RPOC_RHOPA
ID RPOC_RHOPA Reviewed; 1402 AA.
AC Q6N4S0;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=RPA3267;
OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=258594;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-98 / CGA009;
RX PubMed=14704707; DOI=10.1038/nbt923;
RA Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA Harrison F.H., Gibson J., Harwood C.S.;
RT "Complete genome sequence of the metabolically versatile photosynthetic
RT bacterium Rhodopseudomonas palustris.";
RL Nat. Biotechnol. 22:55-61(2004).
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; BX572603; CAE28708.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6N4S0; -.
DR SMR; Q6N4S0; -.
DR STRING; 258594.RPA3267; -.
DR PRIDE; Q6N4S0; -.
DR EnsemblBacteria; CAE28708; CAE28708; RPA3267.
DR KEGG; rpa:RPA3267; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_5; -.
DR OMA; YRNIRVE; -.
DR PhylomeDB; Q6N4S0; -.
DR Proteomes; UP000001426; 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; -; 1.
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..1402
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000225572"
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 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 468
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 812
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 886
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 893
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 896
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1402 AA; 156056 MW; 96D3FE9C96D482CC CRC64;
MAMNQEIMNL FNPTTPAQVF DQIRISIASP EKILSWSYGE IKKPETINYR TFKPERDGLF
CARIFGPIKD YECLCGKYKR MKYKGIICEK CSVEVTLSRV RRERMGHIEL AAPVAHIWFL
KSLPSRIGQL LDMTLKDLER ILYFEYYVVL EPGLTDLKER QLLSEEEYLR AQDQYGQDSF
TAMIGAEAIR ELLKGLELEK IDAQLRAEMA ETDSDIKHKK LAKRLKIVEA FRYSGNKPEW
MILTVVPVIP PDLRPLVPLD GGRFATSDLN DLYRRVINRN NRLKRLMELR APDIIIRNEK
RMLQEAVDAL FDNGRRGRVI TGANKRPLKS LADMLKGKQG RFRQNLLGKR VDYSGRSVIV
VGPELKLHQC GLPKKMALEL FKPFIYSRLD AKGLSTTVKQ AKKLVEKERP EVWDILDEVI
REHPVLLNRA PTLHRLGIQA FEPVLIEGKA IQLHPLVCSA FNADFDGDQM AVHVPLSLEA
QLEARVLMMS TNNILHPANG QPIIVPSQDI VLGLYYLSIM REGLPGEGKV FADLAELEHA
LYSKVIHLHT KIKYRWHWVN EEGENTVRLL ETTAGRILLG QVLPKSPKLP FDVINKLMTK
REISGVIDQV YRHCGQKETV IFCDRIMALG FFNAFKAGIS FGKDDMVVPG SKWKIVDSTR
TLAKDFEQQY NDGLITHGEK YNKVVDAWSK ATEEIAKEMM KEISAVRKAP DGSEQQVNSI
YMMAHSGARG SPAQMRQLAG MRGLMAKPSG EIIETPIISN FKEGLSVLEY FNSTHGARKG
LADTALKTAN SGYLTRRLVD VAQDCIITQA DCGTSLGIKM RAIVDAGTVV ASLGSRILGR
TAGEDVRDPA TNEIIVKRGD LMEERDVEAI HQAGVQEVKI RSALTCELVN GICGKCYGRD
LARGTPVNHG EAVGVIAAQS IGEPGTQLTM RTFHIGGAAQ INEQSVIESN FDGKIVIKNR
AIARNGEGHN VAMVRNMVIA IVDPDGTERA THRIQYGARV HVDEGDMVKR GQRIAEWDPY
TRPILTEVEG EIGFEDLIED QSISETLDES TGIAKRIVID WRSTRGGADL RPAIVIKGKD
GKVLKLARGG DARYMLSVDA ILSVDVGAQV KPGDILARIS TESAKTRDIT GGLPRVAELF
EARRPKDAAI IAEIAGTIRF GRDYKNKRRL SIEPLDKNEE AREYLIPKGK HIHLQDGDVV
EKGDFIVEGN PAPHDILAIK GIEELAAYLV NEIQEVYRLQ GVLINDKHIE VIVRQMLQKI
EITDQGDTDM ISGEQVDKIE FNALNAKAVE EGKKPATGNP VLLGITKASL QTRSFFSAAS
FQETTRVLTE AAVNGKVDPL EGLKENVIVG RLIPAGTGAS MAKIREVAVK RDRLILDERE
KQAAIVPAAA PEAEPLSLPP AE
