL
     VIYDKEAPAG KKAIKDIKEQ EVYMGEIPLM TETGSLVING TERVVVSQLH RSPGVFFEHD
     KGKTHSSGKL LYSARVIPYR GSWLDFEFDP KDCLFVRIDR RRKLPATVIL RALGYDTEQI
     LDMFYKTNHF HLNQETVTLD LIPQRLRGEL AVVEIKDKKG KVIVEANRRI SARHIRLIEK
     AEINKLELPD DYLYGKVIGK TIIDKETGEI IAHANEEITA ELLKNLRATK TASLDTLYIN
     EIECGPYVSD TLRLDTTTNQ LEALVEIYRI MRPGEPPTKE AAESLFENLF FSPERYSLSA
     VGRMKFNRRV GRKELTGLDV LSKEDIVDVL RVLVDIRDGK GDVDDIDHLG NRRIRSVGEM
     AENQFRVGLV RVERAVKDRL SLADVENLMP QDLVNAKPVS AAIKEFFGSS QLSQFMDQNN
     PLSEITHKRR VSALGPGGLT RERAGFEVRD VHVTHYGRVC PIETPEGPNI GLINSLAVFA
     RANEYGFLET PYRKVVDRVV TDETEYLSAI EEGDYYIAQA NTNVDGKGRL VDDLISCRYK
     GEFTLTTPDK INYMDVSPRQ IVSVAAALIP FLEHDDANRA LMGSNMQRQA VPTIRPETPL
     VGTGMERTVA VDSGVTVIAK RSGVIDSVDA SRIVVRVDRK ETEDDDDIGV DIYNLTKFTR
     SNQNTCINQH PIVEVGDKVQ KGDVLADGPS TDIGELALGQ NLLVAFMPWN GYNFEDSILI
     SERLVEEDRF TTIHIQEFTC VARDTKLGPE EITSDIPNVG ESALAKLDES GIVHIGAEVN
     AGDILVGKVT PKGETQLTPE EKLLRAIFGE KASDVKDTSL RVTPGITGTV IDVRIFTREG
     IKKDERTLEI EKAELSKVEK DLNDELRVRE DALFENLEKL LTGRVAAGGP NKLAKGTKIT
     KSYLADLPRQ KWFEIRLQDD AATKRLEASH EHFKELRETR DAKLKDSRQK LTQGGDLAPG
     VIKIVKVYLA VKRRIQPGDK MAGRHGNKGV ISTIVPIEDM PYLEDGTPVD IVLNPLGVPS
     RMNIGQVLET HLGWAAKGLG KKIGEMIEKG ADAKELRNSL KPIYDLSKTQ RFDLEALEDP
     EIVTLAKNLR KGVPISSPVF DGATEEEIKQ LLKMADLPTS GQAALYDGRT GKKFDRSVTV
     GYMYMLKLNH LVDDKMHARS TGSYSLVTQQ PLGGKAQFGG QRFGEMEVWA LEAYGAAYTL
     QEMLTVKSDD VAGRTRMYKN IVDGDHRMDA GMPESFNVLV KEIRSLAIDI GLEND