RPOB_LACAC
ID RPOB_LACAC Reviewed; 1213 AA.
AC Q5FM97;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=LBA0284;
OS Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=272621;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700396 / NCK56 / N2 / NCFM;
RX PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA Hamrick A., Cano R., Klaenhammer T.R.;
RT "Complete genome sequence of the probiotic lactic acid bacterium
RT Lactobacillus acidophilus NCFM.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
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; CP000033; AAV42177.1; -; Genomic_DNA.
DR RefSeq; WP_011254108.1; NC_006814.3.
DR RefSeq; YP_193208.1; NC_006814.3.
DR AlphaFoldDB; Q5FM97; -.
DR SMR; Q5FM97; -.
DR STRING; 272621.LBA0284; -.
DR PRIDE; Q5FM97; -.
DR EnsemblBacteria; AAV42177; AAV42177; LBA0284.
DR GeneID; 56941890; -.
DR KEGG; lac:LBA0284; -.
DR PATRIC; fig|272621.13.peg.269; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_9; -.
DR OMA; FMTWEGY; -.
DR BioCyc; LACI272621:G1G49-278-MON; -.
DR Proteomes; UP000006381; 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..1213
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000224064"
FT REGION 1153..1213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1213 AA; 135822 MW; 4743C6A770CF066D CRC64;
MLNGHVVNYG KHRTRRSFSR IKEVLKLPNL TDVQTESYKW FLDKGIKEVF DDIMPISDFS
GKLSLEYVGY KLQKPKYTVD EARDHDATYA APMHVTLKLT NQETGEIKTQ DVFFGDLPLM
TESGSFIVNG AERVIVSQLV RSPGVYYTGD YDKNGRQIFG TTVIPNRGAW LEYETDAKNV
SYVRVDRTRK LPLTVLIRAM GIGSDSEIIE MFGQSDTLQF TLDKDVHKNP ADSRVAEALK
DIYERLRPGE PKTTDSSRSL LYARFFDPRR YDLAPVGRYK INKKLSLKNR LYGQTLAETL
ADPDTGEIIV KKDTVVTHEI MDKLAPYLDR DDFKMVTYQP SKEGVLPDPI TVQEIKVYSK
VDPEREVKLM SNGHIDADVK HLTPADVLAS INYFFALQDK IGTTDDIDHL GNRRIRRVGE
LLQNQFRIGL ARMERVVRER MSIQDPSTVT PQQLINIRPI VASIKEFFGS SQLSQFMDQH
NPLGELTHKR RMSALGPGGL TRDRAGYEVR DVHYTHYGRL CPIETPEGPN IGLINSLASY
AIINKYGFIE TPYRRVSWDT HKVTDKIDYL TADEEDNYII AGANTPLNDD GSFKEDIILA
RQKEDNVEVT PDKIDYMDVI PKQVVSVASA CIPFLENDDS NRALMGANQQ RQAAPLINPH
SSLVGTGMEY RAAHDSGAAL IAKAAGTVEY VDADEIRIRR EDGTLDKYTL EKYRRSNNSK
SYNQTPNVKL GDHVDESDVI ANGPTMDHGE LALGQNPLIA FMTWNMYNYE DAIMLSERLV
KDDVYTSISI EDYESEARDT KLGPEEITRE LPNIGEDALK DLDADGIVRV GAEVHDGDIL
VGKVTPKGVT ELSAEERLLH AIFGEKAREV RDTSLRVPHG GGGIVQDVKV YTREAGDELS
PGVNTMVRVY IAQKRKIQVG DKMSGRHGNK GTVAAVMPEE DMPYLPDGTP VDICLNPMGV
PSRMNIGQLL ELHLGAAARQ LGIHVATPVF DGANENDVWD TVRQAGMDKD GKTVIYDGRT
GEPFHNRVSV GVMHYLKLTH MVDDKIHARS IGPYSLVTQQ PLGGKAQFGG QRFGEMEVWA
LEAYGAAYTL QEILTYKSDD VVGRVKAYEA IVKGERIPKP GVPESFRVLV KELQSLGLDI
RVLDMDHNEI ELRDMDEDSS EHLNIDTLSR MAEEQEKKKL AEETGKSENK EDSNETADKP
VAPADESDGK VSK
