RPOC1_OSTTA
ID RPOC1_OSTTA Reviewed; 740 AA.
AC Q0P3M5;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01323};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01323};
DE AltName: Full=PEP {ECO:0000255|HAMAP-Rule:MF_01323};
DE AltName: Full=Plastid-encoded RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01323};
DE Short=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01323};
GN Name=rpoC1 {ECO:0000255|HAMAP-Rule:MF_01323}; OrderedLocusNames=OtCpg00270;
OS Ostreococcus tauri.
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Ostreococcus.
OX NCBI_TaxID=70448;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OTTH0595;
RX PubMed=17251180; DOI=10.1093/molbev/msm012;
RA Robbens S., Derelle E., Ferraz C., Wuyts J., Moreau H., Van de Peer Y.;
RT "The complete chloroplast and mitochondrial DNA sequence of Ostreococcus
RT tauri: organelle genomes of the smallest eukaryote are examples of
RT compaction.";
RL Mol. Biol. Evol. 24:956-968(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_01323}.
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_01323};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01323};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01323};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01323};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01323};
CC -!- SUBUNIT: In plastids the minimal PEP RNA polymerase catalytic core is
CC composed of four subunits: alpha, beta, beta', and beta''. When a
CC (nuclear-encoded) sigma factor is associated with the core the
CC holoenzyme is formed, which can initiate transcription.
CC {ECO:0000255|HAMAP-Rule:MF_01323}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC Rule:MF_01323}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01323}.
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DR EMBL; CR954199; CAL36352.1; -; Genomic_DNA.
DR RefSeq; YP_717230.1; NC_008289.1.
DR AlphaFoldDB; Q0P3M5; -.
DR SMR; Q0P3M5; -.
DR STRING; 70448.Q0P3M5; -.
DR PRIDE; Q0P3M5; -.
DR GeneID; 4238799; -.
DR KEGG; ota:OstapCp27; -.
DR eggNOG; ENOG502QPYA; Eukaryota.
DR InParanoid; Q0P3M5; -.
DR OrthoDB; 774084at2759; -.
DR Proteomes; UP000009170; Chloroplast.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; 1.10.274.100; -; 1.
DR Gene3D; 4.10.860.120; -; 1.
DR HAMAP; MF_01323; RNApol_bact_RpoC1; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
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; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR034678; RNApol_RpoC1.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR SMART; SM00663; RPOLA_N; 1.
PE 3: Inferred from homology;
KW Chloroplast; DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Plastid; Reference proteome; Transcription;
KW Transferase; Zinc.
FT CHAIN 1..740
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000277173"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 539
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 541
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 543
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
SQ SEQUENCE 740 AA; 84558 MW; 0912D504719C06C1 CRC64;
MSIEYVQLQL ASPSEIKRWS QRILPTGEVV GEISKADTIN YRTFKPERGG LFCERIFGST
SNGECSCGKT KRRKLIVPVN FNRLTLQKRN AELEATQAII EVCPSCGVEP TNSKVRRYRM
GCISLKKPVA HMWYFRNSPN VLAALLNMRS QEIDETIHFQ TYTPSKYGTQ NYCLHGGVQW
YVNHWEPMHP YFAGDIDVSM DKAASWNSKS TFMPSQIKTI ENCGGEALQE LLTRLDLVFL
QRMLSRKLKN TIEKKKLAAK SLRKRHKRRK TAKLLGRTDQ KNYGITIKVR EYSRRLEFIR
SLARKGLRPE WMILSIFPVL PPDLRPMIQM SSGRFATSDL NDLYRRLIYR KIRFEKFLTL
FDEEFLPDLL IRHDLCLLQE AADSIIDNGR LDKPAQRPNR KPFKSLTSII EGKHGRFRQN
LLGKRVDYSG RSVIVVGPKL RLHQCGLPRE MALELFQPFV IRALLEESGV KNIRAAKNLL
QRRSQMVWDI LDTVVLGHPV LLNRAPTLHR LGIQAFEPIL LSGRAIQLHP LVCPAFNADF
DGDQMAVHVP LGLEAQAEAR LLMLATHNWL SPATGEPSIL PSQDMILGFY YLTTLKPTVS
LKRPVEQPMA VRGRNLIQSN SIFNNFESVL HAYETSKVDL HEIIWLRWSS YIQTTNSEPL
QITVNKTGHV TTVYDSFVMQ SGATNGPDNS MLSVQMKSRD TSSISKVYNC LTSLNAAAFY
ILTTPGRVLF NNLIYENLFL
