RPOB_BREBN
ID RPOB_BREBN Reviewed; 1179 AA.
AC C0ZIH0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, 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}; OrderedLocusNames=BBR47_02110;
OS Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=358681;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=47 / JCM 6285 / NBRC 100599;
RA Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W.,
RA Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S.,
RA Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., Yoshikawa H.,
RA Udaka S., Tanikawa S., Fujita N.;
RT "Brevibacillus brevis strain 47, complete genome.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; AP008955; BAH41188.1; -; Genomic_DNA.
DR RefSeq; WP_012683975.1; NC_012491.1.
DR AlphaFoldDB; C0ZIH0; -.
DR SMR; C0ZIH0; -.
DR STRING; 358681.BBR47_02110; -.
DR PRIDE; C0ZIH0; -.
DR EnsemblBacteria; BAH41188; BAH41188; BBR47_02110.
DR KEGG; bbe:BBR47_02110; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_9; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000001877; 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..1179
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000165792"
FT REGION 1153..1179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1179 AA; 131794 MW; 2C2D4C94D39A4A8E CRC64;
MAGKVIQSGR HRQRRTYSRI NEVLGLPNLI EIQQKSYQWF LDEGLREMFQ DISPIQDFTG
NLVLEFIDYS LGEPKYDVDE SKERDVTYAA PLRVKVRLLN KETGEVKEQE VFMGDFPLMT
ETGTFIINGA ERVIVSQLVR SPSVYYNTKV DKNGKQTFTA TVIPNRGAWL ELETDAKDVI
YVRIDRTRKI PVTVLLRALG FGSDIEILNL LGEDEYIKNT LEKDNTDSTE KALIEIYERL
RPGEPPTVEN AKSLLISRFF DPKRYDLASV GRYKMNKKLH LKNRLYNQRL AETLIDTTTG
EIFAEAGQMI DRRVLERIVP ALEGSIGFID VRTHGGVLED EAIHLQSINI FSPIEDGKII
KVIGNGNVDK SFKHITPADI VSAINYFMNL LHSVGSTDDI DHLGNRRLRS VGELLQNQFR
IGLSRMERVV RERMSIQDQN QITPQALINI RPVIASLKEF FGSSQLSQFM DQTNPLAELT
HKRRLSALGP GGLTRERAGF EVRDVHHSHY GRMCPIETPE GPNIGLINSL SSFARINDYG
FIETPRRKVD PETGFVLTDI SYLTADEEDV FNVAQANQPL DEDGRFVNDM VICRRKGEIL
SVPRDKVDFM DVSPKQVVSV ATALIPFLEN DDANRALMGS NMQRQAVPLL IPQAPFVGTG
MEHKAAQDSG VAIVAKHPGQ VERVTAREIW IRRYQEIDGR KVAGDLDKYK MHKFIRSNQG
TCINQRPIVS TGDWIEKGDI VGDGPSTEKG ELALGRNVIV AFMTWEGYNY EDAILLSEKL
VKDDVYTSIH IEEYESEARD TKLGPEEITR DIPNVGEDAL KNLDERGIIR VGAEIQDGDI
LVGKVTPKGV TELTAEERLL HAIFGEKARE VRDTSLRVPH GGSGIIVDVK VFTRENGDEL
PPGVNQLVRV YIAQKRKISV GDKMAGRHGN KGVIARIMAE EDMPFLPDGS PVEIVLNPLG
VPSRMNIGQV LETHLGMAAK LLGIHVATPV FDGARQAEVF ETLAEAGLDR DGKTILFDGR
TGEPFDRRVT VGCVYMLKLA HLVDDKIHAR STGPYSLVTQ QPLGGKAQFG GQRFGEMEVW
ALEAYGAAYT LQEILTVKSD DVVGRVKTYE AIVKGENVPE PGVPESFKVL IKELQSLGMD
VKILSGDEQE IEMREMEDED EGNGEKLNLV LEGGSLNEE