RPOB_STRE4
ID RPOB_STRE4 Reviewed; 1188 AA.
AC C0M7C8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=SEQ_0098;
OS Streptococcus equi subsp. equi (strain 4047).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=553482;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4047;
RX PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA Maskell D.J., Parkhill J., Waller A.S.;
RT "Genomic evidence for the evolution of Streptococcus equi: host
RT restriction, increased virulence, and genetic exchange with human
RT pathogens.";
RL PLoS Pathog. 5:E1000346-E1000346(2009).
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; FM204883; CAW92040.1; -; Genomic_DNA.
DR RefSeq; WP_012514773.1; NC_012471.1.
DR AlphaFoldDB; C0M7C8; -.
DR SMR; C0M7C8; -.
DR EnsemblBacteria; CAW92040; CAW92040; SEQ_0098.
DR KEGG; seu:SEQ_0098; -.
DR HOGENOM; CLU_000524_4_1_9; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000001365; 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; -; 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; 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..1188
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000165822"
SQ SEQUENCE 1188 AA; 132952 MW; B0180677D1D5A7B5 CRC64;
MAGHDVQYGK HRTRRSFSRI KEVLDLPNLI EIQTDSFQDF LDSGLKEVFE DVLPISNFTD
TMELEFVGYE FKEPKYTLEE ARIHDASYSA PIFVTFRLIN KETGEIKTQE VFFGDFPIMT
EMGTFIINGG ERIIVSQLVR SPGVYFNDKV DKNGKVGYGS TVIPNRGAWL ELETDSKDIA
YTRIDRTRKI PFTTLVRALG FSGDDEIIDI FGDSELVRNT IEKDIHKNQS DSRTDEALKE
IYERLRPGEP KTADSSRSLL TARFFDARRY DLAAVGRYKI NKKLNIKTRL LNQIIAENLI
DSETGEILVE AGTEMTRSVI ESIEEQLDGD LNKFVYTPND YAVVTEPVIL QKFKVVSPVD
PDRVVTIVGN ANPDDKVRAL TPADILAEMS YFLNLAEGLG KVDDIDHLGN RRIRAVGELL
ANQFRIGLAR MERNVRERMS VQDNDVLTPQ QIINIRPVTA AVKEFFGSSQ LSQFMDQHNP
LSELSHKRRL SALGPGGLTR DRAGYEVRDV HYTHYGRMCP IETPEGPNIG LINNLSSFGH
LNKYGFIQTP YRKVDRVIGR VTNEIVWLTA DEEDEFTVAQ ANSKLNPDGT FAEEIVMGRH
QGNNQEFPAS QVDFVDVSPK QVVAVATACI PFLENDDSNR ALMGANMQRQ AVPLIDPKAP
YVGTGMEYQA AHDSGAAVIA QHNGKVVFSD AERVEVRRED GSLDVYHITK FRRSNSGTAY
NQRTLVKIGD IVEKGDFIAD GPSMEKGEMA LGQNPIVAYM TWEGYNFEDA VIMSERLVKE
DVYTSVHLEE FESETRDTKL GPEEITREVP NVGEEALKDL DEMGIIRIGA EVKEGDILVG
KVTPKGEKDL SAEERLLHAI FGDKSREVRD TSLRVPHGGD GIVRDVKIFT RANGDELQSG
VNMLVRVYIA QKRKIKVGDK MAGRHGNKGV VSRIVPVEDM PYLPDGTPVD IMLNPLGVPS
RMNIGQVMEL HLGMAARNLG IHIATPVFDG ATSEDLWETV REAGMDSDAK TVLYDGRTGE
PFDNRVSVGV MYMIKLHHMV DDKLHARSVG PYSLVTQQPL GGKAQFGGQR FGEMEVWALE
AYGASNVLQE ILTYKSDDVN GRLKAYEAIT KGKPIPKPGV PESFRVLVKE LQSLGLDMRV
LDEDDNEVEL RDLDEGEDDD VMHVDDLEKA REKQAQETQD IAESTEDN
