ID   RPOC_BRASO              Reviewed;        1399 AA.
AC   A4YSI2;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE            Short=RNAP subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01322};
DE   AltName: Full=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE   AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
GN   Name=rpoC {ECO:0000255|HAMAP-Rule:MF_01322}; OrderedLocusNames=BRADO3055;
OS   Bradyrhizobium sp. (strain ORS 278).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium; unclassified Bradyrhizobium.
OX   NCBI_TaxID=114615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ORS 278;
RX   PubMed=17540897; DOI=10.1126/science.1139548;
RA   Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C.,
RA   Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA   Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA   Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.-S., Saunders E.,
RA   Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA   Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT   "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL   Science 316:1307-1312(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_01322}.
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_01322};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01322};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01322};
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_01322}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_01322}.
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DR   EMBL; CU234118; CAL76858.1; -; Genomic_DNA.
DR   RefSeq; WP_011926046.1; NC_009445.1.
DR   AlphaFoldDB; A4YSI2; -.
DR   SMR; A4YSI2; -.
DR   STRING; 114615.BRADO3055; -.
DR   PRIDE; A4YSI2; -.
DR   EnsemblBacteria; CAL76858; CAL76858; BRADO3055.
DR   KEGG; bra:BRADO3055; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_3_1_5; -.
DR   OMA; YRNIRVE; -.
DR   OrthoDB; 4421at2; -.
DR   BioCyc; BSP114615:BRADO_RS14315-MON; -.
DR   Proteomes; UP000001994; 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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.274.100; -; 2.
DR   Gene3D; 4.10.860.120; -; 1.
DR   HAMAP; MF_01322; RNApol_bact_RpoC; 1.
DR   InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR   InterPro; IPR012754; DNA-dir_RpoC_beta_prime_bact.
DR   InterPro; IPR000722; RNA_pol_asu.
DR   InterPro; IPR006592; RNA_pol_N.
DR   InterPro; IPR007080; RNA_pol_Rpb1_1.
DR   InterPro; IPR007066; RNA_pol_Rpb1_3.
DR   InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR   InterPro; IPR007083; RNA_pol_Rpb1_4.
DR   InterPro; IPR007081; RNA_pol_Rpb1_5.
DR   InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR   InterPro; IPR038120; Rpb1_funnel_sf.
DR   PANTHER; PTHR19376; PTHR19376; 1.
DR   Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR   Pfam; PF00623; RNA_pol_Rpb1_2; 2.
DR   Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR   Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR   Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR   SMART; SM00663; RPOLA_N; 1.
DR   TIGRFAMs; TIGR02386; rpoC_TIGR; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW   Zinc.
FT   CHAIN           1..1399
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000353301"
FT   REGION          1379..1399
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         71
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         73
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         86
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         89
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         462
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         464
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         466
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         810
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         884
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         891
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         894
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1399 AA;  155727 MW;  7CEFA055FFE200B5 CRC64;
     MNQEIMNLFN PTTPAQVFDQ IRISIASPEK ILSWSYGEIK KPETINYRTF KPERDGLFCA
     RIFGPIKDYE CLCGKYKRMK YKGIICEKCS VEVTLSRVRR ERMGHIELAA PVAHIWFLKS
     LPSRIGLLLD MTLKDLERIL YFEYYVVLEP GLTALKDRQL LSEDEYLKAQ DEYGQDSFTA
     MIGAEAIREL LRGLELEKLE QTLRAEMQET DSDIKHKKLA KRLKIVEAFR HSGNKPEWMI
     MTVVPVIPPD LRPLVPLDGG RFATSDLNDL YRRVINRNNR LKRLMELRAP DIIIRNEKRM
     LQEAVDALFD NGRRGRVITG ANKRPLKSLA DMLKGKQGRF RQNLLGKRVD YSGRSVIVVG
     PELRLHQCGL PKKMALELFK PFIYSRLDAK GLSTTVKQAK KLVEKERPEV WDILDEVIRE
     HPVLLNRAPT LHRLGIQAFE PVLIEGKAIQ LHPLVCSAFN ADFDGDQMAV HVPLSLEAQL
     EARVLMMSTN NILHPANGQP IIVPSQDIVL GLYYVSIMRE GMPGQGMTFG NMAELEHALH
     AKAIHLHSKI KYRWEGMNEE GKIAKRWIET TAGRVMLGNL LPKHPRVTFE VINKLMTKRE
     ISGVIDQVYR HCGQKETVIF CDRIMALGFY NAFKAGISFG KDDMVVPAGK WKIVDTTRTL
     AKDFEQQYND GLITHGEKYN KVVDAWSKAS EEIAKEMMKE ISVTKKTATG ADADINSIYM
     MSHSGARGSP AQMRQLAGMR GLMAKPSGEI IETPIISNFK EGLSVLEYFN STHGARKGLA
     DTALKTANSG YLTRRLVDVA QDCIITQDDC GTHLGIKMRA IVDAGTLVAS LGSRILGRVP
     CDDVRDPATN AVLVKAGTLM EESHIDAIQQ AGVQEVKIRS ALTCELVNGI CKMCYGRDLA
     RGTPVNHGEA VGVIAAQSIG EPGTQLTMRT FHIGGAAQLN EQSFVESNFE GKVVIRNKAI
     ARNSEGHLIA MVRNMVVTIV DPDGTERATH RIQYGSRMHV DDGDMIKRGQ RIAEWDPYTR
     PILTEAEGTI GFEDLTEGLS ISETLDESTG IAKRVVIDWR GTRGGADLRP AIVIKGKDGK
     VLKLARGGDA RYMLSVDAIL SVDIGATVKP GDILARISTE SAKTRDITGG LPRVAELFEA
     RKPKDAAIIA EIAGTIRFGR DYKNKRRISI EPVDKTEEAR EYLIPKGKHI HLQDGDIVEK
     GDFIVEGNPA PHDILAIKGI EELAAYLVNE IQEVYRLQGV LINDKHIEVI VRQMLQKIEV
     TDQGDTDMIA GEQVDKIEFD ALNAKAQEEG KKPASGNPVL LGITKASLQT RSFFSAASFQ
     ETTRVLTEAA VNGKIDPLEG LKENVIVGRL IPAGTGASMA RIREVALKRD KLILDEREKQ
     AAIVPSQPEP QPLALPPAE