RPOB_SODGM
ID RPOB_SODGM Reviewed; 1342 AA.
AC Q2NWR6;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=SG0134;
OS Sodalis glossinidius (strain morsitans).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Bruguierivoracaceae; Sodalis.
OX NCBI_TaxID=343509;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=morsitans;
RX PubMed=16365377; DOI=10.1101/gr.4106106;
RA Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA Aksoy S.;
RT "Massive genome erosion and functional adaptations provide insights into
RT the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL Genome Res. 16:149-156(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; AP008232; BAE73409.1; -; Genomic_DNA.
DR RefSeq; WP_011409998.1; NZ_LN854557.1.
DR AlphaFoldDB; Q2NWR6; -.
DR SMR; Q2NWR6; -.
DR STRING; 343509.SG0134; -.
DR PRIDE; Q2NWR6; -.
DR EnsemblBacteria; BAE73409; BAE73409; SG0134.
DR KEGG; sgl:SG0134; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_6; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR BioCyc; SGLO343509:SGP1_RS01125-MON; -.
DR Proteomes; UP000001932; 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; Transcription;
KW Transferase.
FT CHAIN 1..1342
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000237313"
SQ SEQUENCE 1342 AA; 150366 MW; 08721A971300953A CRC64;
MVYSYTEKKR IRKDFGKRPQ VLDVSYLLSI QLDSFQKFIE RDPEGQYGLE AAFRSVFPIQ
SYSGNSELQY VSYRLGEPVF DVKECQIRGV TFSAPLRVKL RLIIYEREAP EGTVKDIKEQ
EVYMGEIPLM TDNGTFVING TERVIVSQLH RSPGVFFDSD KGKTHSSGKV LYNARIIPYR
GSWLDFEFDP KDNLFVRIDR RRKLPATIIL RALNYSTGQI LDTFFDKVVY EIHDKKLQME
LLPERLRGET ASFDIEANGT VYVEKGRRIT ARHIRQLEKD GVAQIEVPVE YIIGKAVVKD
YIDENTGEII VPANMELTLD LLAKLSQAGH KRIETLFTND LDHGAYISET LRVDPTSDRL
SALVEIYRMM RPGEPPTREA AENLFENLFF SEDRYDLSAV GRMKFNRSLL REEIEGSGIL
SKDDIIEVMK KLIDIRNGKG EVDDIDHLGN RRIRSVGEMA ENQFRVGLVR VERAVKERLS
LGDLDTLMPQ DMINAKPISA AVKEFFGSSQ LSQFMDQNNP LSEITHKRRI SALGPGGLTR
ERAGFEVRDV HPTHYGRVCP IETPEGPNIG LINSLSVYAQ TNEYGFLETP YRRVQDGVVT
DEIHYLSAIE EGNFVIAQAN TNLGDDGSFV DDLVTCRSKG ESSLFSRDQV DYMDVSTQQV
VSVGASLIPF LEHDDANRAL MGANMQRQAV PTLCTDKPLV GTGMERAVAV DSGVTAVAKR
GGTVQYVDAS RIVINVNPDE MYPGEAGIDI YNLTKYIRSN QNTCISQTPC VSLGEPVERG
DVLADGPSTD LGELALGQNM RIAFMPWNGY NFEDSMLVSE RVVQEDRFTT IHIQELACVS
RDTKLGPEEI TADIPNVGEA ALSKLDESGI VYIGAEVTGG DILVGKVTPK GETQLTPEEK
LLRAIFGEKA SDVKDSSLRV PNGVSGTVID VQVFTRDGVE KDKRALEIEE MQLKQAKKDL
TEELQIFEAG LFARIRDVLI SGGIEAEKLD KLTRERWLEL GLADEEKQNQ LEQLAEQYDE
LKHEFEKKLE AKRRKITQGD DLAPGVLKIV KVYLAVKRQI QPGDKMAGRH GNKGVISKIN
PIEDMPYDEN GVPVDIVLNP LGVPSRMNIG QILETHLGMA AKGIGDKINA MLKQHEEVAK
LREFIQKAYN LGDDVRQKVD LNTFSDEEVL RLAENLKKGM PIATPVFDGA KEKEIKELLQ
LGGLPTSGQI TLFDGRTGEQ FERQVTVGYM YMLKLNHLVD DKMHARSTGS YSLVTQQPLG
GKAQFGGQRF GEMEVWALEA YGAAYTLQEM LTVKSDDVNG RTKMYKNIVD GNHMMEPGMP
ESFNVLLKEI RSLGINIELE ED
