RPOB_SYNJA
ID RPOB_SYNJA Reviewed; 1133 AA.
AC Q2JX64;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=CYA_0409;
OS Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone
OS A-Prime).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=321327;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA-3-3Ab;
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; CP000239; ABC98628.1; -; Genomic_DNA.
DR RefSeq; WP_011429317.1; NC_007775.1.
DR AlphaFoldDB; Q2JX64; -.
DR SMR; Q2JX64; -.
DR STRING; 321327.CYA_0409; -.
DR EnsemblBacteria; ABC98628; ABC98628; CYA_0409.
DR KEGG; cya:CYA_0409; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_3; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000008818; 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..1133
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000237319"
FT REGION 1085..1133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1133 AA; 126853 MW; 56DE3467C5CD2D03 CRC64;
MTQLAVPSPA APTLPDLVEI QRESFLWFLR EGFEEELLSF SPIVDYTGKL ELHFLPEYRP
GDPSKGYKIN KPRYDPEEAK RRDATYQAQI RVPTRLINKE TGEIKDMDVF IGELPLMTDR
GTFIINGAER VIVNQIVRSP GVYYKSELDK NGRRTYSASL IPNRGAWLKF ETDKNGLVWV
RIDKTRKLSA AVLLKALGLS DSEIYDSLRH PEFFQKTMEK EGHYSEEEAL MELYRKLRPG
EPPTVSGGQQ LLESRFFDPK RYDLGRVGRY KLNKKLNLNV AENVRVLTVT DILAVIDYLI
NLEYDIGHVD DIDHLGNRRV RSVGELLQNQ VRVGLNRLER IIRERMTVSE SENLTPASLV
NPKPLVAAIK EFFGSSQLSQ FMDQTNPLAE LTHKRRLSAL GPGGLSRERA GFAVRDIHPS
HYGRICPIET PEGPNAGLIG SLATHARVNQ YGFIESPYYR VENGVVRKDL GMVYLTADEE
DEYRVAPGDV PVDAEGRITA DLVPVRYRQE FTTAHPSEVH YVQVSPVQLI SVATSLIPFL
EHDDANRALM GANMQRQAVP LLKPDRPYVG TGLEAQAARD SGMVVVSRTS GVVTYVSADE
IVVRPDDGGD PIVYRLQKYQ RSNQDTCLNQ RPLVYAGDRV VPGQVLADGP ATEGGELALG
QNVLVAYMPW EGYNYEDAIL ISERLVYDDV FTSVHIEKYE IEARQTKLGP EEITREIPNV
GEDALRNLDE 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 DSDGQTRDVE
VDLMADVSSR HTPSRPTYES VTSEDLSPAA GGTFTLARRS REEDEDREEE DDF
