RPOB_GEOKA
ID RPOB_GEOKA Reviewed; 1190 AA.
AC Q5L405;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=GK0098;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
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; BA000043; BAD74383.1; -; Genomic_DNA.
DR RefSeq; WP_011229613.1; NC_006510.1.
DR AlphaFoldDB; Q5L405; -.
DR SMR; Q5L405; -.
DR STRING; 235909.GK0098; -.
DR EnsemblBacteria; BAD74383; BAD74383; GK0098.
DR KEGG; gka:GK0098; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_9; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000001172; 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..1190
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000224059"
FT REGION 1155..1190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1166..1190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1190 AA; 133490 MW; 6367713CEB15D957 CRC64;
MTGRLVQYGR HRQRRSYARI SEVLELPNLI EIQTSSYQWF LDEGLREMFR EISPIEDFSG
NLSLEFIDYS LGEPKYTVEE AKERDVTYAA PLRVKVRLIN KETGEVKEQD VFMGDFPLMT
ETGTFIINGA ERVIVSQLVR SPSVYYSDKV DKNGKRGYSA TVIPNRGAWL EYETDAKDVV
YVRIDRTRKL PVTVLLRALG FSSDQEIIDL LGDNEYLRNT LEKDNTDSTE KALIEIYERL
RPGEPPTLEN AKNLLASRFF DPKRYDLASV GRYKINKKLH IKNRLFNQRL AETIIDPETK
EVIAEAGAMI DRRTLNRLLP YLEKGVGLQT YRPAEGVVDG DISVQTIKIY APNDPDGEKV
INVIGNGFIA EDVKHITPAD IIASISYFFN LLHGVGDTDD IDHLGNRRLR SVGELLQNQF
RIGLSRMERV VRERMSIQDT NTITPQQLIN IRPVIAAIKE FFGSSQLSQF MDQTNPLAEL
THKRRLSALG PGGLTRERAG FEVRDVHYSH YGRMCPIETP EGPNIGLINS LSTYAKVNKF
GFIETPYRRV DPETGRVTDQ IDYLTADEED NYVVAQANVP LAEDGTFLEE NVVARFRGEN
IVVKRDRVDY MDVSPKQVVS AATACIPFLE NDDSNRALMG ANMQRQAVPL LEPEAPIVGT
GMEYVSAKDS GAAVICKHRG IVERVEAKEI WVRRLIEVDG KEVKGDLDKY RLLKFVRSNQ
GTCYNQRPIV KKGDIVEKGE ILADGPSMDK GELALGRNVL VAFMTWDGYN YEDAIIMSER
LVKEDVYTSI HIEEYEAESR DTKLGPEEIT RDIPNVGEDA LKNLDERGIV RIGAEVKDGD
LLVGKVTPKG MTELTAEERL LHAIFGEKAR EVRDTSLRVP HGGGGIVLDV KVFNREDGDE
LPPGVNQLVR VYIVQKRKIS EGDKMAGRHG NKGVISRILP EEDMPFLPDG TPIDIMLNPL
GVPSRMNIGQ VFELHLGMAA KKLGLHIASP VFDGATEEDV WNILEEAGLA RDAKTVLYDG
RTGEPFDNRV SVGIMYMIKL AHMVDDKLHA RSTGPYSLVT QQPLGGKAQF GGQRFGEMEV
WALEAYGAAY TLQEILTVKS DDVVGRVKTY EAIVKGENIP EPGVPESFKV LIKELQSLGM
DVTILTSDEQ EVNMENFDDD DDHAPDAIMV DVKPAEREEA GEEKDAVTKE
