RPOB_WIGBR
ID RPOB_WIGBR Reviewed; 1342 AA.
AC Q8D233;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=WIGBR5220;
OS Wigglesworthia glossinidia brevipalpis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Wigglesworthia.
OX NCBI_TaxID=36870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12219091; DOI=10.1038/ng986;
RA Akman L., Yamashita A., Watanabe H., Oshima K., Shiba T., Hattori M.,
RA Aksoy S.;
RT "Genome sequence of the endocellular obligate symbiont of tsetse flies,
RT Wigglesworthia glossinidia.";
RL Nat. Genet. 32:402-407(2002).
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; BA000021; BAC24668.1; -; Genomic_DNA.
DR RefSeq; WP_011070326.1; NC_004344.2.
DR AlphaFoldDB; Q8D233; -.
DR SMR; Q8D233; -.
DR STRING; 36870.25166478; -.
DR PRIDE; Q8D233; -.
DR EnsemblBacteria; BAC24668; BAC24668; BAC24668.
DR KEGG; wbr:rpoB; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_6; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000000562; 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; -; 2.
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..1342
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000047996"
SQ SEQUENCE 1342 AA; 151550 MW; CD8B78F83029EEA2 CRC64;
MVYSYTERKR IRKDFGKRPQ VLDIPYLLAI QINSFKKFIE KDPEGLYGLE AAFKSIFPIK
SYSGNAELKY ISYRLGCSVF NVKECQTRGT TFSAPLRVIL QLIIYCDESK HVVKNIKEQE
VYMGEIPLMT DNGTFIINGT ERVVVSQLHR SPGVFFDSDK GKTHSSGKVL YNARIIPYRG
SWLDFEFDAK DHLFIRIDRR RKLPVTVLLK ALNFSDGEIL NIFFEKVNFF IRKKNLLMEL
IPKRLRGETA LFDICENGIT YIKKGRRITA KHIRNLENDK ISQITVPFEY IIGKVSAKNY
FDKKTEKPII TANTELTVDL MLNLFKSGYK SIETLFTNDL DHGSYISETL RIDSTTDKTS
ALIEIYRMMR PGEPPTKEAA ENLFYNLFFS EDRYDLSSVG RMKFNKSLSI NSSEGSSLLD
KFDIIEVTKK LIDIRNGKGD VDDIDHLGNR RIRSVGEMAE NQFRIGLVRV ERAVKERLSL
GDLDTIMPQD MINAKPISAA VKEFFGSSQL SQFMDQNNPL SEITHKRRIS ALGPGGLTRE
RAGFEVRDVH PTHYGRVCPI ETPEGPNIGL INSLSVYART NEYGFLETPY RCVLNGIVTN
NIHYLSAIEE GKFIIAQANT NLDKNGYFIN EFVTCRNKGE SSLFNRNQVN YMDVSTQQIV
SVGASLIPFL EHDDANRALM GANMQRQAVP TLMTEKPLIG TGMERAVAVD SGVTAVAKRG
GIVQFLDSSK IIIKVNQEEI IKEKIGIDIY HLTKYVRSNQ NTCINQTPCV CLNDVVERGD
VLADGPSTDL GELALGQNMR IAFMPWNGYN FEDSMLVSEK VVHEDRFTTI HIQELACMSR
DTKLGSEEIT SDIPNVSETS LLKLDESGIV YIGAEVKGGD ILVGKVTPKG ETQLTPEEKL
LRAIFGEKAS DVKDSSLRVP NGVSGTVIDV EIFTRDGVKK DKRALEIEYM QIKEAKKDIY
EELEIFKSSL KIQIEYFLKE NNIEYDSLSE LLKGNIKNLI FKNNNLNNIF EELINKFLRL
KEEFEKKLEI KIKKITQGDD LAPGVLKIVK VYLAVKRQIQ PGDKMAGRHG NKGVISKINP
IEDMPYDENG VPVDMVLNPL GVPSRMNIGQ ILETHLGLAA KGIGNIIDNM LKNNKKIYKI
KKFIQNAYNL GIGIRQKVEL DHFSDKEIIK LANNLRKGMP IATPVFDGAQ EIEIKELLKF
SGNPESGQIT LFDGQTGEKF DRPVTVGYMY MLKLNHLVDD KMHARSTGSY SLVTQQPLGG
KAQFGGQRFG EMEVWALEAY GAAYSLQEML TVKSDDVNGR TKMYKNIVDG SHLMEPGMPE
SFNVLLKEIR SLGINIELEE NN
