RPOB_STRA5
ID RPOB_STRA5 Reviewed; 1191 AA.
AC Q8E239;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, 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=SAG0160;
OS Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=208435;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-611 / 2603 V/R;
RX PubMed=12200547; DOI=10.1073/pnas.182380799;
RA Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R., Radune D.,
RA Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A.,
RA Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T.,
RA Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D.,
RA Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT "Complete genome sequence and comparative genomic analysis of an emerging
RT human pathogen, serotype V Streptococcus agalactiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
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; AE009948; AAM99067.1; -; Genomic_DNA.
DR RefSeq; NP_687195.1; NC_004116.1.
DR RefSeq; WP_000907191.1; NC_004116.1.
DR AlphaFoldDB; Q8E239; -.
DR SMR; Q8E239; -.
DR STRING; 208435.SAG0160; -.
DR PRIDE; Q8E239; -.
DR EnsemblBacteria; AAM99067; AAM99067; SAG0160.
DR GeneID; 66885141; -.
DR KEGG; sag:SAG0160; -.
DR PATRIC; fig|208435.3.peg.160; -.
DR HOGENOM; CLU_000524_4_1_9; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000000821; 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; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..1191
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000047970"
FT REGION 1171..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1191 AA; 133011 MW; 89C029179626D6FE CRC64;
MAGHEVQYGK HRTRRSFSRI KEVLDLPNLI EIQTDSFQDF LDAGLKEVFE DVLPISNFTD
TMDLEFVGYE LKEPKYTLEE ARIHDASYSA PIFVTFRLVN KETGEIKTQE VFFGDFPIMT
EMGTFIINGG ERIIVSQLVR SPGVYFNDKV DKNGKVGYGS TVIPNRGAWL ELETDAKDIA
YTRIDRTRKI PFTTLVRALG FSGDDEIVDI FGDSELVRNT IEKDIHKNPS DSRTDEALKE
IYERLRPGEP KTADSSRSLL VARFFDPRRY DLAAVGRYKI NKKLNLKTRL LNQTIAENLV
DGETGEILVE AGTVMTRDVI DSIAEHIDGD LNKFVYTPND YAVVTEPVIL QKFKVVAPTD
PDRVVTIVGN SNPEDKVRAL TPADILAEMS YFLNLAEGIG KVDDIDHLGN RRIRAVGELL
ANQFRIGLAR MERNVRERMS VQDNEVLTPQ QIINIRPVTA AVKEFFGSSQ LSQFMDQHNP
LSELSHKRRL SALGPGGLTR DRAGYEVRDV HYTHYGRMCP IETPEGPNIG LINNLSSFGH
LNKYGFIQTP YRKVDRSTGA VTNEIVWLTA DEEDEFTVAQ ANSKLNEDGT FAEEIVMGRH
QGNNQEFPSS IVDFVDVSPK QVVAVATACI PFLENDDSNR ALMGANMQRQ AVPLIDPKAP
YVGTGMEYQA AHDSGAAVIA KHDGRVIFSD AEKVEVRRED GSLDVYHVQK FRRSNSGTAY
NQRTLVKVGD LVEKGDFIAD GPSMENGEMA LGQNPVVAYM TWEGYNFEDA VIMSERLVKE
DVYTSVHLEE FESETRDTKL GPEEITREIP NVGEDSLRDL DEMGIIRIGA EVKEGDILVG
KVTPKGEKDL SAEERLLHAI FGDKSREVRD TSLRVPHGGD GVVRDVKIFT RANGDELQSG
VNMLVRVYIA QKRKIKVGDK MAGRHGNKGV VSRIVPVEDM PYLPDGTPVD IMLNPLGVPS
RMNIGQVMEL HLGMAARNLG IHIATPVFDG ASSEDLWETV QEAGMDSDAK TVLYDGRTGE
PFDNRVSVGV MYMIKLHHMV DDKLHARSVG PYSLVTQQPL GGKAQFGGQR FGEMEVWALE
AYGASNVLQE ILTYKSDDVT GRLKAYEAIT KGKPIPKPGV PESFRVLVKE LQSLGLDMRV
LDEDDNEVEL RDLDEGEDDD VMHVDDLEKA RVKQEAEEKQ AEQVSEVVQE D