RPOB_DESOH
ID RPOB_DESOH Reviewed; 1368 AA.
AC A8ZV51;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=Dole_0702;
OS Desulfococcus oleovorans (strain DSM 6200 / JCM 39069 / Hxd3).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfosudaceae; Desulfosudis.
OX NCBI_TaxID=96561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6200 / JCM 39069 / Hxd3;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Wawrik B.,
RA Richardson P.;
RT "Complete sequence of Desulfococcus oleovorans Hxd3.";
RL Submitted (OCT-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; CP000859; ABW66512.1; -; Genomic_DNA.
DR RefSeq; WP_012174131.1; NC_009943.1.
DR AlphaFoldDB; A8ZV51; -.
DR SMR; A8ZV51; -.
DR STRING; 96561.Dole_0702; -.
DR PRIDE; A8ZV51; -.
DR EnsemblBacteria; ABW66512; ABW66512; Dole_0702.
DR KEGG; dol:Dole_0702; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_7; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000008561; 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; 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..1368
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000141685"
SQ SEQUENCE 1368 AA; 152065 MW; F38F15150CC03A2C CRC64;
MSGESMLNRR IRKQFGKLDK IVEIPDLIGM QKESYGRFLQ QGVPPEKREK IGLQAIFQSV
FPIKDFTKSA SLEFVSYSFG GVKHSVAECI QRGMTYEIPV RIRVRLVVYD MDETSGTSSI
RDIKEQEIYF GAIPLMTDNG TFIINGTERV VVSQLHRSSG IFFDHDQGKT HSSGKVVYSS
RIIPVRGSWI DIEIDPKDIV HMRIDRRRKF PGTILFKALG YTVKDILDYF YTKERVFVRK
KKVFKAFSED SLRGQRATVR IKHPETGDLI VDKGRIFNKT VLKNMKSAGI DMVPIRPEDV
VGAVLAAPLA DSSTGEMLAD AGDFISEEVF ERIGELGIEE LQILFIDGAG STDSIVKTLL
LDKVNTKEEA LIDIYRRIRP GNPATPEVAQ DFIDHLFFKP DYYDLSAVGR LKLNHRLGAN
APVSLRTLRR EDLLLAVKTL IHLKNTQGPV DDIDHLGNRR VRAVGELLEN QYRIGLVRME
RAIKERMSLQ EVDALMPHDL INPKPVSAVV REFFGTSQLS QFMDQTNPLS ETTHKRRLSA
LGPGGLTRER AGFEVRDVHP SHYGRICPIE TPEGPNIGLI VSLSTYARVN GYGFIETPYR
VVKDTKVSKE IKMLPAFEEG EHPIAQANAP IGKDGRYVNP VVIARVAGEF SMIKASDVEL
MDVSPNQLVS VSASLIPFLE NDDANRALMG SNMQRQSVPL ARTSAPLVGT GVEKVVARDS
GVAVVARRPG EVVYVDSGRI VVRHDTDDKD PEAKPVTVYN LSKFIRSNQN TCFNHRPIVK
KGQRVAPGDV LADGPATEKG ELALGKNVTV AFMPWGGYNF EDSILVGETL VRDGVFTSIH
IEEFEVVARD TKLGKEEITC DIPNVGEESL VDLDESGIVR LGAEVKPGDV LVGKITPKGE
TQLSPEEKLL RAIFGEKGGN VKDTSLRVPP GVSGTVIDAK VFTRRGVEKD TRTRMIEEEE
IRVLEKNRDD EIAVIEEVTR ERLKALLTGQ KCDTPVKKGK KTILAKGDKI TAALFDEVPT
SQFEKLAVTS DSVTEQAHRV FEWYRTQVDA CREEFEARIS RYGAGEELPP GVIKMVKVYV
AMKRVLSTGD KMAGRHGNKG VVSRILPQED LPYFEDGTTV DMVLNPLGVP SRMNVGQILE
IHLGRAARVL GDQISTMLEE KKYKDLKKKL SAVFNKEIPA AEIEAMSSAR LCEFASEYKD
GVHMETPVFD GAKEAEIKAL LKEGGADETG QAILYDGRTG QPFDERITVG TMYMLKLHHL
VDDKLHARSI GPYSLVTQQP LGGKAQFGGQ RLGEMEVWAM EAYGAAYALQ EFLTVKSDDI
AGRTRMYEKI VKGQNVLDPG IPESFKVLTK EMKALGLDVT LIEQQDKE