RPOB_TRIV2
ID RPOB_TRIV2 Reviewed; 1117 AA.
AC Q3M5D0;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=Ava_4207;
OS Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX NCBI_TaxID=240292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29413 / PCC 7937;
RX PubMed=25197444; DOI=10.4056/sigs.3899418;
RA Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL Stand. Genomic Sci. 9:562-573(2014).
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: In cyanobacteria the RNAP catalytic core is composed of 2
CC alpha, 1 beta, 1 beta', 1 gamma and 1 omega subunit. When a sigma
CC factor is associated with the core the holoenzyme is formed, which can
CC initiate transcription. {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; CP000117; ABA23806.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3M5D0; -.
DR SMR; Q3M5D0; -.
DR STRING; 240292.Ava_4207; -.
DR EnsemblBacteria; ABA23806; ABA23806; Ava_4207.
DR KEGG; ava:Ava_4207; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_3; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000002533; 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; 1.
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..1117
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000237294"
FT REGION 1094..1117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1117 AA; 124943 MW; A097E6E8E4BB830D CRC64;
MISENYIEPA FLLPDLIEIQ RSSFRWFLEE GLIEELNSFS PITDYTGKLE LHFLGHNYKL
KEPKYSVEEA KRRDSTYAVQ MYVPTRLLNK ETGDIKEQEV FIGDLPLMTD RGTFIINGAE
RVIVNQIVRS PGVYYKSEID KNGRRTYSAS LIPNRGAWLK FETDRNDLVW VRIDKTRKLS
AQVLLKALGL SDNEIFDALR HPEYFQKTIE KEGQFSEEEA LMELYRKLRP GEPPTVLGGQ
QLLDSRFFDP KRYDLGRVGR YKLNKKLRLS VPDTVRVLTS GDILAAVDYL INLEYDIGSI
DDIDHLGNRR VRSVGELLQN QVRVGLNRLE RIIRERMTVS DAEVLTPASL VNPKPLVAAI
KEFFGSSQLS QFMDQTNPLA ELTHKRRLSA LGPGGLTRER AGFAVRDIHP SHYGRICPIE
TPEGPNAGLI GSLATHARVN QYGFLETPFR PVENGRVRFD QPAVYMTADE EDDLRVAPGD
IPVDENGHII GPQVPVRYRQ EFSTTTPEQV DYVAVSPVQI VSVATSMIPF LEHDDANRAL
MGSNMQRQAV PLLKPERPLV GTGLEAQGAR DSGMVIVSRT DGDVVYVDAT EIRVRVSGQL
PAASGKSTDN GQLTSQKGQE IRYTVSKYQR SNQDTCLNQK PLVRIGERVV AGQVLADGSS
TEGGELALGQ NIVVAYMPWE GYNYEDAILI SERLVQDDIY TSIHIEKYEI EARQTKLGPE
EITREIPNVG EDALRQLDEQ GIIRIGAWVE AGDILVGKVT PKGESDQPPE EKLLRAIFGE
KARDVRDNSL RVPNGEKGRV VDVRLFTREQ GDELPPGANM VVRVYVAQKR KIQVGDKMAG
RHGNKGIISR ILPIEDMPYL PDGSPVDIVL NPLGVPSRMN VGQVFECLLG WAGHTLGVRF
KITPFDEMYG EESSRRIVHG KLQEARDETG KDWVYNPDDP GKIMVFDGRT GEPFDRPVTI
GVAYMLKLVH LVDDKIHARS TGPYSLVTQQ PLGGKAQQGG QRFGEMEVWA LEAFGAAYTL
QELLTVKSDD MQGRNEALNA IVKGKAIPRP GTPESFKVLM RELQSLGLDI AVHKVETQAD
GSSLDVEVDL MADQLARRTP PRPTYESLSR ESLDDDE
