ID   RPOB_THEAB              Reviewed;        1172 AA.
AC   B7ICR3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=THA_1345;
OS   Thermosipho africanus (strain TCF52B).
OC   Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae; Thermosipho.
OX   NCBI_TaxID=484019;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TCF52B;
RX   PubMed=19124572; DOI=10.1128/jb.01448-08;
RA   Nesboe C.L., Bapteste E., Curtis B., Dahle H., Lopez P., Macleod D.,
RA   Dlutek M., Bowman S., Zhaxybayeva O., Birkeland N.-K., Doolittle W.F.;
RT   "The genome of Thermosipho africanus TCF52B: lateral genetic connections to
RT   the Firmicutes and Archaea.";
RL   J. Bacteriol. 191:1974-1978(2009).
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; CP001185; ACJ75790.1; -; Genomic_DNA.
DR   RefSeq; WP_012580163.1; NC_011653.1.
DR   AlphaFoldDB; B7ICR3; -.
DR   SMR; B7ICR3; -.
DR   STRING; 484019.THA_1345; -.
DR   EnsemblBacteria; ACJ75790; ACJ75790; THA_1345.
DR   KEGG; taf:THA_1345; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_3_0; -.
DR   OMA; FMTWEGY; -.
DR   OrthoDB; 9601at2; -.
DR   Proteomes; UP000002453; 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; 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; Reference proteome;
KW   Transcription; Transferase.
FT   CHAIN           1..1172
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_1000141745"
SQ   SEQUENCE   1172 AA;  132196 MW;  3FF4E81F5FB0D67E CRC64;
     MKEIKSGKRT RFSFGRVQAP IPVPNLVEIQ TKSYQDFLEN GILKVLKKFS PITSSKSDLR
     KEKGFSLEFV SVRVGEPQNT VQECKERLLT YTVPVYTTVR ITDNSTNEMI EEEAFLGYLP
     YMTPRTTFII NGAERVVVNQ LVRSPGIYFV EEPRKTSGTR PIYVAHFLPV RGAWLEILLN
     LNDEVFYARI DRKRRVNLFL LLKALGYSDD LKLLSLFPQW IDVDDEYTLM HSEGLVVLED
     VKTKSGELIA KRGDVITQGL IEKLANSEIE KIKVAHRYAV NTLEKLKHTY GDDVEENRAY
     IEIFRKLRPG ELPRINAAKI FLNNLYFNEE RFELSEVGRF KMNNRLEEAY RKYLIDVEGK
     SPEEVEGVKY TETSNVLTPM DIVLASRNLI EIDKHPGTMD TKDHLGNKRV RTVGELIRIE
     FERAFSKAVF MIQEKLATYT SLDKISVQSL INVRSIIATI NSFFATNPLS QFMDQTNPLA
     ELTHKRRLTA VGPGGLKRER ARFEVRDVHH SHYGRMCPIE TPEGANIGLI TSLSVYSTID
     KYGFLITPYV KVVKGKVTDE IVYLTADEEE NYKIAPSTTP VDEEGNIIPE NVTVRYEEKV
     LYVSKYDVQF LDVAPNQIVS VSTSLIPFLE HDDANRALMG SNMQRQGVPL IETEAPRVGT
     GMEWEAAKYS GTLVLAKHDG IVKKVDANKI IIHRIDENGK EMYDSMGNPV LDTYELLKFT
     RTNQDTCINQ RPIVNVGEVV KKDDPIADGP ATDMGELALG KNVLVAFVPW EGYNFEDAIL
     ISEELLEKET YTSVHIEVYE TTARDTRLGP EEITPDIPNV SKEKLRNLDE DGIIRIGAYV
     QETDILVGKV TPKSESDTTP EEKIIRSVFG EKGKEVKDSS LRVPHGIEGR VIAVHVFDKE
     KDGDLGPGVN KLIRVYVAIR KPLEVGDKLA GRHGNKGVVS KILPKEDMPF LPDGTPVQVV
     LSPLGVPSRM NVGQILETSL GWLAMLTNKW FATPVFDGAK EKDILPELYK ARKKLGLEVG
     DDENNPTGKV TLRDGRTGLE FDHPILVGYM YVMKLIHIAR DKIHARSTGP YSLIHQQPLG
     GKAQFGGQRF GEMEVWALEA YGAAHTLNEM LTVKSDDIMG RNEVYKAIMK GKNIPDPGLP
     ESFKVLVREL RGIALDVRVY DSEGNEIDIE KL