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RPOB_RICCN
ID   RPOB_RICCN              Reviewed;        1373 AA.
AC   Q9RH41; Q9RH39;
DT   11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 121.
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=RC0181;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7, and Moroccan;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
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; AF076434; AAF22433.1; -; Genomic_DNA.
DR   EMBL; AF076435; AAF22435.1; -; Genomic_DNA.
DR   EMBL; AE006914; AAL02719.1; -; Genomic_DNA.
DR   PIR; E97722; E97722.
DR   RefSeq; WP_010976851.1; NC_003103.1.
DR   AlphaFoldDB; Q9RH41; -.
DR   SMR; Q9RH41; -.
DR   EnsemblBacteria; AAL02719; AAL02719; RC0181.
DR   KEGG; rco:RC0181; -.
DR   PATRIC; fig|272944.4.peg.210; -.
DR   HOGENOM; CLU_000524_4_0_5; -.
DR   OMA; FMTWEGY; -.
DR   Proteomes; UP000000816; Chromosome.
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; -; 2.
DR   Gene3D; 2.40.50.150; -; 1.
DR   Gene3D; 3.90.1110.10; -; 2.
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; 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_0000047948"
FT   VARIANT         109
FT                   /note="L -> P (in strain: Moroccan)"
FT   VARIANT         931
FT                   /note="K -> E (in strain: Moroccan)"
SQ   SEQUENCE   1373 AA;  154270 MW;  D19C51E150339E9B CRC64;
     MVSLRDNIEA QPLSHNRRIR KNFGHINLVA DIPNLIEIQK NSYEKNFLQL NIKDSERKNK
     GLQSILNSIF PISDSSNIAN LEFVKYEFDT PKYDVEECSQ RSLSYAAPLK VTLRLSIWDI
     DEDTGTREIK GIKEQEVYMG DIPLMTKNGT FIINGTERVV VSQMHRSPGV FFYHDEGKVH
     SSGKLLYSAR VIPYRGSWLD LEFDAKDVIY FRIDRKRKLY TTTLLRAIGM STEEIIKFYY
     NSVTYKLVKN KGWAVKFIPQ HITAHRLTSD LVDADTGNIL LKAGQKITPR LAKKYSGEGL
     NNILVAHETL IGKYLSEDLR DPASDEVLAK IGEMITADML NVINDLKIKN VNVLVINPQS
     GPYIRNTLFA DKNQDREAAL CDIFRVLRPG EPANIEAAES LFYNLFFDTE RYDLSEVGRI
     KMNSRLELNI SEEVTVLTID DIKNIVRVLV ELKDGKGIID DIDHLGNRRV RSVGELIENQ
     FRIGLVRMEK SVIERMSAGD VDTVMPHDLV NSKILVSVVK EFFSTSQLSQ FMDQTNPLSE
     ITHKRRLSAL GPGGLSRDRA GFEVRDVHPT HYGRICPIET PEGQNIGLIN SMATYARINK
     HGFIESPYRR VKDGCVTDEV VYLSAIEEGK YKIGQANSKI 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 EKFAKDRDDE LEIIEHFVFS WLEKLLVGQV IINGPKQVKV GQTITTEMLK
     GLSKGQFWQI IVEDANVMNE 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
 
 
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