ID   RPOB_LEPBI              Reviewed;        1228 AA.
AC   Q9KK59;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 83.
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};
OS   Leptospira biflexa.
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=172;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Serovar Patoc;
RX   PubMed=10834976; DOI=10.1128/jcm.38.6.2200-2203.2000;
RA   Renesto P., Lorvellec-Guillon K., Drancourt M., Raoult D.;
RT   "rpoB gene analysis as a novel strategy for identification of spirochetes
RT   from the genera Borrelia, Treponema, and Leptospira.";
RL   J. Clin. Microbiol. 38:2200-2203(2000).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF150880; AAF73184.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9KK59; -.
DR   SMR; Q9KK59; -.
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; 2.40.270.10; -; 2.
DR   Gene3D; 2.40.50.150; -; 1.
DR   Gene3D; 3.90.1110.10; -; 1.
DR   HAMAP; MF_01321; RNApol_bact_RpoB; 1.
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..1228
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000047910"
SQ   SEQUENCE   1228 AA;  137913 MW;  564A6AE40D8B66EE CRC64;
     MHTRMQIRNR VNFGKITDLN LLPNLIYVQK KSFDWFLQSE VKDPTKRLNQ GLEAVFRESF
     PIESPNNDMV MEYGHYVLGE PKRDPQECKD TDSSFAVPLK AVIRLIIKDT GEIREQVVYM
     GDLPVMTDHG TFIINGAERV VVSQLHRSPG IFFSYDQVRD TFSARVIPYR GSWLEFEMDN
     KGILVAKIDR KKKFPATLLV KAMGMGTNEE VLRLFYGSSK MKIAGANPKD LKRLIGRRTI
     ADIINMETGE VMLDAGSKIN EDNISILREM KVKEVDVIEF PKGKDNPVLI NCLEKDGVND
     YEDAVKKFHT IMRPGEPSTI ENAEAELKRL FFSPKTFDLG IVGRYKINSK FEFNNPKEFS
     KADDRVLRKQ DIIETVRYLV MLMSEAENYY PDDIDHLGNR RIRSVGELIA NQLKLGFSRV
     ERVIKERMTV QEPEQQTPQL LISIKPITAV INEFFGSSQL SQFMDQTNPL AELTHKRRLN
     ALGPGGLSRD RAGFEVRDVH YSHYGRMCPI ETPEGPNIGL ILSMSSFARV NDYGFIETPY
     RLVKNGKVQK QVEYLTADKE EYHYMAQSNS TVDEKGEFTS KLISTRHRGD FPFRSPAEIQ
     YMDLAPLQVV SVSTALIPFL EHDDANRALM GSNMQRQAVP LLTEEAPFVG TGMEARAAYD
     AGVCIVAKKD GVVSKVDATG VWIKEDQSKE IVHYPLIKFK KTNQGTCFNQ KPNVSMLHTT
     TGGKVSKVSK ERVEVTTPNG EKETHELLLS DEVQFHAVVK EGQEVGIGAP VAGQIIKGEK
     YGDFGQILQK GTVLANGPST DAGYLALGRN VLVAFMPWEG YNFEDAILIS ERIIKDDVFS
     SIHIEEFEIQ ARETKLGQEQ ITRDIPNLSD KAFRDLDESG VIRVGAEVKP GDILVGMVTP
     KGETDLTPEY KLLHSIFGEK AKEVRDSSLR MPNGFEGTVI DIKRYSRETG DELAAGVEEM
     VKVYVARKRK LLVGDKMAGR HGNKGVVARV MAQEDMPYME DGSPVDIVLN PLGVPSRMNL
     GQIFETQLGF AAKKLGINFE TPVFDGASEG DVNDFCKKAG LPENSKFQLY DGRTGEKFIN
     QVFCGYIYML KLAHLVDDKI HARSTGPYSL VTQQPLGGKA QFGGQRLGEM EVWALEAYGA
     SHTLQELLTI KSDDMLGRAR IYEAIVKGIH SIKPGIPESF NVLVQELRGL ALDIIIKDSE
     GLEVDISDYE DEFSKNKKKI KFETIENV