RPOB_THEPX
ID RPOB_THEPX Reviewed; 1238 AA.
AC B0K5G8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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};
GN OrderedLocusNames=Teth514_0859;
OS Thermoanaerobacter sp. (strain X514).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter;
OC unclassified Thermoanaerobacter.
OX NCBI_TaxID=399726;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X514;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Hemme C., Fields M.W., He Z., Zhou J., Richardson P.;
RT "Complete sequence of Thermoanaerobacter sp. X514.";
RL Submitted (JAN-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; CP000923; ABY92161.1; -; Genomic_DNA.
DR RefSeq; WP_003868699.1; NC_010320.1.
DR AlphaFoldDB; B0K5G8; -.
DR SMR; B0K5G8; -.
DR EnsemblBacteria; ABY92161; ABY92161; Teth514_0859.
DR KEGG; tex:Teth514_0859; -.
DR HOGENOM; CLU_000524_4_1_9; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000002155; 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; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 1.
DR HAMAP; MF_01321; RNApol_bact_RpoB; 1.
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..1238
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000165831"
FT REGION 1186..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1193..1238
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1238 AA; 138833 MW; C00538F2F6DC6076 CRC64;
MVRPVQVGNK TRMSFAKIDE VLQMPDLIEV QKKSYKWFLE EGLREVFREI SPIESFTGNL
ALEFVDYRLE NNPKYSVEEC KDRDTTYAVP MKVKVRLTNR ETGEIKESEV FMGDFPLMTE
KGTFIINGAE RVIVSQLVRS PGVYYEQQFD KFGKKLISAT VIPNRGAWLE YEEDSNDIVY
VRIDRTRKVP ITVLLRALGY STDIQILDLL GEEEKLKATL DKDTTKSEEE ALIEIYKRLR
PGEPPTVESA KSLLYALFFD AKRYDLAKVG RYKFNKKLAL KARIANLKSA KKIVNPVTGE
ILVEEGEKIS KEKAEEIQNC GINVVEVLVE GKVVKVIGNN TVDINKYPMP YDVSSLNIKE
AVNLSILKEI LDNFSDEEAV INEIKNRMDE LVPKHITKDD IIATISYQLN LTHGIGSIDD
IDHLGNRRLR SVGELLQNQF RIGLARLERV VKERMTIQDV NEITPQNLIN IRPVVAAIRE
FFGSSQLSQF MDQTNPLAEL THKRRVSALG PGGLSRERAG FEVRDVHYSH YGRICPIETP
EGPNIGLIGS LTTYARVNEY GFIEAPYRRV DKTTGTVTDE IVYMTADEED EYIIAQANEP
LDENNRFINE KVVCRLKEEI IAVPPTEVDF MDVSPKQIVS VATSMIPFLE NDDANRALMG
SNMQRQAVPL IKPEAPIIGT GIEYKAAVDS GVVVLAKNDG VVEKVAADKV VIRTKDGRRD
EYNLLKFKRS NQGTCINQRP IVNEGDEVKK GQVICDGPST DHGELALGKN VLVGFMLWEG
YNYEDAILIS EELVRDDSLT SIHIEEYDAE ARDTKLGPEE ITREIPNVGE DALKDLDERG
IIRIGAEVTA GDILVGKVTP KGETELTAEE RLLRAIFGEK AREVRDTSLR VPHGESGIVV
DVKVYSRENG DELPPGVNQM VRVFVAQKRK ISVGDKMAGR HGNKGVISRI LPVEDMPFLP
DGTPLQICLN PLGVPSRMNI GQVLEVHLGL VAKALGWQIA TPVFDGATEE DIQELLAKSG
FSPDGKVQLY DGRTGEPFDN KVTVGYMYML KLHHLVDDKM HARSTGPYSL VTQQPLGGKA
QFGGQRFGEM EVWALEAYGA AHTLQEILTV KSDDVSGRVK TYEAIVKGEN IPEPGIPESF
KVLVKELQSL ALDVKVITED NQEIPLKEFE DDDDSDVPDA TLNINIEGRE DTPPEEVYEE
GYEEGFEEES EELPEDIDFE PDSFDIENDD LDLEDFDI
