ID   RPOB_LEPIC              Reviewed;        1226 AA.
AC   Q72UA8;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=LIC_10753;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni
OS   (strain Fiocruz L1-130).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=267671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fiocruz L1-130;
RX   PubMed=15028702; DOI=10.1128/jb.186.7.2164-2172.2004;
RA   Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B.,
RA   Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V.,
RA   Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L.,
RA   Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S., Ferro M.I.T.,
RA   Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H.,
RA   Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M.,
RA   Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L.,
RA   Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A.,
RA   Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A.,
RA   Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A.;
RT   "Comparative genomics of two Leptospira interrogans serovars reveals novel
RT   insights into physiology and pathogenesis.";
RL   J. Bacteriol. 186:2164-2172(2004).
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; AE016823; AAS69370.1; -; Genomic_DNA.
DR   RefSeq; WP_000274334.1; NC_005823.1.
DR   AlphaFoldDB; Q72UA8; -.
DR   SMR; Q72UA8; -.
DR   PaxDb; Q72UA8; -.
DR   EnsemblBacteria; AAS69370; AAS69370; LIC_10753.
DR   GeneID; 61144093; -.
DR   KEGG; lic:LIC_10753; -.
DR   HOGENOM; CLU_000524_4_3_12; -.
DR   OMA; FMTWEGY; -.
DR   Proteomes; UP000007037; Chromosome I.
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_0000047911"
SQ   SEQUENCE   1226 AA;  137767 MW;  090E5D43B82B601A CRC64;
     MYGQVERKRV NFGKITNLDY LPNLIQIQKR SFDWFLQADV KDETKRRHQG LEAVFRETFP
     IESPNNDMIM EYSHYILGEP KRSPQECKDT DATFAMPLKA VIRLIIKETG EIREQTVYMG
     DLPVMTEQGT FIINGAERVV VSQLHRSPGI FFSYDMERDV FSARVIPYRG SWLEFEMDNK
     GILIAKIDRK KKFPATLLVK SLGHGTNEEV LRLFYSSKKE KIAGATSKDL KKILGRRTIN
     DIINMETGEV MLEAGSKINE DNISILKEMK VKEVELIEFP KGKDNPILIN ALEKDGVNDY
     EDAILKFHSL MRQGEPSTIE NATTELTRLF FSPKTFDLGE VGRYKINSKF EFNNPKEFSG
     EKSRVLRPAD 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 VVTSVDAENI VVERKGGKES DTYQLTKFKK TNQGTCFNQK PIVGVVHSEI
     NGKVSKVSKE KIEVTGENGE LKEYVLQIGS KQYSPIVSAG EEVKRGSTLA 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