ID   RPOB_DEHMC              Reviewed;        1273 AA.
AC   Q3ZX01;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=cbdbA586;
OS   Dehalococcoides mccartyi (strain CBDB1).
OC   Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC   Dehalococcoidaceae; Dehalococcoides.
OX   NCBI_TaxID=255470;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBDB1;
RX   PubMed=16116419; DOI=10.1038/nbt1131;
RA   Kube M., Beck A., Zinder S.H., Kuhl H., Reinhardt R., Adrian L.;
RT   "Genome sequence of the chlorinated compound-respiring bacterium
RT   Dehalococcoides species strain CBDB1.";
RL   Nat. Biotechnol. 23:1269-1273(2005).
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; AJ965256; CAI82766.1; -; Genomic_DNA.
DR   RefSeq; WP_011309117.1; NC_007356.1.
DR   AlphaFoldDB; Q3ZX01; -.
DR   SMR; Q3ZX01; -.
DR   PRIDE; Q3ZX01; -.
DR   KEGG; deh:cbdbA586; -.
DR   HOGENOM; CLU_000524_4_1_0; -.
DR   OMA; FMTWEGY; -.
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; 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   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   PROSITE; PS01166; RNA_POL_BETA; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Nucleotidyltransferase; Transcription;
KW   Transferase.
FT   CHAIN           1..1273
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000224050"
FT   REGION          1252..1273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1273 AA;  141526 MW;  768900D1E5A57DC9 CRC64;
     MVSMLPKADA ATGVIRKSYA QLPEVVNVPN LIEMQLQSFV WFQEEGLREL IEEISPIKDF
     VGNRLELEFI GYEFREPRLS EYECTQRDQT YSVPLYVKAR LIVKTTGEIK EPFDLFFGDI
     PLMTALGTFI TSGTERVVVS QLLRSPGVYF TISDDPATGR PLCHTNLIPS RGAWLEFETS
     NRDVISVKID GRRKIPVSTL LRAIGYSDDL DILNLFEVID NDPERHYIQS SIDRDPLIKD
     EISALIDIYS RLRPGDPPNA DNARKLINEM FFDPQHYDLG KVGRYKVNRR LELPSREVGE
     NRALTREDIV AIIQRIIMVN NGQDTPDDID HLGNRRIRTV GELVQNQFRI GLVRLERVAR
     ERMSIVNLEM VTPSALVNIR PVVSAVKEFF GGSQLSQFMD QTNPLAEITN KRRLSAMGPG
     GLSRERAGFD VRDVHYSHYG RICPIETPEG PNIGLIGSLA TYSRINRYGF VETPYRKVYS
     KLKNNDKKLV GLKLKIEISE KGKVLAAAGS TISEDSFKLI SKLPECDISV MPFVSAEVKY
     MPADEEDRYI IAQANTRLDE KGYFLDDRIE ARSAERYVVE PPDKIDYMDV SPKQIFSVAA
     SLIPFLEHDD ANRALMGANM QRQAVPLLRA EAPMVATGME REAARYSGQV IFAKHAGVAS
     SVTSEKIIIR TAEGGHDEYL LKKFVRTNQG TCINQHAIIN KGQKIAAGQV LADSSATENG
     ELALGQNCVV AFMSWQGFNY EDAIILSERL VREDAFTSIH ITKHELEARD TKLGVEEITR
     DIPNVGEESL RELDEDGIIR IGAEVGPDDI LVGKITPKGE TELSAEEKLL RAIFGEKARE
     VKDTSLRMPH GEWGKVINVR IFSRDSGDDL PARVNKWVQV WVAQKRKVSV GDKLAGRHGN
     KGVISIIAPV EDMPYLPDGT PVDVVLNPIG VPSRMNLGQI LETHLGWAGH LLGFRVATPV
     FDGADDTVIE DALARSWLSA KAGAIDMSPE NKRPSADAHK AIEWIKQQGF DGKKIFDEKH
     PGLAKEVSLK LWLKDMGVDA SALSGAELEK KAYDVSSQSR LPSPIVGKSV LRDGRTGETF
     DQPVTVGNMY ILKLIHLVED KVHARATGPY SLISQQPLGG KAQFGGQRFG EMEVWAMYAY
     GTAHNLQEML TIKSDDIAGR AKAYESIVKG EDVLQPGVPE SFKVLVKELQ SLGLAVEVIN
     EEVKIAPSEK VSSLNEGNLP ASDEISAEIL PETLYANTED ISEDSMMSVI DADDQDLVVS
     SNDEEVSEND ERS