RPOB_LACDA
ID RPOB_LACDA Reviewed; 1221 AA.
AC Q1GBM5;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=Ldb0386;
OS Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081
OS / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM
OS 00102 / Lb 14).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=390333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB
RC 11778 / NCTC 12712 / WDCM 00102 / Lb 14;
RX PubMed=16754859; DOI=10.1073/pnas.0603024103;
RA van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P.,
RA Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R.,
RA Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P.,
RA Weissenbach J., Ehrlich S.D., Maguin E.;
RT "The complete genome sequence of Lactobacillus bulgaricus reveals extensive
RT and ongoing reductive evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(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}.
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DR EMBL; CR954253; CAI97221.1; -; Genomic_DNA.
DR RefSeq; WP_011543638.1; NZ_JQAV01000001.1.
DR AlphaFoldDB; Q1GBM5; -.
DR SMR; Q1GBM5; -.
DR STRING; 390333.Ldb0386; -.
DR EnsemblBacteria; CAI97221; CAI97221; Ldb0386.
DR KEGG; ldb:Ldb0386; -.
DR PATRIC; fig|390333.7.peg.345; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_9; -.
DR OMA; FMTWEGY; -.
DR BioCyc; LDEL390333:LDB_RS01640-MON; -.
DR Proteomes; UP000001259; 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..1221
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300331"
FT REGION 1176..1221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1187..1212
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1221 AA; 135844 MW; 3A6D3D929A5E60F1 CRC64;
MLNGHVVNYG QHRTRRSFSR IKEILPLPNL TDVQTESYKW FLDEGVKEVF DDILPISDTS
GRLTLEYVDY KLQEPKYTVD ESRKHDATYS APMHVTLKLT NHETGEIKTQ DVFFGDLPLM
TKSGSFIVNG AERVIVSQLV RSPGVYYSGE FDKNGRQIFG TTVIPNRGAW LEFETDAKNI
SYVRVDRTRK LPLSVLVRAL GFGSDSEIKE IFGDSDTLDL TLDKDVHKNP ADSRVAEALK
DIYDRLRPGE PKTTDSSRSL LVSRFFDPRR YDLAAVGRYK VNKKLSLKNR LLGYTLAETL
ADPGTGEVLA AKGTVVNNEV MDVLKDYLDR DDFKTVTYTP SDEGVIPEPV TVQEIKVFSR
EIPDREIKLI SNGHIAEDVK CITPADIIAS VNYFLELQEG VGNIDDIDHL GNRRIRRVGE
LLQNQMRIGL ARMERVVRER MSIQDAATVT PQQLINIRPI VGSIKEFFGS SQLSQFMDQN
NPLGELTHKR RMSALGPGGL SRDRAGYEVR DVHYTHYGRL CPIETPEGPN IGLINSMATY
AIINKYGFLE TPYRRVSWAT HKVTDKIDYL TADEEDNYII AGANTPLNED GSFVDDVILC
RHREDNVEVS PDRIDYIDVI PKQVVSVTSA CIPFLENDDS NRALMGANHQ RQAVPLINPH
GPLVATGMEY RAGHDSGDAL LAEADGEVEY VDANEIRVRR EDQTLDTYTL EKYRRSNATK
NYNQTPNVKR GDKVVDGQVI ANGPSMADGE LALGQNPVIA FTTWNMYNFE DAIMLSERLV
KEDVYTSIHI EDYDSEARDT KLGPEEITRE IPNVGEDALK DLDENGIIRI GAEVHDGDIL
VGKVTPKGIT ELSAEERLLH AIFGEKAREV RDTSLRVPHG GGGVVQDVQV FTREAGDELA
PGVNTLVRVY IVQKRKIQVG DKMSGRHGNK GTVALIAPVE DMPYLPDGTP VDICLNPMGV
PSRMNIGQLL EIHLGRAARA LGIHVATPVF DGASEDDVWD FVREAGVDSD GKTVLYDGRT
GEPFHNRVSV GVMYYLKLTH MVDDKIHARS IGPYSLVTQQ PLGGKAQFGG QRFGEMEVWA
LEAYGAAYTL QEILTYKSDD VVGRVKAYEA IVKGERITKP GVPESFRVLV KELQSLGLDL
RVLDSDENEV ELRDMDEDSN EHVNIDALSR LAEAQEKKKL AEEEAEIAAE AEAEGSAEGD
AAEADADANE AETADDDKAS K