RPOB_THEFY
ID RPOB_THEFY Reviewed; 1155 AA.
AC Q47LI5;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=Tfu_2654;
OS Thermobifida fusca (strain YX).
OC Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC Thermobifida.
OX NCBI_TaxID=269800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YX;
RX PubMed=17209016; DOI=10.1128/jb.01899-06;
RA Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G.,
RA Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B.,
RA Kyrpides N.;
RT "Genome sequence and analysis of the soil cellulolytic actinomycete
RT Thermobifida fusca YX.";
RL J. Bacteriol. 189:2477-2486(2007).
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; CP000088; AAZ56687.1; -; Genomic_DNA.
DR RefSeq; WP_011293077.1; NC_007333.1.
DR AlphaFoldDB; Q47LI5; -.
DR SMR; Q47LI5; -.
DR STRING; 269800.Tfu_2654; -.
DR PRIDE; Q47LI5; -.
DR EnsemblBacteria; AAZ56687; AAZ56687; Tfu_2654.
DR KEGG; tfu:Tfu_2654; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_11; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
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; -; 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; 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; 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..1155
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000224115"
SQ SEQUENCE 1155 AA; 128814 MW; 21DD80564DC1098A CRC64;
MAASRIASAN ALGPNRVSFA RIKEPLEVPN LLALQTESFD WLLGNERWRA RVEAARKAGR
KDIPEQSGLE EIFEEISPIE DFSGTMSLSF RDHRFEPPKY SEEECKDKDM TYSAPMFVTA
EFINNDTGEI KSQTVFMGDF PLMTAKGTFI INGTERVVVS QLVRSPGVYF DSQMDKSSDK
ELYGCKIIPS RGAWLEFEID KRDFVGVRID RKRKQAVTIL LKALGWTTDQ ILERFGEYES
IRATLEKDPT AGTDDALLDI YRKLRPGEPP TKEAAQALLE NLYFNPKRYD LAKVGRYKIN
KKLGLEIDIT QGTLTEEDIV ATVDYLVRLH AGEKELVRPH GTFPIEVDDI DHFGNRRLRT
VGELIQNQVR LGLARMERVV RERMTTQDVE AITPQTLINI RPVVASIREF FGTSQLSQFM
DQTNPLAGLT HKRRLSALGP GGLSRERAGF EVRDVHPSHY GRMCPIETPE GPNIGLIGSL
AAYARVNSFG FIETPYRKVV DGRITDEVVY LTADEEDRYV IAQANTPVNP DGTFAESQVL
ARRKGGEFES VAAEEVHYMD ISPRQMVSVA TAMIPFLEHD DANRALMGSN MQRQAVPLLR
AEAPLVGTGM EYRAATDAGD VILAEKSGVV EDVTADYITV LADDGTRKTY RVHKFRRTNQ
GTCFNQRPIV EEGQRVEEGQ VLADGPSTEA GEMALGKNLL VAYMSWEGHN YEDAIVLSQR
LVEEDILSSI HIEEHEVDAR ETKLGPEEIT REIPNVSEEV LADLDERGII RIGAEVVDGD
ILVGKVTPKG ETELTPEERL LRAIFGEKAR EVRDTSLKVP HGESGKVIGV RVFSREEGDE
LPPGVNELVR VYVAQKRKIT DGDKLAGRHG NKGVIAKILP KEDMPFLEDG TPVDIVLNPL
GVPGRMNIGQ IMEMHLGWLA KHGWKVEGDD AEWKRRLRDI GAHEAPPNSK VATPVFDGAR
EDEISGLLSC VLPDQDGDIL VNKFGKAKLY DGRTGEPFKE PVAVGYAYFL KLHHLVDDKI
HARSTGPYSM ITQQPLGGKA QFGGQRFGEM EVWALEAYGA AYALQELLTI KSDDINGRVK
VYEAIVKGEN IPEPGIPESF KVLIKEMQSL CLNVEVLSRD GMSIEMRDSE EDVFRAAEEL
GIDLGRREPS SVEEV
