RPOB4_ENTFC
ID RPOB4_ENTFC Reviewed; 1208 AA.
AC Q8GCR3;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 76.
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};
OS Enterococcus faecium (Streptococcus faecium).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1352;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=38-15;
RA Enne V.I., Bennett P.M.;
RT "Rifampin resistance and its fitness cost in Enterococcus faecium.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
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; AY167141; AAO00731.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8GCR3; -.
DR SMR; Q8GCR3; -.
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..1208
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000047902"
SQ SEQUENCE 1208 AA; 135006 MW; 99E0F2D093AE7BF6 CRC64;
MKSLAGHVVK YGKHRERRSF ARISEVLELP NLIEIQTDSY QWFLDEGLRE MFEDILPIDD
FNGNLSLEFV DYELKEPKYT VAEARAHDAN YSAPLHVTLR LTNRETGEIK AQEVFFGDFP
LMTEQGTFII NGAERVIVSQ LVRSPGVYFH GKVDKNGKEG FGSTVIPNRG AWLEMETDAK
DISYVRIDRT RKIPLTVLVR ALGFGSDDTI FEIFGDSETL RNTVEKDLHK NASDSRTEEG
LKDVYERLRP GEPKTADSSR NLLNARFFDP KRYDLANVGR YKVNKKLDLK TRLLNLTLAE
TLVDPETGEI IVEKGTVLTH QVMETLAPFI ENGLNSVTYY PSEDGVVTDP MTVQVIKVFS
PKDPEREVNV IGNGYPEAPV KTVRPADIIA SMSYFLNLME GIGNVDDIDH LGNRRIRSVG
ELLQNQFRIG LARMERVVRE RMSIQDTETL TPQQLINIRP VVASIKEFFG SSQLSQFMDQ
TNPLGELTHK RRLSALGPGG LTRDRAGYEV RDVHYSHYGR MCPIETPEGP NIGLINSLSS
YAKVNKFGFI ETPYRRVDRQ TGRVTDQIDY LTADIEDHYI VAQANSPLNE DGTFAQDVVM
ARAQSENLEV SIDKVDYMDV SPKQVVAVAT ACIPFLENDD SNRALMGANM QRQAVPLINP
QAPWVGTGME YKSAHDSGAA LLCKHDGVVE FVDASQIRVR RDNGALDKYD ITKFRRSNSG
TSYNQRPIVH LGEKVEKGDT LADGPSMEQG EMALGQNVLS VSMTWEGYNY EDAIIMSRRL
VKDDVYTSIH IEEYESEARD TKLGPEEITR EIPNVGEDAL KDLDEMGIIR IGAEVKDGDL
LVGKVTPKGV TELSAEERLL HAIFGEKARE VRDTSLRVPH GGGGIVHDVK IFTREAGDEL
SPGVNMLVRV YIVQKRKIHE GDKMAGRHGN KGVVSRIMPE EDMPFLPDGT PIDIMLNPLG
VPSRMNIGQV LELHLGMAAR QLGIHVATPV FDGASDEDVW ETVREAGMAS EAKTVLYDGR
TGEPFDGRVS VGVMYMIKLA HMVDDKLHAR SIGPYSLVTQ QPLGGKAQFG GQRFGEMEVW
ALEAYGAAYT LQEILTSKSD DVVGRVKTYE AIVKGEPIPK PGVPESFRVL VKELQSLGLD
MRVLDIKDAE IELRDMDDED DDLITVDALT KFAEQQTAKE LEKKAAEQVE DERQDVIQNF
ETAEDKLD