RPOB_SYMTH
ID RPOB_SYMTH Reviewed; 1250 AA.
AC Q67JT3;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=STH3085;
OS Symbiobacterium thermophilum (strain T / IAM 14863).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC Symbiobacterium.
OX NCBI_TaxID=292459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T / IAM 14863;
RX PubMed=15383646; DOI=10.1093/nar/gkh830;
RA Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA Ikeda H., Hattori M., Beppu T.;
RT "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT that depends on microbial commensalism.";
RL Nucleic Acids Res. 32:4937-4944(2004).
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; AP006840; BAD42067.1; -; Genomic_DNA.
DR RefSeq; WP_011197200.1; NC_006177.1.
DR AlphaFoldDB; Q67JT3; -.
DR SMR; Q67JT3; -.
DR STRING; 292459.STH3085; -.
DR EnsemblBacteria; BAD42067; BAD42067; STH3085.
DR KEGG; sth:STH3085; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_9; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000000417; 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; -; 2.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 2.
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; 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; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..1250
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000224113"
FT REGION 1139..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1180
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1208..1226
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1250 AA; 139532 MW; 0AEA3C755AB24C48 CRC64;
MPKIVQAGRR QRLSFSRIDE VLEMPNLIEL QRNSYQWFLR EGLQEMFQDI SPIQDFTGNL
VLEFIDYSLG EPKYSIEECK ERDVTYAAPL RVRVRLINKE TGEVKEQEVF MGDFPLMTPT
GTFIINGAER VIVSQLVRSP GVYFSEQIDP SGKKLFFATM IPNRGAWLEF ESDVNDVIYV
RVDRTRKLPA TVLLRALGFG SDQEILDAVG DSEYIRRTLE KDSTESEEEA LIEIYKRLRP
GEPPAADNAR QLLETLFFEP KRYDLMHVGR YRLNKKLALK RRIVGTSTVD RVVHPETGEV
LAEAGVQIDK RLAEKIDEAG VDALTVRLRD GGIVRVVANG RPDIRVKTIV RQDIVAVINY
MVSLFKGLGS VDDIDHLGNR RVRSVGELLQ NQFRIGLARM ERVIKERMTI QDVDIITPQA
LINIRPVVAA VKEFFGSSQL SQFMDQTNPL AELTNKRRLS ALGPGGLSRE RAGYEVRDVH
TSHYGRMCPI ETPEGPNIGL IGALATFARI NEYGFIETPY RKVDQESGRV TDEIVYLTAD
EEDENIIAQA NEPLNPDGTF ARDRVTCRYR DEILQVPPSQ VDYMDVSPKQ VVSIATALIP
FLENDDASRA LMGSNMQRQA VPLLRTEAPY VGTGMEYRSA WDSGVCVIAE NDGVVLRATA
SEVVVQYDDM QVKKYKLTKF TRSNQGTCMN QKPIVRAGDR VRKGDVIADG PSTDQGELAL
GRNVLVAYMC YEGYNYEDAI IINERLVRED VFTSIHIEEH ECEARDTKLG PEEITRDIPN
VGEDVLKDLD ERGIIRIGAE VRPGDILVGK VTPKGETELT AEERLLRAIF GEKAREVRDT
SLRVPHGESG IVVDVKVFTR ENGDELSPGV NELVRVYMAQ KRKISQGDKM AGRHGNKGVI
SVIVPEEDMP FMPDGTPIDI ILTPLGVPSR MNIGQIMEIH LGWAAKTLGM YVASPVFDGA
NEQDIREMLL KAHLPPNGKT VLYDGKTGEP FDNEVTVGYK YMLKLHHLVD DKIHARSTGP
YSLVTQQPLG GKAQFGGQRF GEMEVWALEA YGAAYTLQEL LTVKSDDVVG RVKTYEAIVK
GENVPEPGVP ESFKVLIKEL QSLALDVKVL DESGNEIELR ELDDEMDLSD RDLEIPTLGG
AELAKPAPDA QAGEESGEAG EESEGEPEEE DVEEIDVPLD PEELEKVAGA LKNPVRAGRR
GAGGGLADDD QEMDEEDLFD EGDEDLADDV GLYRGRSRRL ADDFGDEEEE
