RPOB_ACIET
ID RPOB_ACIET Reviewed; 1374 AA.
AC B9MH47;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=Dtpsy_3246;
OS Acidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Diaphorobacter.
OX NCBI_TaxID=535289;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TPSY;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Coates J.D.;
RT "Complete sequence of Diaphorobacter sp. TPSY.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001392; ACM34675.1; -; Genomic_DNA.
DR RefSeq; WP_015914492.1; NC_011992.1.
DR AlphaFoldDB; B9MH47; -.
DR SMR; B9MH47; -.
DR STRING; 535289.Dtpsy_3246; -.
DR EnsemblBacteria; ACM34675; ACM34675; Dtpsy_3246.
DR KEGG; dia:Dtpsy_3246; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_4; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000000450; 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..1374
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000165804"
SQ SEQUENCE 1374 AA; 153302 MW; 269F20DEB20486E8 CRC64;
MAQTSTYSYT ERKRIRKSFG SRDSVLKVPY LLQMQRDAYT AFLQADTAPQ KRSIEGLQAA
FNSAFPIVSH NGFVEMKFVE YNLAKPAFDV RECQTRGLTF ASAVRAKVQL IIYDRESSTS
QSKVVKEVKE QEVYMGEVPL MTDKGSFIIN GTERVIVSQL HRSPGVFFEH DKGKTHSSGK
LLFSARIIPY RGSWLDFEFD PKDILYFRVD RRRKMPVTIL LKAIGLNPES ILANFFVNDN
FRLMDSGAQL EFVPERLRGE VARFDITDKA GKVIVAKDKR VTARHTRELE QSGTTHISVP
EDFLIGRVVA RNIVDGDTGE ILAKANEELT EALLKKLRAA GVQDLQVIYT NELDQGAYIS
QTLRIDETVD EFAARVAIYR MMRPGEPPTE DAVQALFQRL FYNPDTYDLS RVGRMKFNAK
IGRDEATGPM VLSNDDILAV VKILVDLRNG KGEVDDIDHL GNRRVRCVGE LAENQYRTGL
ARIEKAVKER LGQAEQEPLM PHDLINSKPI SAALKEFFGA SQLSQFMDQT NPLAEITHKR
RVSALGPGGL TRERAGFEVR DVHVTHYGRV CPIETPEGPN IGLINSLALY ARLNEYGFIE
TPYRRVVDGK VTMEIDYLSA IEEGKYIIAQ ANATLDAEGR LTGDLVSARE KGESTLVSAD
RVQYMDVSPA QIVSVAASLV PFLEHDDANR ALMGANMSRQ AVPVLRPEKP MVGTGIERVA
AVDSGTVVTA NRGGVVDYVD ATRIVVRVND DEAVAGEVGV DIYNLIKYQR SNQNTNIHQR
PIVKKGDKLA KGDVIADGAS TDLGEIAIGQ NMLIAFMPWN GYNFEDSILI SERVVAEDRY
TSIHIEELVV MARDTKLGAE EITRDIPNLS EQQLNRLDES GIIYVGAEVQ PGDTLVGKVT
PKGETTLTPE EKLLRAIFGE KASDVKDTSL RVDQGSQGTV IDVQVFTREG IQRDKRAQQI
IDDELKRFRL DLNDQLRIVE ADAFDRIEKL LTGRVANGGP QKLAKGTKID KAYLASVEKF
HWFDIRPAEE EVATQLESIK NALEQTRHSF DLAFEEKRKK LTQGDELPAG VLKMVKVYLA
VKRRLQPGDK MAGRHGNKGV VSKIVPVEDM PYMADGTPAD IVLNPLGVPS RMNIGQVLEV
HLGWAGKGMG QRIGDMLQRE AKTAELRKFL EEIYNSRGRK EELSQLSDDE ILAMARELTS
GVPFASPVFD GASEEEIKDM LKLAYPDDLA QAKGLTETRT QAYLYDGRTG ERFERPTTVG
YMHYLKLHHL VDDKMHARST GPYSLVTQQP LGGKAQFGGQ RFGEMEVWAL EAYGAAYVLQ
EMLTVKSDDV QGRTKVYENI VKGEHAIEAG MPESFNVLVK EIRSLGLDIE LERS
