ID   RPOB_RICB8              Reviewed;        1372 AA.
AC   A8GV24;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=A1I_01515;
OS   Rickettsia bellii (strain OSU 85-389).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=391896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OSU 85-389;
RA   Madan A., Lee H., Madan A., Yoon J.-G., Ryu G.-Y., Dasch G., Ereemeva M.;
RT   "Complete genome sequencing of Rickettsia bellii.";
RL   Submitted (SEP-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; CP000849; ABV78695.1; -; Genomic_DNA.
DR   RefSeq; WP_012151623.1; NC_009883.1.
DR   AlphaFoldDB; A8GV24; -.
DR   SMR; A8GV24; -.
DR   KEGG; rbo:A1I_01515; -.
DR   HOGENOM; CLU_000524_4_0_5; -.
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   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; 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..1372
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_1000051978"
SQ   SEQUENCE   1372 AA;  153832 MW;  46A76042AB33D587 CRC64;
     MVSLRDNIEV QPLSHNKRVR KNFGHINLVA DIPNLIEIQK NSYEKNFLQL DTKDSERKNK
     GLQSILNSIF PISDPSNIAN LEFVKYEFDT PKYDVEECTQ RSLSYDSALK VTLRLSIWDI
     DEDTGSREIK GIKEQQVYMG NIPLMTKNGT FIINGTERVV VSQMHRSPGV FFYHDEGKVH
     SSRKLLYSAR VIPYRGSWLD LEFDAKDIIY FRIDRKRKLY ATTLLKAIGM STEEIIKFYY
     DSVNYKVVKN KGWAVKFMPS HITAHRLTSD LIDADTGNVL LKAGQKITPR LAKKYAGEGL
     NNILVSHEAL IGKYLSEDLK DPESDEILAK IGEMITVELL SVISDLKIKN ISVLVINPQS
     GPYIRNTLFS DKNQDRESAL FDIFRVLRPG EPANIEAAES LFYNLFFDPE RYDLSEVGRI
     KMNSRLELNI SDETTVLTTD DIKNILRVLV ELKDRKGIID DIDHLGNRRV RSVGELIENQ
     FRIGLVRMEK SVVERMSAGD IDTVMPHDLV NSKILVSVVK EFFSTSQLSQ FMDQTNPLSE
     ITHKRRLSAL GPGGLSRDRA GFEVRDVHPT HYGRICPIET PEGQNIGLIN SMATYARINK
     HGFIESPYRK VKDGHVTDEV VYLSAIEEGK YKIGQANSKV DKDGILQGEF INCRVEGGNF
     VMVEPHEVDF IDVTPMQVVS VAASLIPFLE NDDANRALMG SNMQRQAVPL IKTDAPFVGT
     GVEGVVAKDS GASVLALNDG IVEQVDSNRI VIRAIGQKTE SAPSVDIYNL LKFQKSNHNT
     CINQKPLVKV GHYVKKNDII ADGPSTDNGE IALGRNVLVA FLPWNGYNFE DSILISERIV
     KEDVFTSVHI EEFEVIARDT RLGPEEITRD IPNVSEEALR HLDEVGIIYV GAEVKAGDIL
     VGKVTPKSES PITPEEKLLR AIFGEKAFDV KDSSLHVPSG VSGTVVEVRV FSRRGVEKDQ
     RAIAIEKQQI EKLAKDRDDE LEIIEHFVFS WLEKLLVGQV SINGPKTVKT GQTITSEILK
     GLSKGQLWQF TVEDANVMNE IEQLKGHYDG KKEALNKRFA TKVEKLQSGD DLPQGALKVV
     KVFIATKHKL QPGDKMAGRH GNKGVISRIV PEEDMPFLED GTVVDIVLNP LGLPSRMNIG
     QVLETHLGWA SVNLAKKIAG LVEEHKTKHA SIEKIKKFLI ELYGENINHI LEKSDEEIIS
     FCNEAAKGVY FATPVFDGAK VEDVKDMLRL AGQDLSGQVK LIDGRTGEYF DRLVTVGQKY
     LLKLHHLVDN KIHSRSIGPY SLVTQQPLGG KSHFGGQRFG EMECWALQAY GAAYTLQEML
     TVKSDDVNGR IKIYDSIVRG ENNFESGIPE SFNVMIKEFR SLCLNVKLEV TS