RPOB_BRUA1
ID RPOB_BRUA1 Reviewed; 1377 AA.
AC B2S687;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-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};
GN OrderedLocusNames=BAbS19_I11790;
OS Brucella abortus (strain S19).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=430066;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S19;
RX PubMed=18478107; DOI=10.1371/journal.pone.0002193;
RA Crasta O.R., Folkerts O., Fei Z., Mane S.P., Evans C., Martino-Catt S.,
RA Bricker B., Yu G., Du L., Sobral B.W.;
RT "Genome sequence of Brucella abortus vaccine strain S19 compared to
RT virulent strains yields candidate virulence genes.";
RL PLoS ONE 3:E2193-E2193(2008).
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; CP000887; ACD72684.1; -; Genomic_DNA.
DR RefSeq; WP_002966855.1; NC_010742.1.
DR AlphaFoldDB; B2S687; -.
DR SMR; B2S687; -.
DR EnsemblBacteria; ACD72684; ACD72684; BAbS19_I11790.
DR GeneID; 45124609; -.
DR KEGG; bmc:BAbS19_I11790; -.
DR HOGENOM; CLU_000524_4_0_5; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000002565; Chromosome 1.
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..1377
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000141667"
SQ SEQUENCE 1377 AA; 153669 MW; B7E291EE7B6FE496 CRC64;
MAQTHSFNGR KRVRKFFGKI PEVAEMPNLI EVQKASYDQF LMVEEPSGGR PDEGLQAVFK
SVFPIQDFSG ASMLEFVRYE FDPPKFDVDE CRQRDLTYSA PLKVTLRLIV FDIDEDTGAK
SIKDIKEQDV YMGDMPLMTD NGTFIVNGTE RVIVSQMHRS PGVFFDHDKG KTHSSGKLLF
AARVIPYRGS WLDIEFDSKD IVYARIDRRR KLPATTLLMA LGMDGEEILS TFYKTVTYTR
DGDNWRIPYS AERFKGMKII SDLVDADTGE VVLEAGKKLT ARAAKQLAEK GLKAIKATED
DLFGSYLAED VVNYATGEIY LEAGDEIDEK VLKTLIDTGE TEINVLDIDH VNIGAYIRNT
LAVDKNESRQ EALFDIYRVM RPGEPPTMDS AEAMFHSLFF DSERYDLSAV GRVKMNMRLD
LDAEDTVRVL RKEDILAVVK MLVELRDGRG EIDDIDNLGN RRVRSVGELM ENQYRVGLLR
MERAIKERMS SIEIDTVMPQ DLINAKPAAA AVREFFGSSQ LSQFMDQTNP LSEITHKRRL
SALGPGGLTR ERAGFEVRDV HPTHYGRICP IETPEGPNIG LINSLATFAR VNKYGFIESP
YRKVVDGKVT NDVVYLSAME EAKHSVAQAN VELDEQGGFV DEFVICRHAG EVMMAPRENV
DLMDVSPKQL VSVAAALIPF LENDDANRAL MGSNMQRQAV PLVRAEAPFV GTGMEPIVAR
DSGAAIAARR GGIVDQVDAT RIVIRATEEL DPSKSGVDIY RLQKFQRSNQ STCINQRPLV
RVGDRIHKGD IIADGPSTDL GDLALGRNVL VAFMPWNGYN YEDSILLSEK IVSDDVFTSI
HIEEFEVAAR DTKLGPEEIT RDIPNVSEEA LKNLDEAGIV YIGAEVHPGD ILVGKITPKG
ESPMTPEEKL LRAIFGEKAS DVRDTSMRMP PGTYGTVVEV RVFNRHGVEK DERAMAIERE
EIERLAKDRD DEQAILDRNV YGRLADMIDG KVAAAGPKGF KKGTTITREL MTEYPRSQWW
QFAVEDEKLQ GELEALRSQY DDSKKLLEAR FMDKVEKVQR GDEMPPGVMK MVKVFVAVKR
KIQPGDKMAG RHGNKGVVSR ILPVEDMPFL EDGTHADIVL NPLGVPSRMN VGQILETHLG
WACAGMGKKI GELLDVYRKT ANIEPLRQTL EHIYPDNDRN EPVRSYDDDA ILMLANQVKR
GVSIATPVFD GAVEADINAM LTDAGLATSG QSTLYDGRTG EPFDRQVTMG YIYMLKLHHL
VDDKIHARSI GPYSLVTQQP LGGKAQFGGQ RFGEMEVWAL EAYGAAYTLQ EMLTVKSDDV
AGRTKVYEAI VRGDDTFEAG IPESFNVLVK EMRSLGLNVE LDDTREAEQP ALPDAAE
