ID   RPOB1_NOCFA             Reviewed;        1162 AA.
AC   Q5YQP4;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta 1 {ECO:0000255|HAMAP-Rule:MF_01321};
DE            Short=RNAP subunit beta 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01321};
DE   AltName: Full=Transcriptase subunit beta 1 {ECO:0000255|HAMAP-Rule:MF_01321};
GN   Name=rpoB1 {ECO:0000255|HAMAP-Rule:MF_01321}; OrderedLocusNames=NFA_46460;
OS   Nocardia farcinica (strain IFM 10152).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX   NCBI_TaxID=247156;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 10152;
RX   PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA   Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA   Shiba T., Hattori M.;
RT   "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
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; AP006618; BAD59497.1; -; Genomic_DNA.
DR   RefSeq; WP_011211181.1; NC_006361.1.
DR   AlphaFoldDB; Q5YQP4; -.
DR   SMR; Q5YQP4; -.
DR   STRING; 247156.NFA_46460; -.
DR   EnsemblBacteria; BAD59497; BAD59497; NFA_46460.
DR   GeneID; 61135250; -.
DR   KEGG; nfa:NFA_46460; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_3_11; -.
DR   BioCyc; NFAR247156:NFA_RS23040-MON; -.
DR   Proteomes; UP000006820; 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; 1.
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..1162
FT                   /note="DNA-directed RNA polymerase subunit beta 1"
FT                   /id="PRO_0000224084"
SQ   SEQUENCE   1162 AA;  127879 MW;  68568FCF75BB094C CRC64;
     MLEGRIVTVS SRTESPLAAP GVPGAPRRLS FARIREPLAV PGLLDIQTES FGWLIGAPDW
     CARAAARGTE PVAGLAEVLA EISPIEDFAG TMSLTLSDPR FEEVKASVEE CKDKDLTYAA
     PWFVTAEFVN NNTGEIKSQT VFMGDFPMMT AHGTFVVNGT ERVVVSQLVR SPGVYFDHAI
     DKGSEKDVHS ARVIPSRGAW LEFDVDKRDT LGVRIDRKRR QPVTVLLKAL GWSAERIAER
     FGFAPLIMAS LAKDNVAGTD DALLEIHRKL RPGEPPTKES AQNLLANLFF TEKRYDLARV
     GRYKIDKKLG LRAPGAPRVL TEDDIAATIE YLVRLHAGER TMIAPGGVEV PVEVDDIDHF
     GNRRVRTVGE LIQNQIRVGL SRMERVVRER MTTQDVEAIT PQSLMNIRPV VAAMKEFFGT
     SQLSQFMDQR NPLASLTNKR RLSALGPGGL SRERAGLEVR DVHYSHYGRM CPIETPEGPN
     IGLMGYLSVY ARVNPFGFVE TPYRRVVDGR VTDEVDYLTA DEEDRHVVAQ ANEPLDAEGR
     FLAARIPVRR KNSEVELVDS AAVDYMDVSP RQMVSVATAM IPFLEHDDAN RALMGANMQR
     QAVPLIRSEA PIVGTGMELR AAVDAGDVVV NEKAGVVEEV SADYVTVMAD DGTRKSYRMR
     KFNRSNQGTC SNQRPIVDEG QRVEAGQVLA DGPCTENGEM ALGKNLLVAI MPWEGHNYED
     AIILSQRLVE QDVLTSIHIE EHEIDARDTK LGAEEITRDI PNVSDEVLAD LDERGIVRIG
     AEVRDGDILV GKVTPKGETE LTPEERLLRA IFGEKAREVR DTSLKVPHGE SGKVIGIRVF
     SREDDDDLPP GVNELVRVYV AQKRKIQDGD KLAGRHGNKG VIGKILPTED MPFLPDGTPV
     DIILNTHGVP RRMNIGQILE THLGWIGKAG WKVEGNPEWA KDLPEEMWEA PADSNIATPV
     FDGAREEELT GLLGSTLPNR DGERMVDDNG KAVLFDGRSG EPFPYPVAVG YMYILKLHHL
     VDDKIHARST GPYSMITQQP LGGKAQFGGQ RFGEMECWAM QAYGAAYTLQ ELLTIKSDDV
     VGRVKVYEAI VKGDNIPEPG VPESFKVLLK ELQALCLNVE VLSAGAAVEL AHGVDDDHER
     TAANLGINLS RAESITETEL SG