RPOB_GLOVI
ID RPOB_GLOVI Reviewed; 1112 AA.
AC Q7NIA0;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=glr2283;
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
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; BA000045; BAC90224.1; -; Genomic_DNA.
DR RefSeq; NP_925229.1; NC_005125.1.
DR AlphaFoldDB; Q7NIA0; -.
DR SMR; Q7NIA0; -.
DR STRING; 251221.35212851; -.
DR PRIDE; Q7NIA0; -.
DR EnsemblBacteria; BAC90224; BAC90224; BAC90224.
DR KEGG; gvi:glr2283; -.
DR PATRIC; fig|251221.4.peg.2318; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_3; -.
DR InParanoid; Q7NIA0; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR PhylomeDB; Q7NIA0; -.
DR Proteomes; UP000000557; 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..1112
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000047904"
FT REGION 1087..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1112 AA; 124478 MW; 346006CF9B26C8E4 CRC64;
MPDFRYADAL PEVRMSNALT TPNYLLPDLV EIQRESFRWF LEEGLIEELL SFSPITDYTG
KMELHFLQDY KLKEPKYSVE EAKRRDSTYS VQMYVSTRLV NKETGEIKEQ QVFIGELPLM
TDRGTFIING AERVIVNQIV RSPGVYYKQE LDTNGRKTFN ASLIPNRGAW LKFETDANDL
VWVRIDKTRK LSAVVLLKAL GLSDNEILDA FRHPEYFQKT IEKEGNYSEE EALLELYRKL
RPGEPPTVSG GQQLLETRFF DPKRYDLGRV GRYKLNKKLR LSVPETTRIL TPQDILASID
YLINLEFDIG SPDDIDHLGN RRVRSVGELL QNQVRVGLNR LERIIRERMT VSEAETLTPA
SLVNPKPLVA AIKEFFGSSQ LSQFMDQTNP LAELTHKRRL SALGPGGLTR ERAGFAVRDI
HPSHYGRICP IETPEGPNAG LIGSLATHAR VNSYGFIETP YKVVKDGRLS GEIKYLTADE
EDEFRVAAGD VAVDEGGNIL ANPVTIRYRQ EFGLASPAEV DYVAVSPIQI VSVATSLIPF
LEHDDANRAL MGANMQRQAV PLLRPERPLV GTGLEGQAAR DSGMVIVSDI DGAITYVSGE
QIRVRGENGQ EFAYPLQKYQ RSNQDTCLSQ RPIVNVGDQV RNGQILADGS ATEGGELALG
QNILVAFMPW EGYNYEDAIL ISERLVYDDV FTSIHVEKFE IEARQTKLGP EEITREIPNV
GEDSLRNLDE RGIVRIGAWM EAGDILVGKV TPKGESDQPP EEKLLRAIFG EKARDVRDNS
LRVPNGEKGR VVDVRVFTRE QGDELPPGAN MVVRVYLAQK RKVQVGDKVA GRHGNKGIIS
KILPKEDMPY LPDGRPVDIV LNPLGVPSRM NVGQVFETLL GWAGACLNVR FKVTPFDEMY
IKEASRYLVH EKLMEAREVT GDPWVYSDTG KHIGKIQVYD GRTGEAFDRP VTVGQIYMMK
LVHLVDDKIH ARSTGPYSLV TQQPLGGKAQ QGGQRFGEME VWALEAFGAA YTLQELLTVK
SDDMTGRNEA LNAIVKGKAI PRPGIPESFK VLVRELQSLG LDVSVHKIET QHDGSSRDVE
VDLMADVGGR RTPNRPTYEN IGGPREMEFS ED
