ID   RPOB_BRUSU              Reviewed;        1377 AA.
AC   Q8G069; G0KAG4;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 113.
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=BR1243, BS1330_I1239;
OS   Brucella suis biovar 1 (strain 1330).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=204722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=12271122; DOI=10.1073/pnas.192319099;
RA   Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA   Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA   Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA   Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT   "The Brucella suis genome reveals fundamental similarities between animal
RT   and plant pathogens and symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=22038969; DOI=10.1128/jb.06181-11;
RA   Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT   "Revised genome sequence of Brucella suis 1330.";
RL   J. Bacteriol. 193:6410-6410(2011).
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; AE014291; AAN30162.1; -; Genomic_DNA.
DR   EMBL; CP002997; AEM18580.1; -; Genomic_DNA.
DR   RefSeq; WP_006190505.1; NZ_KN046804.1.
DR   AlphaFoldDB; Q8G069; -.
DR   SMR; Q8G069; -.
DR   GeneID; 45052276; -.
DR   KEGG; bms:BR1243; -.
DR   KEGG; bsi:BS1330_I1239; -.
DR   PATRIC; fig|204722.21.peg.3399; -.
DR   HOGENOM; CLU_000524_4_0_5; -.
DR   PhylomeDB; Q8G069; -.
DR   PRO; PR:Q8G069; -.
DR   Proteomes; UP000007104; Chromosome I.
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:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR   CDD; cd00653; RNA_pol_B_RPB2; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 2.40.50.150; -; 1.
DR   Gene3D; 3.90.1100.10; -; 2.
DR   Gene3D; 2.30.150.10; DNA-directed RNA polymerase, beta subunit, external 1 domain; 1.
DR   Gene3D; 2.40.270.10; DNA-directed RNA polymerase, subunit 2, domain 6; 1.
DR   Gene3D; 3.90.1800.10; RNA polymerase alpha subunit dimerisation domain; 1.
DR   Gene3D; 3.90.1110.10; RNA polymerase Rpb2, domain 2; 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   NCBIfam; TIGR02013; rpoB; 1.
DR   PANTHER; PTHR20856; DNA-DIRECTED RNA POLYMERASE I SUBUNIT 2; 1.
DR   PANTHER; PTHR20856:SF20; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 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   SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 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_0000047871"
SQ   SEQUENCE   1377 AA;  153641 MW;  5523F3E2A260F57F 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 AVLEAGKKLT 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
//