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RPOB_THEMA
ID   RPOB_THEMA              Reviewed;        1263 AA.
AC   P29398;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 2.
DT   03-AUG-2022, entry version 140.
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=TM_0458;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=8177738; DOI=10.1093/nar/21.21.4904;
RA   Palm P., Schleper C., Arnold-Ammer I., Holz I., Meier T., Lottspeich F.,
RA   Zillig W.;
RT   "The DNA-dependent RNA-polymerase of Thermotoga maritima; characterisation
RT   of the enzyme and the DNA-sequence of the genes for the large subunits.";
RL   Nucleic Acids Res. 21:4904-4908(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-404.
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=1429627; DOI=10.1016/s0021-9258(18)50016-8;
RA   Liao D., Dennis P.P.;
RT   "The organization and expression of essential transcription translation
RT   component genes in the extremely thermophilic eubacterium Thermotoga
RT   maritima.";
RL   J. Biol. Chem. 267:22787-22797(1992).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
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; X72695; CAA51246.1; -; Genomic_DNA.
DR   EMBL; AE000512; AAD35543.1; -; Genomic_DNA.
DR   EMBL; Z11839; CAA77863.1; -; Genomic_DNA.
DR   PIR; S41466; F44466.
DR   RefSeq; NP_228268.1; NC_000853.1.
DR   RefSeq; WP_004081508.1; NZ_CP011107.1.
DR   AlphaFoldDB; P29398; -.
DR   SMR; P29398; -.
DR   STRING; 243274.THEMA_02400; -.
DR   PRIDE; P29398; -.
DR   EnsemblBacteria; AAD35543; AAD35543; TM_0458.
DR   KEGG; tma:TM0458; -.
DR   KEGG; tmw:THMA_0468; -.
DR   PATRIC; fig|243274.18.peg.472; -.
DR   eggNOG; COG0085; Bacteria.
DR   InParanoid; P29398; -.
DR   OMA; FMTWEGY; -.
DR   OrthoDB; 9601at2; -.
DR   Proteomes; UP000008183; 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; Reference proteome;
KW   Transcription; Transferase.
FT   CHAIN           1..1263
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000047984"
SQ   SEQUENCE   1263 AA;  143138 MW;  04B79368567C8237 CRC64;
     MKEISCGRRT RVSFGKSREP LPIPDLVEIQ KSSYRRFLEE GLLEVLKKFS PIYSQATRSD
     LRKSDRGFAL EFVSTRTGEP AIDPLECKAK GLTYSVPIYA TARLTDMKSG EMKEEEVFLG
     YIPYMTDRGT FIINGAERVV VNQIVVSPGL YFSSEYIDRE EYGGYFLPSR GAWLEVILDP
     YDGVLYAGLD GKKVNLFLFL KTIGYEKDED ILSLYPTYLD ADDEDSLLLH VGSILLEDIY
     DGGRKIAEKW DILTKDLAER ILMIDDINQI KIVHPIAQNT FEKMLEVVSS SSEEGEEEEE
     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 AAKNSGYVIL 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
 
 
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