RPOB_ACIAC
ID RPOB_ACIAC Reviewed; 1374 AA.
AC A1TVT0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=Aave_4531;
OS Acidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. citrulli).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=397945;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAC00-1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT "Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1.";
RL Submitted (DEC-2006) 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; CP000512; ABM35068.1; -; Genomic_DNA.
DR RefSeq; WP_011797537.1; NC_008752.1.
DR AlphaFoldDB; A1TVT0; -.
DR SMR; A1TVT0; -.
DR STRING; 397945.Aave_4531; -.
DR PRIDE; A1TVT0; -.
DR EnsemblBacteria; ABM35068; ABM35068; Aave_4531.
DR KEGG; aav:Aave_4531; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_4; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000002596; 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; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..1374
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300269"
SQ SEQUENCE 1374 AA; 153099 MW; 81259BE0607C19B8 CRC64;
MAPTSTYSYT ERKRIRKSFG SRDSVLKVPY LLQMQKDAYT AFLQADMAPQ KRTNEGLQAA
FNAAFPIVSH NGFVEMKFVE YNLAKPAFDV RECQTRGLTF ASAVRAKVQL IIYDRESSTS
QSKVVKEVKE QEVYMGEVPL MTDKGSFIIN GTERVIVSQL HRSPGVFFEH DKGKTHSSGK
LLFSARIIPY RGSWLDFEFD PKDILYFRVD RRRKMPVTIL LKAIGLNPES ILANFFVNDN
FRLMDSGAQM EFVADRLKGE VARFDITDKS GKVVVAKDKR ITARHTRELE QSGTTHISVP
EDFLIGRVVA RNIVDGDTGE IVAKANEELT EALLKKLRSA GVQDLQVIYT NELDQGAYIS
QTLRIDETVD EFAARVAIYR MMRPGEPPTE DAVQALFQRL FYNPDTYDLS RVGRMKFNAK
IGRDESTGPM VLSNDDILAV VKILVDLRNG KGEVDDIDHL GNRRVRCVGE LAENQYRTGL
ARIEKAVKER LGQAEQEPLM PHDLINSKPI SAALKEFFGA SQLSQFMDQT NPLAEITHKR
RVSALGPGGL TRERAGFEVR DVHVTHYGRV CPIETPEGPN IGLINSLALY ARLNEYGFIE
TPYRRVVDGK VTDQIDYLSA IEEGKYVIAQ ANAALDAEGR LTGDLVSARE KGESTLLSAE
RVQYMDVSPA QIVSVAASLV PFLEHDDANR ALMGANMSRQ AVPVLRPEKP MVGTGIERVA
AVDSGTVVTA NRGGIVDYVD ATRIVVRVND DEAVAGEVGV DIYNLIKYQR SNQNTNIHQR
PIVKKGDVLA KGDVIADGAS TDLGEIAIGQ NMLIAFMPWN GYNFEDSILI SERVVAEDRY
TSIHIEELVV MARDTKLGAE EITRDIPNLS EQQLNRLDES GIIYVGAEVQ PGDTLVGKVT
PKGETTLTPE EKLLRAIFGE KASDVKDTSL RVDQGSSGTV IDVQVFTREG IQRDKRAQQI
IDDELKRFRL DLNDQLRIVE ADAFDRIEKL LNGRVANGGP QKLAKGTKID KAYLASVEKF
HWFDIRPAED EVATQLESIK NALEQTRHSF DLAFEEKRKK LTQGDELPAG VLKMVKVYLA
VKRRLQPGDK MAGRHGNKGV VSKIVPVEDM PYMADGTPAD IVLNPLGVPS RMNIGQVLEV
HLGWAGKGIG QRIGDMLRDQ AKAAEMRKFL EEVYNSRGRK EDLSVLSDDE VMAMAANLTN
GVPYATPVFD GASEAEIKDM LKLAYPDDIK ERKGLTESRT QAYLYDGRTG ERFERPTTIG
YMHYLKLHHL VDDKMHARST GPYSLVTQQP LGGKAQFGGQ RFGEMEVWAL EAYGASYVLQ
EMLTVKSDDV QGRTKVYESI VKGEHAIEAG MPESFNVLVK EIRSLGLDIE LERS
