RPOB_LIGS1
ID RPOB_LIGS1 Reviewed; 1199 AA.
AC Q1WVA5;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=LSL_0197;
OS Ligilactobacillus salivarius (strain UCC118) (Lactobacillus salivarius).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=362948;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCC118;
RX PubMed=16617113; DOI=10.1073/pnas.0511060103;
RA Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P.,
RA Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., Collins J.K.,
RA Higgins D., Shanahan F., Fitzgerald G.F., van Sinderen D., O'Toole P.W.;
RT "Multireplicon genome architecture of Lactobacillus salivarius.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(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; CP000233; ABD99012.1; -; Genomic_DNA.
DR RefSeq; WP_003699705.1; NC_007929.1.
DR RefSeq; YP_535095.1; NC_007929.1.
DR AlphaFoldDB; Q1WVA5; -.
DR SMR; Q1WVA5; -.
DR STRING; 362948.LSL_0197; -.
DR PRIDE; Q1WVA5; -.
DR EnsemblBacteria; ABD99012; ABD99012; LSL_0197.
DR KEGG; lsl:LSL_0197; -.
DR PATRIC; fig|362948.14.peg.274; -.
DR HOGENOM; CLU_000524_4_3_9; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000006559; 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..1199
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300334"
FT REGION 1177..1199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1199 AA; 134609 MW; 16209DD1B97CB2EE CRC64;
MNNLAGHLVK YGKHRVRRSY SRIKEVLDLP NLIEVQTDSY KWFLDEGLRE MFDDIMPIED
FQGKLSLEFV DYQLLEPKYT VEEARQHDAN YSAPLHVTLR LINHETGEIK SQDVFFGDFP
LMTKQGTFII NGAERVIVSQ LVRSPGVYFN SELDKNGRTN YGTTVIPNRG AWLEYETDAK
NVAYVRIDRT RKIPLTELIR ALGYGSDNEI VEILGSNSDS LMLTLEKDVH KNMDDSRVEE
SLKDIYERLR PGEPKTADSS RSLLTARFFD PKRYDLAPVG RYKINKKLDL KTRLLNLTVA
ETLADPDTGE IIVNKDEVID KQVMDKLAPY LARDDFKTFT FHPSEEGVVQ EPMTLQIVKV
YSPKDPEKVV NVIGNANVDI QFKHITPADI VASMNYFFNL QEGMGSTDDI DHLGNRRTRS
VGELLQNQFR IGLSRMERVV RERMSIQDTS TVTPQQLINI RPVVASIKEF FGSSQLSQFM
DQTNPLGELS HKRRFSALGP GGLTRDRAGY EVRDVHYTHY GRMCPIETPE GPNIGLINSL
SSYARINKYG FVETPYRRVS WETHKVTDKI DYLTADEEDN YVIAQANSPL NDDGSFVDDV
VMARKKDDDV EISTEKVDYM DVSPKQVVAV ATACIPFLEN DDSNRALMGA NMQRQAVPLI
KPHAPLVGTG IEYKAAHDSG VALISEHEGT VEYVDAREIR VRRDDGSLDK YKLMKFHRSN
GGKNYNQTPI VRVGDRVDAD EVLADGPAME NGELALGQNP LIAFMTWDGY NFEDAIAINE
RLVKEDVYTS IHIEEHESEA RDTKLGPEEI TREIPNVGED ALKNLDEFGI IRIGAEVKDG
DILVGKVTPK GVTELSAEER LLHAIFGEKA REVRDTSLRV PHGAGGIVQD VKIFTREGGD
ELSPGVNMMV RVYIAQKRKL QVGDKMAGRH GNKGTVSVVI PEEDMPFMPD GTPIDIMLSP
MGVPSRMNIG QVLDLHLGMA ARKLGIHVAS PVFDGARDED IWSALQEAGL PGDGKTVLYD
GRTGEAFDNR IAVGVMYYLK LAHMVDDKIH ARSIGPYSLV TQQPLGGKAQ FGGQRFGEME
VWALEAYGAA YTLQEILTYK SDDVVGRVKT YEAIVKGEPI PKPGVPESFR VLVKELQALG
MDMKVLDADK NEIELRDMDD EDDDIVNVDA LKKFAKEQEE KKAKEAEQET AEKEETKTE
