RPOB_STRPC
ID RPOB_STRPC Reviewed; 1197 AA.
AC Q1JNX8;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 88.
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=MGAS9429_Spy0083;
OS Streptococcus pyogenes serotype M12 (strain MGAS9429).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=370551;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS9429;
RX PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R.,
RA Musser J.M.;
RT "Molecular genetic anatomy of inter- and intraserotype variation in the
RT human bacterial pathogen group A Streptococcus.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABF31271.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CP000259; ABF31271.1; ALT_FRAME; Genomic_DNA.
DR AlphaFoldDB; Q1JNX8; -.
DR SMR; Q1JNX8; -.
DR EnsemblBacteria; ABF31271; ABF31271; MGAS9429_Spy0083.
DR KEGG; spk:MGAS9429_Spy0083; -.
DR HOGENOM; CLU_000524_4_1_9; -.
DR Proteomes; UP000002433; 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; -; 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..1197
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300410"
SQ SEQUENCE 1197 AA; 133791 MW; EFB37C99BAB80758 CRC64;
MAGHEVRYGK HRTRRSFSRI KEVLDLPNLI EIQTDSFQDF LDSGLKEVFE DVLPISNFTD
TMELEFVGYE FKEPKYTLEE ARIHDASYSA PIFVTFRLVN KETGEIKTQE VFFGDFPIMT
EMGTFIINGG ERIIVSQLVR SPGVYFNDKV DKNGKVGYGS TVIPNRGAWL ELETDSKDIA
YTRIDRTRKI PFTTLVRALG FSGDDEIVDI FGESDLVRNT IEKDIHKNPS DSRTDEALKE
IYERLRPGEP KTADSSRSLL IARFFDARRY DLAAVGRYKV NKKLNIKTRL LNQIIAENLV
DAETGEILVE AGTEMTRSVI ESIEEHLDGD LNKFVYTPND YAVVTEPVVL QKFKVVSPID
PDRVVTIVGN ANPDDKVRAL TPADILAEMS YFLNLAEGLG KVDDIDHLGN RRIRAVGELL
ANQFRIGLAR MERNVRERMS VQDNDVLTPQ QIINIRPVTA AVKEFFGSSQ LSQFMDQHNP
LSELSHKRRL SALGPGGLTR DRAGYEVRDV HYTHYGRMCP IETPEGPNIG LINNLSSFGH
LNKYGFIQTP YRKVDRATGR VTNEIVWLTA DEEDEYTVAQ ANSKLNEDGT FAEEIVMGRH
QGNNQEFSAS VVDFVDVSPK QVVAVATACI PFLENDDSNR ALMGANMQRQ AVPLIDPKAP
YVGTGMEYQA AHDSGAAVIA QHNGKVVFSD AEKVEIRRQD GSLDVYHITK FRRSNSGTAY
NQRTLVKVGD IVEKGDFIAD GPSMENGEMA LGQNPVVAYM TWEGYNFEDA VIMSERLVKE
DVYTSVHLEE FESETRDTKL GPEEITREIP NVGEEALKDL DEMGIIRIGA EVKEGDILVG
KVTPKGEKDL SAEERLLHAI FGDKSREVRD TSLRVPHGGD GIVRDVKIFT RANGDELQSG
VNMLVRVYIA QKRKIKVGDK MAGRHGNKGV VSRIVPKGVV SRIVPVEDMP YLPDGTPVDI
MLNPLGVPSR MNIGQVMELH LGMAARNLGI HIATPVFDGA SSEDLWDTVR EAGMDSDAKT
VLYDGRTGEP FDNRVSVGVM YMIKLHHMVD DKLHARSVGP YSLVTQQPLG GKAQFGGQRF
GEMEVWALEA YGASNVLQEI LTYKSDDVTG RLKAYEAITK GKPIPKPGVP ESFRVLVKEL
QSLGLDMRVL DEDDNEVELR DLDEGEDDDI MHVDDLEKAR EKQAQETQEV SETTDEK
