RPOB_LEPBJ
ID RPOB_LEPBJ Reviewed; 1226 AA.
AC Q04QI9;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=LBJ_2365;
OS Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=355277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB197;
RX PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A.,
RA Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L.,
RA Rood J.I., Davies J.K., Adler B.;
RT "Genome reduction in Leptospira borgpetersenii reflects limited
RT transmission potential.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006).
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; CP000350; ABJ76831.1; -; Genomic_DNA.
DR RefSeq; WP_011669621.1; NC_008510.1.
DR AlphaFoldDB; Q04QI9; -.
DR SMR; Q04QI9; -.
DR PRIDE; Q04QI9; -.
DR EnsemblBacteria; ABJ76831; ABJ76831; LBJ_2365.
DR KEGG; lbj:LBJ_2365; -.
DR HOGENOM; CLU_000524_4_3_12; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000000656; Chromosome 1.
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; 1.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF10385; RNA_pol_Rpb2_45; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 2.
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..1226
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300338"
SQ SEQUENCE 1226 AA; 137683 MW; 3C4B7440FF5E4F04 CRC64;
MYGQVERKRV NFGKITNLDY LPNLIQIQKR SFDWFLQADV KDETKRKHQG LEAVFRETFP
IESPNNDMIM EYSHYILGEP KRSPQECKDT DATFAMPLKA VIRLIIKETG EIREQTVYMG
DLPVMTEQGT FIINGAERVV VSQLHRSPGI FFSYDMERDV FSARVIPYRG SWLEFEMDNK
GILIAKIDRK KKFPATLLIK SLGHGTNEEV LRLFYSSKKE KIAGATSKDL KKILGRRTIN
DIINMETGEV MLEAGSKVNE DNISILKEMK VKEVELIEFP KGKDNPILIN ALEKDGVNDY
EDAILKFHSL MRQGEPSTIE NATTELTRLF FSPKTFDLGE VGRYKINSKF EFNNPKEFSG
EKARVLRPAD IIETVRYILN LFSETENYYP DDIDHLGNRR IRSVGELISN QLKTGFSRVE
RVIKERMTVQ EIETQTPQLL ISIKPITAVI NEFFGSSQLS QFMDQTNPLA ELTHKRRLNA
LGPGGLSRDR AGMEVRDVHY SHYGRMCPIE TPEGPNIGLI LSMSSYARVN DYGFLETPYR
TVKNGKVTGQ IEHLTADKEE YHYIAQASGV IDEKGELKNK LISTRHRGDF PFRNPSEIQY
MDLAPLQVVS VSTALIPFLE HDDANRALMG SNMQRQAVPL LREEAPFVGT GMETRAAYDS
RICIVNKHDG VVTSVDAETI VVERKGGKES DTYSLTKFKK TNQGTCFNQK PIVGVVHSEI
NGKVSKVSKE KIEVTGENGE LKEYVLQIGS KQYAPIVSSG EEVKRGTTLA GQVVVGEKLD
EMGNILVKGT VLADGPAVDN GVLALGRNVL AAFMPWEGYN FEDAILISER IVRDDVFSSI
HIEEFEIQAR ETKLGPEQIT RDIPNLSDKA FRDLDETGVI RIGAEVKPGD ILVGMVTPKG
ETDLTPEYKL LHSIFGEKAK DVRDSSLRMP NGFEGTVIDI KRFSRENQDE LPAGVEEMVK
VFVARKRKLL VGDKMAGRHG NKGVVARVMA EEDMPYMEDG TPLDIVLNPL GVPSRMNLGQ
IFETQLGFAA SKLGISFETP VFDGAEESDV DNFCKEANLP LNSKFKLYDG RTGLPFMNEV
FCGYIYILKL AHLVEDKIHA RSTGPYSLVT QQPLGGKAQF GGQRLGEMEV WALEAYGASH
TLQELLTIKS DDMLGRARIY EAIVKGIHSI KPGIPESFNV LVQELRGLAL DIIITDSEGN
TVDISDYEDE YSKSKKKIKF ETIENA