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RPOB_RICPU
ID   RPOB_RICPU              Reviewed;        1373 AA.
AC   C4K1N9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=RPR_03955;
OS   Rickettsia peacockii (strain Rustic).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=562019;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rustic;
RX   PubMed=20027221; DOI=10.1371/journal.pone.0008361;
RA   Felsheim R.F., Kurtti T.J., Munderloh U.G.;
RT   "Genome sequence of the endosymbiont Rickettsia peacockii and comparison
RT   with virulent Rickettsia rickettsii: identification of virulence factors.";
RL   PLoS ONE 4:E8361-E8361(2009).
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; CP001227; ACR47489.1; -; Genomic_DNA.
DR   AlphaFoldDB; C4K1N9; -.
DR   SMR; C4K1N9; -.
DR   EnsemblBacteria; ACR47489; ACR47489; RPR_03955.
DR   KEGG; rpk:RPR_03955; -.
DR   HOGENOM; CLU_000524_4_1_5; -.
DR   OMA; FMTWEGY; -.
DR   Proteomes; UP000005015; 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_1000214487"
SQ   SEQUENCE   1373 AA;  154302 MW;  CCEE5BBD2F995C87 CRC64;
     MVSLRDNIEA QPLSHNRRIR KNFGHINLVA DIPNLIEIQK NSYEKNFLQL NIKDSERKNK
     GLQSILNSIF PISDSSNIAN LEFVKYEFDT TKYDVEECSQ RSLSYAAPLK VTLRLSIWDI
     DEDTGTREIK GIKEQEVYMG DIPLMTKNGT FIINGTERVV VSQMHRSPGV FFYHDEGKVH
     SSGKLLYSAR VIPYRGSWLD LEFDAKDVIY FRIDRKRKLY TTTLLRAIGM STEEIIKFYY
     NSVTYKLVKN KGWAVKFIPQ HITAHRLTSD LVDADTGNIL LKAGQKITPR LAKKYFGEGL
     NNILVAHETL IGKYLSEDLR DPASDEVLAK IGEMITADML NVINDLKIKN VNVLVINPQS
     GPYIRNTLFA DKNQDREAAL CDIFRVLRPG EPVNIEAAES LFYNLFFDTE RYDLSEVGRI
     KMNSRLELNI SEEVTVLTID DIKNIVRVLV ELKDGKGIID DIDHLGNRRV RSVGELIENQ
     FRIGLVRMEK SVIERMSAGD VDTVMPHDLV NSKILVAVVK EFFSTSQLSQ FMDQTNPLSE
     ITHKRRLSAL GPGGLSRDRA GFEVRDVHPT HYGRICPIET PEGQNIGLIN SMATYARINK
     HGFIESPYRR VKDGCVTDEV VYLSAIEEGK YKIGQANSKI NKDGKLQGEF INCRVEGGNF
     VMVEPYEVDF IDVTPMQVVS VAASLIPFLE NDDANRALMG SNMQRQAVPL IKTDAPFVGT
     GVEGVVAKDS GASVLALHDG IVEQVDSNRI VIRILEQKVD GSPSVDIYNL LKFQKSNHNT
     CINQKPLVKV GHYVKKNDII ADGPSTDNGE IALGRNVLVA FLPWNGYNFE DSILISERIV
     KEDVFTSIHI EEFEVIARDT RLGPEEITRD IPNVSEEALR HLDEVGIIYI GAEVQAGDIL
     VGKVTPKSES PITPEEKLLR AIFGEKAFDV KDSSLHVPSG VNGTVVEVRV FSRRGVEKDQ
     RAIAIEKQQI EKFAKDRDDE LEIIEHFVFS WLEKLLVGQV IINGPKQATV GQTITTEMLK
     GLSKGQFWQI TVEDANVMNE IEQIKTHYDE KKEALDKRFA TKVEKLQSGD DLPQGALKVV
     KVFIATKHKL QPGDKMAGRH GNKGVISRIV PEEDMPFLED GTVVDIVLNP LGLPSRMNIG
     QILETHLGWA SINLAKKIST LVKEYKNKHI GIEQIKKFLI ELYGENINSI LERPEEEIIA
     FCKKVSKGVH FATPVFDGAK VQDVKDMLKL AGQDPSGQVK LIDGRTGEYF DRLVTVGQKY
     LLKLHHLVDN KIHSRSIGPY SLVTQQPLGG KSHFGGQRFG EMECWALQAY GAAYTLQEML
     TVKSDDVNGR IKTYDSIVRG ENNFESGIPE SFNVMIKEFR SLCLNVKLEV TSS
 
 
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