RPOB_EHRRG
ID RPOB_EHRRG Reviewed; 1380 AA.
AC Q5FFD9;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
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};
GN OrderedLocusNames=ERGA_CDS_01650;
OS Ehrlichia ruminantium (strain Gardel).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=302409;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gardel;
RX PubMed=16547041; DOI=10.1128/jb.188.7.2533-2542.2006;
RA Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y.,
RA Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.;
RT "Comparative genomic analysis of three strains of Ehrlichia ruminantium
RT reveals an active process of genome size plasticity.";
RL J. Bacteriol. 188:2533-2542(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; CR925677; CAI27617.1; -; Genomic_DNA.
DR RefSeq; WP_011255344.1; NC_006831.1.
DR AlphaFoldDB; Q5FFD9; -.
DR SMR; Q5FFD9; -.
DR EnsemblBacteria; CAI27617; CAI27617; ERGA_CDS_01650.
DR KEGG; erg:ERGA_CDS_01650; -.
DR HOGENOM; CLU_000524_4_1_5; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR BioCyc; ERUM302409:ERGA_RS00855-MON; -.
DR Proteomes; UP000000533; 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; -; 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..1380
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000224055"
SQ SEQUENCE 1380 AA; 155947 MW; A2121D1D81DBBA8C CRC64;
MSSSVTSKYV LNSFSSVPRL SYAKSIDIKD SLTDLIKIQR DSYNAFIGID QDVDSGIKNI
FQSMFPIQDL LGRAVLQFVS YSIGEPQYDE YECIKRGITY SVPIRIVLRF IVWKVQEVSF
KEVKYVVDEE TSEKSIKYIK EQEVSIGDLP TMTSYGTFII NGVERVIVSQ MHRSPGVFFD
SDKGKTYSSG KLIYLARIIP YRGSWLDFEF DIKDILYFRI DRKRKLPVSL LLRALGLSNS
EILDTFYDKI RYERCENGWV VPFVVDRFRG VRLSYDLVDI DGNVLVKANT RITLRLAKKL
ASDGLKKYLV PFAEIQGLFI ANDLVDPASN VMIMCAGESI TSEHINKLKL FDINEIFILN
IDFLTVGPYI LNTLFLDKNI SYEDALFEIY KVLRSGESPS LDTMKAFFDG LFFEKERYDL
STVGRIKLND HLGLDISEDV TVLTKDDIIH VIKKLVLLRD GEGFVDDIDH LGNRRVRSVG
EFIENQFRIG ILRLERMIMD YMSSVNFDNA MPCDFVNPKV LATVLKDFFS SSQLSQFMDQ
TNPLSEVTHK RRLSALGPGG LTRERAGFEV RDVHPTHYGR ICPIETPEGQ NIGLISSLAI
YARINKHGFI ESPYRKVDNG IVTDKVEYLL AMQESNYYIA DASATLDENN RFVDDMLYCR
HDGNFVMVKR EQVDYIDVSP KQIVSVAASL IPFLENNDAN RALMGSNMQR QAVPLLKADA
PLVGTGMESI VAAGSGTVVL AKRSGIVHRV DGLYIVIRAF DKEKNEYLGV DIYNLRKFQR
SNHNTCINQK PLVKPGDYVR ENDVIADGSA IDQGELALGK NVLVAFMSWQ GYNFEDSIVI
SSEVVKKDVF TSIHIEEFEC VVRDTALGPE KIMRSIPDVN EDSLSHLDDV GIVNVGAEVS
AGDILVGKVT PRPPVSLPPE TKLLVTIFGE KVFDCVDSSL YLPIDVEGTV VDVHVFVRRG
VEENDRSLLI KQNEINGFIK ERDYEIDVVS EYFYDELKRV LVNTNTEYNN QNIEDYLKSI
PQKSWWDIKL SDESVLSQIS DLKEKFDSMI ENAHSKFDQK IDKLNYGYDL PQGVLCIVKV
FVAVKHNLQP GDKMAGRHGN KGVISRIVPV EDMPYLEDGT PVDIILNSLG VPSRMNVGQI
LETHLGWASV NLGKKIGNIL DNIDELTIAH LRNFLDQVYD GQDLKYSIRS MSDDDLLAFA
ERLRDGVPMA APVFEGPKDN QISNLLKLAD LDVSGQVDLY DGRIGEKFDR KVTVGYIYML
KLHHLVDDKI HARSVGPYGL VTQQPLGGKS HFGGQRFGEM ECWALQAYGA AYTLQEMLTV
KSDDIVGRVK IYESIIKGDS NFECGIPESF NVMVKELRSL CLDVALKQDK DFLHDRKINN
