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 27-MAR-2024, 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};
GN OrderedLocusNames=COXBURSA331_A0328;
OS Coxiella burnetii (strain RSA 331 / Henzerling II).
OC Bacteria; Pseudomonadota; 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 KEGG; cbs:COXBURSA331_A0328; -.
DR HOGENOM; CLU_000524_4_0_6; -.
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:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1100.10; -; 2.
DR Gene3D; 2.30.150.10; DNA-directed RNA polymerase, beta subunit, external 1 domain; 1.
DR Gene3D; 2.40.270.10; DNA-directed RNA polymerase, subunit 2, domain 6; 1.
DR Gene3D; 3.90.1800.10; RNA polymerase alpha subunit dimerisation domain; 1.
DR Gene3D; 3.90.1110.10; RNA polymerase Rpb2, domain 2; 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 NCBIfam; TIGR02013; rpoB; 1.
DR PANTHER; PTHR20856; DNA-DIRECTED RNA POLYMERASE I SUBUNIT 2; 1.
DR PANTHER; PTHR20856:SF20; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 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 SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 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
//
