RPOB_THIDA
ID RPOB_THIDA Reviewed; 1359 AA.
AC Q3SLQ6;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=Tbd_0398;
OS Thiobacillus denitrificans (strain ATCC 25259).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=292415;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25259;
RX PubMed=16452431; DOI=10.1128/jb.188.4.1473-1488.2006;
RA Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT anaerobic bacterium Thiobacillus denitrificans.";
RL J. Bacteriol. 188:1473-1488(2006).
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; CP000116; AAZ96351.1; -; Genomic_DNA.
DR RefSeq; WP_011310911.1; NC_007404.1.
DR AlphaFoldDB; Q3SLQ6; -.
DR SMR; Q3SLQ6; -.
DR STRING; 292415.Tbd_0398; -.
DR PRIDE; Q3SLQ6; -.
DR EnsemblBacteria; AAZ96351; AAZ96351; Tbd_0398.
DR KEGG; tbd:Tbd_0398; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_4; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000008291; 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..1359
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000224117"
SQ SEQUENCE 1359 AA; 152058 MW; 0FC12078B52F5A6D CRC64;
MAYTFTEKKR LRKSFASRTN TLPVPFLLAT QLESYRAFLQ EGRSRDERLN EGLQAAFTSI
FPIESHSKNA RLEYVSYQLG EPVFDIKECQ QRGLTYCAPL RAKVRLVIMD KEASKPTIKE
VKEQEVYMGE IPLMTPTGSF VINGTERVIV SQLHRSPGVF FEHDRGKTHS SGKLLFSARV
IPYRGSWLDF EFDAKDILFF RVDRRRKMPV TILLKALGYT PESILDAFFN KDTFYINTLG
IQFELVPERL RGEIARFDIC GKDDKVIVAK DKRITAKHIR ELDAAGVKKW AVPGEFVVGR
VLAHDVVDKD TGELVARAND EITEELLKKL AAAGIDKFQT LYTNDLDHGA FISQTLRTDD
TTDEYAAKVA IYRMMRPGEP PTEDAVNALF VNLFFSDERY DLSAVGRMKF NRRIGRDELT
GTGTLSTEDI VAVIKILVEL RNGRGEIDDI DHLGNRRVRS VGELAENQFR AGLVRVERAV
RERLSQAESD NLMPHDLINA KPVSAAIKEF FGSSQLSQFM DQTNPLSEIT HKRRVSALGP
GGLTRERAGF EVRDVHPTHY GRVCPIETPE GPNIGLINSL ALFARTNWYG FIETPYRKVV
DNKVTDEIEY LSAIEESKYV IAQANAELDA KGKFKDDLVS CRFKNEFTLS APDRIEYMDV
APAQIVSVAA SLIPFLEHDD ANRALMGSNM QRQAVPCLRP EKPFVGTGIE RTAAVDSGTV
VIAHRGGRVD YVDAGRIVIR VHDEEARAGE VGVDIYSLIK YTRSNQNTNI NQRPLVKVGD
VIARGDVIAD GASTDMGELA LGQNMLVAFM PWNGYNFEDS ILINEKVVAE DRYTSIHIEE
LSVVARDTKL GPEEITRDIS NLAERQLARL DESGIIAIGA EVEAGDVLVG KVTPKGETQL
TPEEKLLRAI FGEKASDVKD TSLKVPSGMS GVVIDVQVFT REGIERDKRA QSIIDTQLAE
YKKDLTDRMR IVEDDTFARL EKLLHLKVVN GGPKKLAKGS KISKEYLDSL NRHDWFDIRL
ADDEASRQVE SLKDSLTQKR VEFDAMFEEK KQKLTAGDEL PPGVQKMVKV YLAVKRRLQP
GDKMAGRHGN KGVVSKIVPV EDMPFMADGR PVDIVLNPLG VPSRMNIGQI LETHLGWASK
GLGEKIGQMM AAQTKSVVKE LRHFFKEVYN QSGKAEDIDN FTDDEILELG QNLQKGVPFA
SPVFDGATEE EIRRMLALAG LPEGGQVTLY DGRTGEAFDR QVTVGYKHVL KLHHLVDDKM
HARSTGPYSL VTQQPLGGKA QFGGQRFGEM EVWALEAYGA SYVLQEMLTV KSDDVNGRTK
VYENIVKGDH KIEAGMPESF NVLVKEIRSL GIDIDLERY
