RPOC_RHOP2
ID RPOC_RHOP2 Reviewed; 1400 AA.
AC Q2IXR9;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=RPB_2286;
OS Rhodopseudomonas palustris (strain HaA2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=316058;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HaA2;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A.,
RA Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris HaA2.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000250; ABD06991.1; -; Genomic_DNA.
DR RefSeq; WP_011441178.1; NC_007778.1.
DR AlphaFoldDB; Q2IXR9; -.
DR SMR; Q2IXR9; -.
DR STRING; 316058.RPB_2286; -.
DR PRIDE; Q2IXR9; -.
DR EnsemblBacteria; ABD06991; ABD06991; RPB_2286.
DR KEGG; rpb:RPB_2286; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_5; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000008809; 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; Transcription; Transferase; Zinc.
FT CHAIN 1..1400
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000240819"
FT REGION 1377..1400
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 1400 AA; 156039 MW; ADDAD3DE9CAF52BE CRC64;
MNQEIMNLFN PTTPAQVFDQ IRISIASPEK ILSWSYGEIK KPETINYRTF KPERDGLFCA
RIFGPIKDYE CLCGKYKRMK YKGIICEKCS VEVTLSRVRR ERMGHIELAA PVAHIWFLKS
LPSRIGQLLD MTLKDLERIL YFEYYVVLEP GLTDLKERQL LSEEEYLRAQ DQYGQDSFTA
MIGAEAIREL LKGLELEKID AQLRVEMAET DSDIKHKKLA KRLKIVEAFR FSGNKPEWMI
LTVVPVIPPD LRPLVPLDGG RFATSDLNDL YRRVINRNNR LKRLMELRAP DIIIRNEKRM
LQEAVDALFD NGRRGRVITG ANKRPLKSLA DMLKGKQGRF RQNLLGKRVD YSGRSVIVVG
PELKLHQCGL PKKMALELFK PFIYSRLDAK GLSTTVKQAK KLVEKERPEV WDILDEVIRE
HPVLLNRAPT LHRLGIQAFE PVLIEGKAIQ LHPLVCAAFN ADFDGDQMAV HVPLSLEAQL
EARVLMMSTN NILHPANGQP IIVPSQDIVL GLYYLSILRE GLPGEGKVFG DLAELEHALF
SKVIHLHTKI KYRWDSLDDE GKPYQRLIET TAGRILLGQV LPKSVKLPFE VINKLMTKRE
ISSVIDQVYR HCGQKETVIF CDRIMALGFF NAFKAGISFG KDDMVVPASK WKIVDTTRTL
AKDFEQQYND GLITHGEKYN KVVDAWSKAT EEIAKEMMKE ISAVRKNASG AETQVNSIYM
MAHSGARGSP AQMRQLAGMR GLMAKPSGEI IETPIISNFK EGLSVLEYFN STHGARKGLA
DTALKTANSG YLTRRLVDVA QDCIITQDDC GTSLGIKMRA IIDAGTVVAS LGSRILGRTA
GEDVRDPQTN EVIVKKGQLM EERDVEAIHQ AGVQEVKIRS ALTCELVNGI CGKCYGRDLA
RGTPVNHGEA VGVIAAQSIG EPGTQLTMRT FHIGGAAQIN EQSVIESNFE GKVVIKNKAI
ARNGENHSVA MVRNMVVAIV DPDGTERATH RIQYGARMHV DEGDTVKRGQ RIAEWDPYSR
PVLTEVEGTI DFEDLVEDQS ISETLDESTG IAKRIVIDWR STRGGADLRP AIVVKGKDGK
VLKLARGGDA RYMLSVDAIL SVDVGAKVKP GDILARISTE SAKTRDITGG LPRVAELFEA
RKPKDAAIIA EIAGTIRFGR DYKNKRRISI EPMDSEEEAR EYLIPKGKHI HLQDGDIVEK
GDFIVEGNPA PHDILAIKGI EELAAYLVNE IQEVYRLQGV LINDKHIEVI VRQMLQKVEI
TDQGETDMIS GEQIDKIEFD QLNAKARDEG KKIATGTPVL LGITKASLQT RSFFSAASFQ
ETTRVLTEAA VNGKVDPLEG LKENVIVGRL IPAGTGASMA KLREVAMKRD RMILDEREKQ
ATIVPPAAPE AEPLALPPVE
