RPOB_THEVB
ID RPOB_THEVB Reviewed; 1108 AA.
AC Q8DL55;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=tll0642;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
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; BA000039; BAC08193.1; -; Genomic_DNA.
DR RefSeq; NP_681431.1; NC_004113.1.
DR RefSeq; WP_011056489.1; NC_004113.1.
DR AlphaFoldDB; Q8DL55; -.
DR SMR; Q8DL55; -.
DR STRING; 197221.22294363; -.
DR EnsemblBacteria; BAC08193; BAC08193; BAC08193.
DR KEGG; tel:tll0642; -.
DR PATRIC; fig|197221.4.peg.681; -.
DR eggNOG; COG0085; Bacteria.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000000440; 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; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..1108
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000047980"
FT REGION 1081..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1108 AA; 124272 MW; D37D51F8EC0C9BCD CRC64;
MASNQIYTPP AFTLPDLVEI QRASFRWFLE EGLIEELESF SPITDYTGKI ELHFLAKDYR
LKEPKYSVDE AKRRDATYSM QMYVPTRLIN KENGNIIDQD VFIGDLPLMT DRGTFIINGA
ERVIVNQIVR SPGVYYKSET DKNGRRTYNA SLIPNRGAWL KFETDKNDLL WVRIDKTRKL
SAHVLLKALG LTDSEILERL RHPEYYQKTV EKEGKFSEEE ALIELYKKLR PGEPPTVSGG
QQLLESRFFD PKRYDLGRVG RYKLNRKLQL NIPDSVRILT PEDILAAIDY LINLEFDLGT
IDDIDHLGNR RVRSVGELLQ NQVRVGLNRL ERIIRERMTV SDTDSLTPTS LVNPKPLVAA
IKEFFGSSQL SQFMDQTNPL AELTHKRRLS ALGPGGLTRE RAGFAVRDIH PSHYGRICPI
ETPEGPNAGL IGSLATHARV NEYGFIETPF YPVKDGRVLK DQPPIYMTAD EEDDKRVAPG
DVPTDENGYI LGDVVPVRYR QDFTTTTPDQ VDYVAVSPVQ IISVATSLIP FLEHDDANRA
LMGSNMQRQA VPLLRPQRPL VGTGLEAQAA RDSGMVILSQ TNGVVSYVDA NQIRVKTDNG
PEITYTLQKY QRSNQDTCLN QRPIVFVGDR VQAGQVIADG SATEGGELAL GQNILVAYMP
WEGYNYEDAI LISERLVQED VYTSIHIEKY EIEARQTKLG PEEITREVPN VSEEALRQLD
ENGIIRIGAF VEAGDILVGK VTPKGESDQP PEEKLLRAIF GEKARDVRDN SLRVPNGEKG
RVVDVRVFTR EQGDELPPGA NMVVRVYVAQ KRKIQVGDKM AGRHGNKGII SRILPVEDMP
FLPDGRPVDI VLNPLGVPSR MNVGQVYECL LGWAGACLGR RFKITPFDEM HGKEKSRETV
HAKLQEARDV TGQDWVFNPE NPGKMVVYDG RTGEPFDRPV TVGMAYMLKL VHLVDDKIHA
RSTGPYSLVT QQPLGGKAQQ GGQRFGEMEV WALEAYGAAY ILQELLTVKS DDMQGRNEAL
NAIVKGQSIP RPGTPESFKV LMRELQSLCL DISVRKASIP SFDDDGEMKP DPEVDLMVDV
SPRRTPARPT IDYSALDDTD DKEGATTF
