RPOB_THESQ
ID RPOB_THESQ Reviewed; 1263 AA.
AC B1L935;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=TRQ2_0477;
OS Thermotoga sp. (strain RQ2).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga;
OC unclassified Thermotoga.
OX NCBI_TaxID=126740;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RQ2;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D.B., Goodwin L., Pitluck S., Saunders E., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA Richardson P.;
RT "Complete sequence of Thermotoga sp. RQ2.";
RL Submitted (MAR-2008) 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; CP000969; ACB08833.1; -; Genomic_DNA.
DR RefSeq; WP_012310570.1; NC_010483.1.
DR AlphaFoldDB; B1L935; -.
DR SMR; B1L935; -.
DR EnsemblBacteria; ACB08833; ACB08833; TRQ2_0477.
DR KEGG; trq:TRQ2_0477; -.
DR HOGENOM; CLU_000524_4_0_0; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000001687; 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 Gene3D; 3.90.1110.10; -; 3.
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; 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; 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..1263
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000141746"
SQ SEQUENCE 1263 AA; 143191 MW; 6618DD28457D7AA9 CRC64;
MKEISCGRRT RVSFGKSREP LPIPDLVEIQ KISYRRFLEE GLLEVLKKFS PIYSQATRSD
LKKSDRGFAL EFVSTRIGEP VVDPLECKAK GLTYSVPIYA TARLTDMKSG EMKEEEVFLG
YIPYMTDRGT FIINGAERVV VNQIVVSPGL YFSSEYIDRE EYGGYFLPSR GAWLEVILDP
YDGVLYAGLD GKKVNLFLFL KTIGYEKDED ILSLYPTYLD ADDEDSLLLH VGSILLEDIY
DGDRKIAEKW DILTKDLAER ILMIDDINQI KIVHPIAQNT FEKMLELVSS SGEEGEEEEE
KTKIYGLNEV TVVDAYLEIF RRLRPEELPR INAAKRYLHD LFFNPERYDL SEVGRYKVNE
RLRNAYIRYL IEVEGEDPEE ARKKVYNETS LVLKPLDIVL ASRILFDYFE RRYVNDFEID
SYELKNLIRI FKEEYLEKRK TAPYDLRKLV SVFRRNYGVT SDLGVFAAIR YVSNINKELP
SIPFDTKDHL GNKRVRTVGE LVQREFERLF ARAQKAIQER LTLINSLSKV SIQSLINIKS
IISTVNQFFA MNQLSQFMDQ VNPLSELTHK RRVSAVGPGG LRRESKVFEA RNVHYSQYGR
LCPIETPEGA NIGFITSLAI YAKIDEYGFL MTPYRKVVNG KVTDEVVYLR ANEEEEYKII
PATTPVDEEG NIIPERVVAR MGEDIRLVPK EEVDFMDVST KQPFSVSASL IPFLEHDDAS
RALMGSNMQR QAVPLLKTEA PLVGTGMEWE AAKNSGYVVL AEHDGIVKEV DAARVVVHRT
DENGNLMYDD KGNPVVDEYR LLKFVRSNQD TMINQKPIVN EGDFVKKGDP IADGPATDMG
ELALGRNILV AFMPWEGYNY EDAILVSQEL LEEDVFTSIH IEVYETQARE TRLGPEEITA
DIPNVSKELL KNLDENGIIR VGAYVVSDYG VGSQAILVGK VTPKGEGDTT PEEKIIRSVF
GERGRDVKDT SLRLPHGVEG RVIRVDVYDQ NDIAELGAGV LKLVRVYVAS RKTLDIGDKL
AGRHGNKGVV SNILPKEDMP FLPDGTPVQM VLNPLGIPSR MNVGQILETH LGWLAKLTGK
WFATPVFEGA KEDEILRPLY EERKKRGLHL GDDENNPNGK VVLRDGRTGE PFDNPVVVGY
MYMLKLIHIA KEKIHARSTG PYSLIHQQPL GGKSHFGGQR LGEMEVWALE AYGAAHTLAE
MLTIKSDDIK GRNEAYKAIL KNMNIPEPGV PESFRVLIKE LRGLALDVRL YDENGNEIDI
DKY
