RPOB_DESRM
ID RPOB_DESRM Reviewed; 1145 AA.
AC A4J103;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=Dred_0207;
OS Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS (Desulfotomaculum reducens).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=349161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1160 / DSM 100696 / MI-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT "Complete sequence of Desulfotomaculum reducens MI-1.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta'
CC and 1 omega subunit. When a sigma factor is associated with the core
CC the holoenzyme is formed, which can initiate transcription.
CC {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; CP000612; ABO48756.1; -; Genomic_DNA.
DR AlphaFoldDB; A4J103; -.
DR SMR; A4J103; -.
DR STRING; 349161.Dred_0207; -.
DR EnsemblBacteria; ABO48756; ABO48756; Dred_0207.
DR KEGG; drm:Dred_0207; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_9; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000001556; 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; -; 2.
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; 2.
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..1145
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000073237"
FT REGION 1101..1145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1114..1145
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1145 AA; 129390 MW; 3B1249DD9C3C0B31 CRC64;
MAYPEKVGNR VRWNYGKLRE VLDLPNLIEV QRNSYEWFLQ EGLREVFHDI SPIQDFTGNL
ILEFLDYTLG EPKYSVEECK ERDVTYAAPL RVKVRLINKE TGEVKEQEVF MGDFPLMTSK
GTFIINGAER VIVSQLVRSP GVYFADQIDP SGKRLFATTM IPNRGAWLEF ETDVNDHIFV
RIDRTRKIPA TVLIRALGYG SNALIMELFE NDKFVQETLT RDNTDTEEEA LVEIYKRLRP
GEPPTVESAR SLLNTLFFDP KRYDLAHVGR YKLQKKLKHG ILYRYPNGEE GPKEWDRLLN
KEVPVDREFI RELTKEDIIA TFRYLLNLMQ GEGIVDDIDH LGNRRLRSVG ELLQNQFRIG
LSRMERVVRE RMTIQDVDVI TPQVLINIRP VVASIKEFFG SSQLSQFMDQ TNPLAELTHK
RRLSALGPGG LSRERAGFEV RDVHHSHYGR MCPIETPEGP NIGLIGSLST YARINSFGFM
EAPYRKVDKE NKRVTDEIVY LTADEEEDHI IAQANAPLDE NGYFVEERVN ARRGHDTLLV
PTDRVEYMDV SPKQVFSVAT SLIPFLEHDD ANRALMGANM QRQAVPLLRC QAPVVGTGIE
HRAAKDSGVC IVAERGGEVV RVTATEVAVR TDEGRTDTYK LLKFTRSNQG TCINQKPIVN
KGDRVEEGQI LADGPATEQG ELALGRNILV AFMTWEGNNY EDAILISEKA VKEDFFTSIH
IEEYECDARD TKLGPEEITR DIPNVGEDIL KDLDERGIIR VGAEVRPGDI LVGKVTPKGE
TELTAEERLL RAIFGEKARE VRDTSLRVPH GEAGKIVDVK VFSRENGDEL PPGVNHLVRC
YIAQKRKISE GDKMAGRHGN KGVVARILPE EDMPFMADGT PVQIVLNPLG VPSRMNIGQV
LETHLGWAAK TLGFNVATPV FNGASEESIW ETLRRAELPE DGKTVLYDGR TGEPFDNRVT
VGYIYMIKLH HLVDDKIHAR STGPYSLVTQ QPLGGKAQFG GQRFGEMEVW ALEAYGAAYT
LQEILTVKSD DVVGRVKTYE AIVKGENVPE PGVPESFKVL IKELQSLGLD VKVLAEDEKE
IEIKEIEEDI TETAKELGIE LPEERRVSSS KEEIEEEEEV EDNSDEFDET FLEEAEDDFS
LDDED
