RPOB_MOOTA
ID RPOB_MOOTA Reviewed; 1141 AA.
AC Q2RFN9;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=Moth_2468;
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Moorella group; Moorella.
OX NCBI_TaxID=264732;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39073 / JCM 9320;
RX PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT thermoaceticum).";
RL Environ. Microbiol. 10:2550-2573(2008).
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; CP000232; ABC20750.1; -; Genomic_DNA.
DR RefSeq; WP_011393945.1; NC_007644.1.
DR RefSeq; YP_431293.1; NC_007644.1.
DR AlphaFoldDB; Q2RFN9; -.
DR SMR; Q2RFN9; -.
DR STRING; 264732.Moth_2468; -.
DR PRIDE; Q2RFN9; -.
DR EnsemblBacteria; ABC20750; ABC20750; Moth_2468.
DR KEGG; mta:Moth_2468; -.
DR PATRIC; fig|264732.11.peg.2686; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_9; -.
DR OMA; FMTWEGY; -.
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; -; 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; 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..1141
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000237304"
FT REGION 1063..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1077
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1141
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1141 AA; 127977 MW; 35E6AC4D9F8DECF3 CRC64;
MAYPVKVGAR ERWTFAKIKE TLELPNLIEI QRNSYQWFID TGLRELFHDI SPIQDFTGNL
ILQFVDYSLG EPKYSEDECK ERDMTYAAPL RVKVRLINRE TGEVKEQEVF MGDFPLMTDK
GTFIINGAER VIVSQLVRSP GAYYAEGIDA SGTKVYGATV IPNRGAWLEF ETDNTESIYV
RIDRTRKIPV TILLRALGYN TNARILELFD YDGRIQNTLE KDNTESEEEA LVEIYKRLRP
GEPPTVDSAR NLLESLFFDP RRYDLGNVGR YKLHKKFNHG ILTREVDGRE EYIRTLTKED
IIYTIKYLLR LMDGEVKPDD IDHLGNRRLR SVGELLQNQF RIGLARMERV VRERMTIQDV
DVITPQVLIN IRPVVAAIKE FFGSSQLSQF MDQTNPLAEL THKRRLSALG PGGLSRERAG
FEVRDVHTSH YGRMCPIETP EGPNIGLIGS LSTYARINEF GFIETPYRRV DKEKGIVTNQ
VDYLTADEED KYFIAQANAP LDEEGHFLEK RVNARHGGEI LVVPASQVDY MDVSPKQMVS
VATALIPFLE HDDANRALMG ANMQRQAVPL LRTEAPIVGT GMEWRAARDS GTVVLARNNG
VVERVTAREI VIRTDNGHLE TYRLQKFVRS NQGTCINQKP IVRKGERVSA GQTIADGPST
DQGELALGRN ILVAFMTWEG YNYEDAILIS EKLVKDDIFT SIHIEEYECD ARDTKLGPEE
ITRDIPNVSE DVLKDLDERG IIRIGAEVRP GDILVGKVTP KGETELTAEE RLLRAIFGEK
AREVRDTSLR VPHGESGIVV DVKVFSRENG DELAPGVNEL VRVYIAQKRK ISVGDKMAGR
HGNKGVISRI LPEEDMPFLP DGTPIEIVLN PLGVPSRMNL GQILETHLGR AARALGITVA
TPVFDGATEE EIKEAFRKAG LPEDGKTILY DGRTGEPFDR PITVGYMYML KLAHLVDDKI
HARSTGPYSL VTQQPLGGKA QFGGQRFGEM EVWALEAYGA AYTLQEILTV KSDDVVGRVK
TYEAIVKGEN VPEPGVPESF KVLIKELQSL GLDVKVLSEE NEEIEIKEDD DDVSESAQEL
GLDVHGQPNT APESEGGNEE DKEAEADEDF DPADLDPSEL ELDADLNDDL VVPDEAYGDE
E
