RPOC_RHOPS
ID RPOC_RHOPS Reviewed; 1400 AA.
AC Q134R9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=RPD_3194;
OS Rhodopseudomonas palustris (strain BisB5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=316057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB5;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL Submitted (MAR-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; CP000283; ABE40420.1; -; Genomic_DNA.
DR AlphaFoldDB; Q134R9; -.
DR SMR; Q134R9; -.
DR STRING; 316057.RPD_3194; -.
DR PRIDE; Q134R9; -.
DR EnsemblBacteria; ABE40420; ABE40420; RPD_3194.
DR KEGG; rpd:RPD_3194; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_5; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR BioCyc; RPAL316057:RPD_RS16035-MON; -.
DR Proteomes; UP000001818; 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_1000086409"
FT REGION 1378..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; 156167 MW; AD95A7174D6B2CED CRC64;
MNQEIMNLFN PTTPAQVFDQ IRISIASPEK ILSWSYGEIK KPETINYRTF KPERDGLFCA
RIFGPIKDYE CLCGKYKRMK YKGIICEKCS VEVTLSRVRR ERMGHIELAA PVAHIWFLKS
LPSRIGQLLD MTLKDLERIL YFEYYVVLEP GLTDLKERQL LSEEEYLRAQ DQYGQDSFTA
MIGAEAIREL LKGLELEKID AQLRVEMAET DSDIKHKKLA KRLKIVEAFR YSGNKPEWMI
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 DLAELEHALH
AKVIHLHTKI KYRWDSLDDE GKPYKRLIET TAGRILLGQV LPKSVKLPYE TINKLMTKRE
ISSVIDQVYR HCGQKETVIF CDRIMALGFF NAFKAGISFG KDDMVVPASK WKIVDTTRTL
AKDFEQQYND GLITHGEKYN KVVDAWSKAT EEIAKEMMKE ISAVRKNASG AESQVNSIYM
MAHSGARGSP AQMRQLAGMR GLMAKPSGEI IETPIISNFK EGLSVLEYFN STHGARKGLA
DTALKTANSG YLTRRLVDVA QDCIITQDDC GTSLGIKMRA IIDAGTVVAS LGSRILGRTA
GEDVRDPQTN EVIVKKGELM EERDIEAIHQ AGVQEVKIRS ALTCELVNGI CGKCYGRDLA
RGTPVNHGEA VGVIAAQSIG EPGTQLTMRT FHIGGAAQIN EQSVIESNFE GKVVIKNKAI
ARNGENHNVA MVRNMVVAIV DPDGTERATH RIQYGARMHV DEGDTIKRGH RIAEWDPYSR
PVLTEVEGTI DFEDLIEDQS ISETLDESTG IAKRIVIDWR STRGGADLRP AIVIKGKDGK
VLKLARGGDA RYMLSVDAIL SVDVGAKVKP GDILARISTE SAKTRDITGG LPRVAELFEA
RKPKDAAIIA EIAGTIRFGR DYKNKRRISI EPMDKEEEAR EYLIPKGKHI HLQDGDIVEK
GDFIVEGNPA PHDILAIKGI EELAAYLVNE IQEVYRLQGV LINDKHIEVI VRQMLQKVEI
TDQGETDMIS GEQIDKIEFD QLNVKARDEG KKIATGTPVL LGITKASLQT RSFFSAASFQ
ETTRVLTEAA VNGKVDPLEG LKENVIVGRL IPAGTGASMA KIREVAMKRD RMILDEREKQ
ATIVPPAAPE AEPLALPPAE
