RPOB_SYNJB
ID RPOB_SYNJB Reviewed; 1139 AA.
AC Q2JJ19;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=CYB_2436;
OS Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium
OS Yellowstone B-Prime).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=321332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA-2-3B'a(2-13);
RX PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N.,
RA Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT "Population level functional diversity in a microbial community revealed by
RT comparative genomic and metagenomic analyses.";
RL ISME J. 1:703-713(2007).
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}.
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; CP000240; ABD03370.1; -; Genomic_DNA.
DR RefSeq; WP_011433999.1; NC_007776.1.
DR AlphaFoldDB; Q2JJ19; -.
DR SMR; Q2JJ19; -.
DR STRING; 321332.CYB_2436; -.
DR KEGG; cyb:CYB_2436; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_3; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000001938; 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..1139
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000237318"
FT REGION 1085..1139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1139 AA; 127602 MW; 9F4C19E4AA3ECBC1 CRC64;
MTQLAVPSPV APTFPDLVEI QRESFLWFLR EGFEEELLSF SPIIDYTGKL ELHFLPEYRP
GDPSKGYKIN RPRYDPEEAK RRDATYQAQI RVPTRLINKE TGEIKDMDVF IGELPLMTDR
GTFIINGAER VIVNQIVRSP GVYYKSELDK NGRRTYSASL IPNRGAWLKF ETDKNGLVWV
RIDKTRKLSA AVLLKALGLS DSEIYDNLRH PEFFQKTMEK EGPYTEEEAL MELYRKLRPG
EPPTVSGGQQ LLESRFFDPK RYDLGRVGRY KLNKKLNLNV AESVRVLTVT DILAVIDYLI
NLEYDIGHVD DIDHLGNRRV RSVGELLQNQ VRVGLNRLER IIRERMTVSE SENLTPASLV
NPKPLVAAIK EFFGSSQLSQ FMDQTNPLAE LTHKRRLSAL GPGGLSRERA GFAVRDIHPS
HYGRICPIET PEGPNAGLIG SLATHARVNQ YGFIESPYYR VENGVVRKDL GMVYLTADEE
DEYRVAPGDV PVDAEGRITA DLVPVRYRQE FTTAHPTEVH YVQVAPVQVI SVATSLIPFL
EHDDANRALM GANMQRQAVP LLKPDRPYVG TGLEAQAARD SGMVVVSRTN GVVTYVSADE
IVVRPDDGGD PIVYRLQKYQ RSNQDTCLNQ RPLVYTGDRV VAGQVLADGP ATEGGELALG
QNVLVAYMPW EGYNYEDAIL ISERLVYDDV FTSVHIEKHE IEARQTKLGP EEITREIPNV
GEDALRDLDE NGIVRIGAWV EAGDILVGKV TPKGESDQPP EERLLRAIFG EKARDVRDNS
LRVPNGERGR VVDVRIFTRE QGDELPPGAN MVVRVYIALK RKIQVGDKIA GRHGNKGIIS
RILPIEDMPY LADGTPVDVV LNPLGVPSRM NVGQVYECLL GWAAEHLGVR FKLMPFDEMH
GLEASRLTVE AKLREAREKT GKDWIFNPEG KYCGKIQVFD GRTGEPFDQP VTVGRAYMLK
LVHLVDDKIH ARSTGPYSLV TQQPLGGKAQ QGGQRFGEME VWALEAFGAA YILQELLTVK
SDDMVGRNEA LNAIVKGKPI PRPGTPESFK VLVRELQSLC LDVSVHKVEV DSEGQTHDVE
VDLMADTSNR HTPSRPTYES VTSEDLSPSP AFTRVLRTAD ANASRSLEED EDEEEEEDF
