ID   RPOB_KORVE              Reviewed;        1489 AA.
AC   Q1IHH4;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=Acid345_4676;
OS   Koribacter versatilis (strain Ellin345).
OC   Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae;
OC   Candidatus Koribacter.
OX   NCBI_TaxID=204669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ellin345;
RX   PubMed=19201974; DOI=10.1128/aem.02294-08;
RA   Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA   Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA   Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA   Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA   Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA   Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA   Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA   Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT   "Three genomes from the phylum Acidobacteria provide insight into the
RT   lifestyles of these microorganisms in soils.";
RL   Appl. Environ. Microbiol. 75:2046-2056(2009).
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; CP000360; ABF43676.1; -; Genomic_DNA.
DR   RefSeq; WP_011525473.1; NC_008009.1.
DR   AlphaFoldDB; Q1IHH4; -.
DR   SMR; Q1IHH4; -.
DR   STRING; 204669.Acid345_4676; -.
DR   PRIDE; Q1IHH4; -.
DR   EnsemblBacteria; ABF43676; ABF43676; Acid345_4676.
DR   KEGG; aba:Acid345_4676; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_1_0; -.
DR   OMA; FMTWEGY; -.
DR   OrthoDB; 9601at2; -.
DR   Proteomes; UP000002432; 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..1489
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000300267"
SQ   SEQUENCE   1489 AA;  167265 MW;  6CD38A69992E125A CRC64;
     MAEKKIAFRN RQDFSKIPAT IQIPNLIEVQ KRSYDRFLQM DLLPSERDDA GLQAVFQSVF
     PITDFRNVSQ LEFVDYAIGN WECKCGHLKG LHHLRTTCKN CGATVVTDPF HPGDVLCHKC
     GTFNANTPDF CNKCGDPVGL QLKYDVAECE ERGMTYSAPL KVTMRLTIFD KDPETNNRTI
     RDIKEQEVFF GDVPLMTQNG TFIINGTERV IVSQLHRSPG VFFETANNRT YFLGKIIPYR
     GSWVEFEYDQ KNILYVRIDR KRKFLGTIFL RALGLRTDED ILRTFYTVDR IAVKDKKLYW
     TLEPGIERPT NLVGLKLSHA IKAKNGEEVA HSGRKVTASV LKEIQKHKIS ELEIELGDLE
     GAYVASDVID TNTGEVLLEA NQELTADKLS KMIDAGIGEV NVFFPERDDV GTVISATLRR
     DSVKTPQEAL IEIYRKLRPG DPPTLDTATA LFHGMFFDAR KYDFSRVGRL KFNIKLFDRQ
     DPTGLDKRTL DPDDFYHTIR YLLKLRRNLG AVDDIDHLGN RRVRAVGELL ENQFRIGLVR
     MERAIKEKMS VYQEMSTAMP HDLVNAKPVM AAIREFFGSS QLSQFMDQTN PLSEITHKRR
     LSALGPGGLS RERAGFEVRD VHPTHYGRIC PIETPEGPNI GLISSLSCYA RINDYGFIES
     PYRRVKGGRV IDYVQVTHAG DSDYRVGDKM EKSEAQKANE ELRGRKKRGI ELEPYSFYLS
     AWEEDKWTIA QANAELDEKG KITSELVNAR KAGNFVLISR DDIDYIDVSP KQLVSVAASL
     VPFLEHDDAN RALMGANMQR QSVPLLRAEA PIVGTGMEGV TARDSGAVVL ARRSGIIDSV
     DSERVIVRVE GEHHPMQLSR EVGSDIYQLT KFKRSNQNTC INQKPIVKQG DHVKKGQVIA
     DGPCTDHGEL GLGRNVLVSF MPWRGYNFED AILVSEKLVK EDYYTSVHIE EFEIEARDTK
     LGPEEITRDI PNVSESALRD LDESGVIRIG APVKAGDILV GKVTPKGETQ LTPEEKLLRA
     IFGEKAGDVR DASLTCPPGI EGVVVDVKIF SRKGQEKDER AKQIEGTQIA KLEKNLADEI
     RILTDERLKR LEGLLGAKVV QADLHDERTN KRLLTKDAVL DRETIERIST RNLKRIKYAD
     KDPRVNEQID EIEEMTSRQI DVLRKIVREK IEKLQKGDEL PPGVIKLVKV YIAMKRKLSV
     GDKMAGRHGN KGVIARILPE EDMPYLEDGT PVEIVLNPLG VPSRMNVGQI LETHLGWAGH
     ELGKKIAEFM VENSEAGQVR KHLKQLFKDT AFVDHVTELD DEMLLKVAKG MQDGVFFGSA
     VFDGSTEAEI KSLLDQAGLP TSGKTFLYDG MTGDRFEQPV TVGYIYMLKL SHLVDDKIHA
     RSIGPYSLIT QQPLGGKAQF GGQRFGEMEV WALEAYGAAY ILQELLTAKS DDVYGRTKIY
     EAIVKGEAAI EPGVPESFNV LIRELQSLCL DVELIKTKEK AAPAPVAAD