RPOB_LIMRD
ID RPOB_LIMRD Reviewed; 1202 AA.
AC A5VLL4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=Lreu_1492;
OS Limosilactobacillus reuteri (strain DSM 20016) (Lactobacillus reuteri).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=557436;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20016;
RX PubMed=21379339; DOI=10.1371/journal.pgen.1001314;
RA Frese S.A., Benson A.K., Tannock G.W., Loach D.M., Kim J., Zhang M.,
RA Oh P.L., Heng N.C., Patil P.B., Juge N., Mackenzie D.A., Pearson B.M.,
RA Lapidus A., Dalin E., Tice H., Goltsman E., Land M., Hauser L., Ivanova N.,
RA Kyrpides N.C., Walter J.;
RT "The evolution of host specialization in the vertebrate gut symbiont
RT Lactobacillus reuteri.";
RL PLoS Genet. 7:E1001314-E1001314(2011).
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; CP000705; ABQ83738.1; -; Genomic_DNA.
DR AlphaFoldDB; A5VLL4; -.
DR SMR; A5VLL4; -.
DR STRING; 557436.Lreu_1492; -.
DR PRIDE; A5VLL4; -.
DR EnsemblBacteria; ABQ83738; ABQ83738; Lreu_1492.
DR KEGG; lre:Lreu_1492; -.
DR PATRIC; fig|557436.17.peg.131; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_9; -.
DR Proteomes; UP000001991; 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..1202
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000073238"
FT REGION 1154..1202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1202 AA; 135051 MW; 469F80B3AC436C7D CRC64;
MAGHLVKYGK HRTRRSYSRI KEVLELPNLI EIQTDSYNWF MEKGLREMFD DIMPIDDFQG
KLSLEFVDYQ LLEPKYTVDE AREHDANYSA PLHVTLRLTN HETGEIKSQD VFFGDFPLMT
DQGTFIINGA ERVIVSQLVR SPGVYYSEEN DKNGRPNYGA TFIPNRGAWL EYETDAKNVS
YVRIDRTRKL PMTELIRALG FGSDDEIIDM FGGDSETLSL TLDKDVHKNA EDSRVEEALK
DIYERLRPGE PKTADSARSL LTARFFDPKR YDMAPVGRYK TNKKLMLKYR LLGQTLAETL
ADPDTGEVLA QKGDTVTKEL LNKLEPYLDR DDFKTITYTP SDEAVVTEPV KLQKILVYSK
NDPDRVVPII GNGHIPLEYK HIEPADILAS LNYFFNLQEG IGSTDDIDHL GNRRIRSVGE
LLQNQFRIGL ARMERVVRER MSIQDPDTVT PQQLINIRPV VASIKEFFGS SQLSQFMDQT
NPLGELTHKR RLSALGPGGL TRDRAGYEVR DVHYTHYGRM CPIETPEGPN IGLINSLSSY
ARVNKYGFIE TPYRRVSWKD HKVTDKIDYL TADEEDNFII AQANTPLNDD GSFVDDQVMA
RDKDDYIETS VENIDYMDVS PKQVVSVASA CIPFLENDDS NRALMGANMQ RQAVPLINPH
APLVSTGIDY KAAHDSGVAM IAKKPGTVEY VDAREVRVRE EDGTLDTYKL MKFRRSNGGK
NYNQRPIVKV GEHVDADDVL ADGPSMEQGE LALGQNPLIA FMTWQGYNFE DAIAINERLV
KDDVYTSIHI ESYESEARET KLGPEEMTRE IPNVGDDALK DLDENGIVRV GAEVHDGDIL
VGKVTPKGMT ELSAEERLLH AIFGEKSREV RDTSLRVPHG GGGIIQDVKV FTRENGDELS
PGVNTMVRVY IAQKRKIQVG DKMSGRHGNK GTVSIVVPEE DMPYMPDGTP IDIMLSPMGV
PSRMNIGQLL ELHLGMAARR LGIHMATPVF DGASDKDVWD AVRESGFPED GKTILYDGRT
GEPFENRIAV GSMHYLKLAH MVDDKIHARS TGPYSLVTQQ PLGGKAQFGG QRFGEMEVWA
LEAYGAAYTL QEILTYKSDD TVGRVRTYDA IINGQPIPKP GVPESFRVLV KELQALGLDM
KVLDGNNKEI QLKNMDEDDD EVVNVDALAK YAEEHKADDK KNEEENKSEA TSTTTDDKTN
QN
