RPOB_STRS2
ID RPOB_STRS2 Reviewed; 1190 AA.
AC A4VYU3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=SSU98_0122;
OS Streptococcus suis (strain 98HAH33).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=391296;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=98HAH33;
RX PubMed=17375201; DOI=10.1371/journal.pone.0000315;
RA Chen C., Tang J., Dong W., Wang C., Feng Y., Wang J., Zheng F., Pan X.,
RA Liu D., Li M., Song Y., Zhu X., Sun H., Feng T., Guo Z., Ju A., Ge J.,
RA Dong Y., Sun W., Jiang Y., Wang J., Yan J., Yang H., Wang X., Gao G.F.,
RA Yang R., Wang J., Yu J.;
RT "A glimpse of streptococcal toxic shock syndrome from comparative genomics
RT of S. suis 2 Chinese isolates.";
RL PLoS ONE 2:E315-E315(2007).
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; CP000408; ABP91282.1; -; Genomic_DNA.
DR AlphaFoldDB; A4VYU3; -.
DR SMR; A4VYU3; -.
DR KEGG; ssv:SSU98_0122; -.
DR HOGENOM; CLU_000524_4_1_9; -.
DR OMA; FMTWEGY; -.
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; Transcription;
KW Transferase.
FT CHAIN 1..1190
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300416"
SQ SEQUENCE 1190 AA; 132870 MW; C02E5BD057C016F6 CRC64;
MAGHEVQYGK HRTRRSFSRI KEVLDLPNLI EIQTDSFQDF LDYGLKEVFE DVLPVSNFTD
TMELEFVGYE LKEPKYTLEE ARAHDANYSA PIYVTFRLVN KETGEIKTQE VFFGEFPIMT
EMGTFIINGA ERIIVSQLVR SPGVYFNDKV DKNGKVGYGS TVIPNRGAWL ELETDSKDIA
YTRIDRTRKI PFTTLVRALG FSGDDEIFDI FGDSELVRNT IEKDIHKNPA DSRTDEALKE
IYERLRPGEP KTAESSRSLL TARFFDPRRY DLAPVGRYKI NKKLNLRTRL LNQTLAEHVI
NGETGEIVLE AGTVLSRDVL EKVEAQFDEL NLVEYIPNDN AVLLEPVLLQ KFKIVAPKDP
ERVVTVIGNA NPAENVRTVT PADILAEMSY FLNLAEGLGR VDDIDHLGNR RIRAVGELLA
NQVRIGLTRM ERNLRERMSV QDNEVLTPQQ IINIRPVTAA IKEFFGSSQL SQFMDQHNPL
SELSHKRRLS ALGPGGLTRD RAGYEVRDVH YTHYGRMCPI ETPEGPNIGL INNLSSYGHL
NKYGFIQTPY RKIDRATGTV TNEIVWLTAD EEDAYIVAQS TSPLDENNRF VDKIVMGRHQ
GNNQEFPADS ADFMDVSPKQ VVAVATACIP FLENDDSNRA LMGANMQRQA VPLIDPKAPY
VGTGMEYQAA HDSGAAIIAQ HDGKVVYADA DKVEVRREDG SLDVYHISKF RRSNSGTAYN
QRTLVKLGDI VEKGDFIADG PSMENGEMAL GQNPIVAYMT WEGYNFEDAV IMSERLVKDD
VYTSVHLEEY ESETRDTKLG PEEITREIPN VGEDALRNLD EMGIIRIGAE VKEGDILVGK
VTPKGEKDLS AEERLLHAIF GDKSREVRDT SLRVPHGADG VVRDVKIFTR ANGDELQSGV
NMLVRVYIAQ KRKIKVGDKM AGRHGNKGVV SRIVPVEDMP YLPDGTPVDI MLNPLGVPSR
MNIGQVMELH LGMAARNLGI HIATPVFDGA SSEDLWSTVK EAGMDSDAKT ILYDGRTGEP
FDNRVSVGVM YMIKLHHMVD DKLHARSVGP YSLVTQQPLG GKAQFGGQRF GEMEVWALEA
YGASNVLQEI LTYKSDDVTG RLKAYEAITK GKPIPKPGVP ESFRVLVKEL QSLGLDMRVL
DEDNNEVELR DLDEGEDDDI IHVDDLEKAR AKAAADAAAA FAAEEAEGKE