RPOB_LACH4
ID RPOB_LACH4 Reviewed; 1213 AA.
AC A8YXJ8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=lhv_0302;
OS Lactobacillus helveticus (strain DPC 4571).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=405566;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DPC 4571;
RX PubMed=17993529; DOI=10.1128/jb.01295-07;
RA Callanan M., Kaleta P., O'Callaghan J., O'Sullivan O., Jordan K.,
RA McAuliffe O., Sangrador-Vegas A., Slattery L., Fitzgerald G.F.,
RA Beresford T., Ross R.P.;
RT "Genome sequence of Lactobacillus helveticus: an organism distinguished by
RT selective gene loss and IS element expansion.";
RL J. Bacteriol. 190:727-735(2008).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000517; ABX26529.1; -; Genomic_DNA.
DR RefSeq; WP_012211372.1; NC_010080.1.
DR AlphaFoldDB; A8YXJ8; -.
DR SMR; A8YXJ8; -.
DR STRING; 405566.lhv_0302; -.
DR EnsemblBacteria; ABX26529; ABX26529; lhv_0302.
DR KEGG; lhe:lhv_0302; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_9; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000000790; 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..1213
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000329183"
FT REGION 1169..1213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1213 AA; 135705 MW; C6EE43E3C79A499A CRC64;
MLNGHVVNYG KHRTRRSFSR IKEVLKLPNL TDVQTESYKW FLDKGIKEVF DDIMPISDFS
GKLSLEYEGY KLQKPKYTVD EARDHDATYA APMRVTLKLT NQETGEIKTQ DVFFGDLPLM
TESGSFIVNG AERVIVSQLV RSPGVYYTGD YDKNGRQIFG TTVIPNRGAW LEYETDAKNV
SFVRVDRTRK LPLTVLIRAM GIGSDSDIID MFGQSDTLQF TLDKDVHKNP ADSRVAEAIK
DIYERLRPGE PKTTDSSRSL LYARFFDPRR YDLAPVGRYK INKKLSLKNR LYGQTLAETL
ADPDTGEIIA KKDTVVTHEV MDKLAPYLDR DDFKMVTYQP SKEGVLPDPI TVQEIKVYSK
VDPEREVKLM SNGHIAEDVK HLTPADVLAS INYFFALQDK IGTTDDIDHL GNRRIRRVGE
LLQNQFRIGL ARMERVVRER MSIQDPLTVT PQQLINIRPI VASIKEFFGS SQLSQFMDQH
NPLGELTHKR RMSALGPGGL TRDRAGYEVR DVHYTHYGRL CPIETPEGPN IGLINSLASY
AIINKYGFIE TPYRRVSWKT HKVTDKIDYL TADEEDNYII AGANTPLNDD GSFKSDVILA
RQKEDNVEVT PDKIDYMDVI PKQVVSVASA CIPFLENDDS NRALMGANQQ RQAEPLINPH
GSLVGTGMEY RAAHDSGAAL IAKAAGTVEY VDANEIRIRR EDGTLDKYTL EKYRRSNNSK
SYNQTPNVKL GDHVDVSDVI ANGPTMDHGE LALGQNPLIA FMTWNMYNYE DAIMLSERLV
KDDVYTSISI EDYESEARDT KLGPEEITRE LPNIGEDALK DLDADGIVRV GAEVHDGDIL
VGKVTPKGVT ELSAEERLLH AIFGEKAHEV RDTSLRVPHG GGGIVQDVKV YTREAGDELS
PGVNTMVRVY IAQKRKIQVG DKMSGRHGNK GTVAAVVPEE DMPYLPDGTP VDICLNPMGV
PSRMNIGQLL ELHLGAAARQ LGIHVATPVF AGANENDVWD TVRQAGIDKD GKTVIYDGRT
GEPFHNRVSV GVMHYLKLTH MVDDKIHARS IGPYSLVTQQ PLGGKAQFGG QRFGEMEVWA
LEAYGAAYTL QEILTYKSDD VVGRVKAYEA IVKGERIPKP GVPESFRVLV KELQSLGLDI
RVLDMNHNEI ELRDMDEDSS EHLNIDSLSR MAEEQEKKKL AEETGKSGDK KENKKDADKP
VAPADESDDK VSK