RPOB_CLOTE
ID RPOB_CLOTE Reviewed; 1236 AA.
AC Q890N4;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=CTC_02609;
OS Clostridium tetani (strain Massachusetts / E88).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=212717;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Massachusetts / E88;
RX PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA Gottschalk G.;
RT "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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; AE015927; AAO37062.1; -; Genomic_DNA.
DR RefSeq; WP_011100723.1; NC_004557.1.
DR AlphaFoldDB; Q890N4; -.
DR SMR; Q890N4; -.
DR STRING; 212717.CTC_02609; -.
DR EnsemblBacteria; AAO37062; AAO37062; CTC_02609.
DR GeneID; 64179933; -.
DR KEGG; ctc:CTC_02609; -.
DR HOGENOM; CLU_000524_4_0_9; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000001412; 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; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..1236
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000047886"
FT REGION 1185..1236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1188..1207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1219..1236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1236 AA; 138903 MW; 23F8B82A4C2C1F71 CRC64;
MVHPVQVGKR TRMSFSKIKE VCEMSNLIEV QLDSYEWFLQ EGLQEVFDDI NPIQDYTGNL
SLEFVGYKLD MENIKYSVEE CKERDATYAA PLKVSVRLIN KETGEIKEQD VFMGDFPLMT
EQGTFIINGA ERVIVSQLVR SPGVYYDVSL DKSGKELFSA TVIPNRGAWL EYETDSNDII
YVRIDKTRKL PISILIRALE YGSDLEIIDY FGEDERLKAS IEKDNTKTKE EALLEIYKRL
RPGEPPTVDS AMSLIGSLFF DAKRYDLSRV GRYKFNKKLA LHLRIANQIS AQDIVNPATG
EIVVQEGEKI DRDKAIEIQN SGINSVDIQL DDKVLRVIGN NFVDIKSFVK FDIDDLNIKE
YVHYPTLKEI LDNYSDEEMI KEQIKKNINV LIPKHIIRDD IMSTISYEIG LPYGIGYTDD
IDHLGNRRLR SVGELLQNQF RIGLSRMERV VKERMTIQDQ DSITPQALIN IRPVTASIKE
FFGSSQLSQF MDQTNPLSEL THKRRLSALG PGGLSRERAG FEVRDVHHSH YGRMCPIETP
EGPNIGLINS LATYAKVNEY GFIETPYRKV DKATGVVTHD IIYMTADEED HYLIAKANEI
LNDDGTFIDD KITVRDQEDV LVVPKEEVDF MDVSPRQLVS VATAMIPFLE NDDASRALMG
SNMQRQAVPL LKPEAPIVGT GIEYKAAVDS AVLPKAKKPG VVTYVSASEI RVKKDKPDSN
GDVDKYKLLK FKRSNQGTCI NQKPLVSKGD KVDTKTVLAD GPSTDLGEIA LGKNIRMGFI
TWEGYNYEDA MLISEELVRE DVFTSIHIEE YEAEARDTKL GPEEITRDIP NVGEDALKDI
DERGIIRIGA EVRSGDILVG KVTPKGETEL TAEERLLRAI FGEKAREVRD TSLRVPHGEA
GIIVDVKVFT RENGDELSPG VNKLVRCYIA QKRKISVGDK MAGRHGNKGV ISRVLPEEDM
PFLPDGRPLQ ICLNPLGVPS RMNIGQVLEV HLGLAASKLG WHVATPVFDG ATEPEIVECL
EKAGYEGDGK TVLYDGRTGE PFDNRVTVGY MYILKLAHLV DDKIHARSTG PYSLVTQQPL
GGKAQFGGQR FGEMEVWALE AYGAAHTLQE ILTVKSDDVV GRVKTYEAIV KGENIPEPGV
PESFKVLIKE LQALCLDVKV LNDDNEEIAI KELADDDMVE LEVNIEGSED YTEPKQPNDN
YLEEEENKDK ESDYDEDLNF DDLTKGLQLD DFNDEH
