RPOB_RICBR
ID RPOB_RICBR Reviewed; 1372 AA.
AC Q1RHD0;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=RBE_1153;
OS Rickettsia bellii (strain RML369-C).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=336407;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RML369-C;
RX PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA Fournier P.-E., Claverie J.-M., Raoult D.;
RT "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT gene exchanges between intracellular pathogens.";
RL PLoS Genet. 2:733-744(2006).
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; CP000087; ABE05234.1; -; Genomic_DNA.
DR RefSeq; WP_011477812.1; NC_007940.1.
DR AlphaFoldDB; Q1RHD0; -.
DR SMR; Q1RHD0; -.
DR STRING; 336407.RBE_1153; -.
DR PRIDE; Q1RHD0; -.
DR EnsemblBacteria; ABE05234; ABE05234; RBE_1153.
DR KEGG; rbe:RBE_1153; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_5; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000001951; 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; 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_0000272393"
SQ SEQUENCE 1372 AA; 153845 MW; 72431578B8F20B58 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
NNILVSHKAL 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 VIRAIAQKTE 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
