ID   RPOB_RICMA              Reviewed;        1373 AA.
AC   Q9RH43;
DT   11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 86.
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   Rickettsia massiliae.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=35791;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Mtu1;
RX   PubMed=10508014; DOI=10.1128/aac.43.10.2400;
RA   Drancourt M., Raoult D.;
RT   "Characterization of mutations in the rpoB gene in naturally rifampin-
RT   resistant Rickettsia species.";
RL   Antimicrob. Agents Chemother. 43:2400-2403(1999).
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; AF076433; AAF22431.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9RH43; -.
DR   SMR; Q9RH43; -.
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; 1.
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..1373
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000047949"
SQ   SEQUENCE   1373 AA;  154279 MW;  C530FE629F99CACE CRC64;
     MVSLRDNIEA QPLSHNRRIR KNFGHINLVA DIPNLIEIQK NSYEKNFLQL NIKDSERKNK
     GLQSILNSIF PISDSSNIAN LEFVKYEFDT PKYDVEECSQ RSLSYAAPLK VTLRLSIWDI
     DEDTGTREIK GIKEQEVYMG DIPLMTKNGT FIINGTERVV VSQMHRSPGV FFYHDEGKVH
     SSGKLLYSAR VIPYRGSWLD LEFDAKDVIY FRIDRKRKLY ITTLLRAIGM STEEIIKFYY
     NSVTYKLVKN KGWAVKFIPQ HITAHRLTSD LVDADTGNIL LKAGQKITPR LAKKYFGEGL
     NNILVAHETL IGKYLSEDLR DPTSDEVLAK IGEMITADML NVINALKIKN VNVLVINPQS
     GPYIRNTLFA DKNQDREAAL CDIFRVLRPG EPANIEAAES LFYNLFFDVD RYDLSEVGRI
     KMNSRLELNI SEEVTVLTID DIKNIVRVLV ELKDGKGIID DIDHLGNRRV RSVGELIENQ
     FRIGLVRMEK SVIERMSAGD VDTVMPHDLV NSKILVSVVK EFFNTSQLSQ FMDQTNPLSE
     ITHKRRLSAL GPGGLSRDRA GFEVRDVHPT HYGRICPIET PEGQNIGLIN SMATYARINK
     HGFIESPYRR VKDGCVTDEV VYLSAIEEGK YKIGQANSKV NKDGKLQGEF INCRVEGGNF
     VMVEPYEVDF IDVTPMQVVS VAASLIPFLE NDDANRALMG SNMQRQAVPL IKTDAPFVGT
     GVEGVVAKDS GASVLALHDG IVEQVDSNRI VIRTLEQKVD GSPSVDIYNL LKFQKSNHNT
     CINQKPLVKV GHYVKKNDII ADGPSTDNGE IALGRNVLVA FLPWNGYNFE DSILISERIV
     KEDVFTSIHI EEFEVIARDT RLGPEEITRD IPNVSEEALR HLDEVGIIYI GAEVKAGDIL
     VGKVTPKSES PITPEEKLLR AIFGEKAFDV KDSSLHVPSG VSGTVVEVRV FSRRGVEKDQ
     RAIAIEKQQI EKLAKDRDDE LEIIEHFVFS WLEKLLVGQV IINGPKQVKV GQTITTEMLK
     GLSKGQFWQI TVEDANVMNE IEQIKTHYDE KKEALDKRFA TKVEKLQSGD DLPQGALKVV
     KVFIATKHKL QPGDKMAGRH GNKGVISRIV PEEDMPFLED GTVVDIVLNP LGLPSRMNIG
     QILETHLGWA SINLAKKIST LVKEYKNKHI GIEQIKKFLI ELYGENINSI LERPEEEIIS
     FCKKVSKGVH FATPVFDGAK VQDVKDMLKL AGQDPSGQVK LIDGRTGEYF DRLVTVGQKY
     LLKLHHLVDN KIHSRSIGPY SLVTQQPLGG KSHFGGQRFG EMECWALQAY GAAYTLQEML
     TVKSDDVNGR IKTYDSIVRG ENNFESGIPE SFNVMIKEFR SLCLNVKLEV TSS