ID   RPOB_HERAR              Reviewed;        1368 AA.
AC   A4G9U5;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=HEAR3173;
OS   Herminiimonas arsenicoxydans.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herminiimonas.
OX   NCBI_TaxID=204773;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ULPAs1;
RX   PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA   Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA   Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA   Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA   Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA   Perdrial N., Schoepp B., Siguier P., Simeonova D.D., Rouy Z., Segurens B.,
RA   Turlin E., Vallenet D., van Dorsselaer A., Weiss S., Weissenbach J.,
RA   Lett M.-C., Danchin A., Bertin P.N.;
RT   "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT   environments.";
RL   PLoS Genet. 3:518-530(2007).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CU207211; CAL63282.1; -; Genomic_DNA.
DR   RefSeq; WP_011872535.1; NC_009138.1.
DR   AlphaFoldDB; A4G9U5; -.
DR   SMR; A4G9U5; -.
DR   STRING; 204773.HEAR3173; -.
DR   EnsemblBacteria; CAL63282; CAL63282; HEAR3173.
DR   KEGG; har:HEAR3173; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_0_4; -.
DR   OMA; FMTWEGY; -.
DR   OrthoDB; 9601at2; -.
DR   Proteomes; UP000006697; 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..1368
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000300326"
SQ   SEQUENCE   1368 AA;  152432 MW;  DAC4948E75068124 CRC64;
     MHYSFTEKKR IRKSFAKRAN VHNVPFLLAT QLESYHDFLQ EDKIPSQRKN EGLQSAFTSI
     FPIVSHNGFA RLEFLSYVLG DPPFNIKECQ QRGLTYASPL RAKVRLVILD KESPTKPVVK
     EMKEQEVYMG ELPLMTSTGS FVINGTERVI VSQLHRSPGV FFEHDRGKTH SSGKLLFSAR
     IIPYRGSWLD YEFDPKDILF FRVDRRRKMP VTILLKAIGM TPEQILENFF VFDDFTLHAD
     GAEMKFVAER LRGEVARFDI TDKAGKVLVA KDKRINSKHV RDVEAAGIKQ ISVPEDYLLG
     RILAKNIVDA DTGEVIASAN DELTDDLLAR LREGKISHIQ TLYTNDLDQG GYISQTLRMD
     DTNDQMAAKV AIYRMMRPGE PPTEDSVEAL FNGLFYNPDR YDLSAVGRMK FNRRIGRDSL
     TGDMTLSNED VLAVIKILVE LRNGRGEVDD IDHLGNRRVR CVGELAENQF RAGLVRVERA
     VKERLGQAEA DNLMPHDLIN SKPISAAIRE FFGSSQLSQF MDQTNPLSEI THKRRVSALG
     PGGLTRERAG FEVRDVHPTH YGRVCPIETP EGPNIGLINS LALYARLNEY GFLETPYRKV
     EGSKVTDQID YLSAIEEGRY IIAQANATID KAGMLSDELV SAREAGETIL VSPERVQYMD
     VAPGQVVSVA ASLIPFLEHD DANRALMGAN MQRQAVPCLR PEKALVGTGI ERTVAVDSGT
     TVQALRGGIV DYIDAGRVVI RVNDDEAQAG EVGVDIYNLI KYTRSNQNTN INQRPIVQVG
     DRVAKHDVIA DGASTDLGEL ALGQNMLVAF MPWNGYNFED SILISEKVVA DDRYTSIHIE
     ELSVVARDTK LGAEEITRDI SNLAENQLAR LDESGIVYIG AEVTAGDTLV GKVTPKGETQ
     LTPEEKLLRA IFGEKASDVK DTSLRVPSGM VGTVIDVQVF TREGIPRDKR AQQIIDDELQ
     RYRLDLNDQL RIVEGDAFQR LEKMLVGKVV NGGPKKIAKG TKITAEYLAD LDKYHWFDIR
     PSDDTSANAL EAIKESIAEK RHQFDLAFEE KRKKLTQGDE LPPGVQKMVK VYLAVKRRLQ
     PGDKMAGRHG NKGVVSRILP IEDMPHMADG TPADVVLNPL GVPSRMNVGQ VLEVHLGWAA
     KGLGLRIGEM LNTQVQIAEL RKFLAAIYNE SGKTEDLDSF SDAEILELAS NLKNGVPFAT
     PVFDGADEGE TRRMLDLAYP DHIAKQLGMT ASKNQVTMYD GRTGEAFERT VTVGYMHYLK
     LHHLVDDKMH ARSTGPYSLV TQQPLGGKAQ FGGQRFGEME VWALEAYGAS YVLQEMLTVK
     SDDVNGRTKV YENLVKGDHV IDAGMPESFN VLVKEIRSLG IDIDLERD