RPOB_COXB2
ID RPOB_COXB2 Reviewed; 1375 AA.
AC B6J270; O87903;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 73.
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=CbuG_1774;
OS Coxiella burnetii (strain CbuG_Q212) (Coxiella burnetii (strain Q212)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=434923;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9511749; DOI=10.1016/s0378-1119(97)00618-5;
RA Mollet C., Drancourt M., Raoult D.;
RT "Determination of Coxiella burnetii rpoB sequence and its use for
RT phylogenetic analysis.";
RL Gene 207:97-103(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CbuG_Q212;
RX PubMed=19047403; DOI=10.1128/iai.01141-08;
RA Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D.,
RA Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E.,
RA Heinzen R.A.;
RT "Comparative genomics reveal extensive transposon-mediated genomic
RT plasticity and diversity among potential effector proteins within the genus
RT Coxiella.";
RL Infect. Immun. 77:642-656(2009).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACJ19048.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U86688; AAC61666.1; -; Genomic_DNA.
DR EMBL; CP001019; ACJ19048.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; B6J270; -.
DR SMR; B6J270; -.
DR KEGG; cbg:CbuG_1774; -.
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_0000366031"
SQ SEQUENCE 1375 AA; 153672 MW; EA2821A144699297 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 NTNVDEKGRL 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
VKKDERTLEI EKAELSKVEK DLNDELRVRE DALFENLEKL LTGRVAAGGP NKLAKGTKIT
KSYLADLPRQ KWFEIRLQDD AATKRLEASH EHFKELRETR DAKLKDSRQK LTQGGDLAPG
VIKIVKVYLA VKRRIQPGDK MAGRHGNKGV ISTIVPIEDM PYLEDGTPVD IVLNPLGVPS
RMNIGQVLET HLGWAAKGLG KKIGEMIEKG ADAKELRKSL KPIYDLSKTQ RFDLEALEDP
EIVMLAKNLR KGVPISSPVF DGATEEEIKQ LLKMADLPTS GQAALYDGRT GKKFDRSVTV
GYMYMLKLNH LVDDKMHARS TGSYSLVTQQ PLGGKAQFGG QRFGEMEVWA LEAYGAAYTL
QEMLTVKSDD VAGRTRMYKN IVDGDHRMDA GMPESFNVLV KEIRSLAIDI GLEND