RPOC1_LACSA
ID RPOC1_LACSA Reviewed; 689 AA.
AC Q56P12; Q1KXP2; Q332Z0;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 64.
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}; ORFNames=PSC013;
OS Lactuca sativa (Garden lettuce).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Cichorioideae; Cichorieae;
OC Lactucinae; Lactuca.
OX NCBI_TaxID=4236;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15917497; DOI=10.1093/molbev/msi174;
RA Kim K.-J., Choi K.-S., Jansen R.K.;
RT "Two chloroplast DNA inversions originated simultaneously during the early
RT evolution of the sunflower family (Asteraceae).";
RL Mol. Biol. Evol. 22:1783-1792(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Cisco;
RX PubMed=16604461; DOI=10.1007/s11248-005-3997-2;
RA Kanamoto H., Yamashita A., Asao H., Okumura S., Takase H., Hattori M.,
RA Yokota A., Tomizawa K.;
RT "Efficient and stable transformation of Lactuca sativa L. cv. Cisco
RT (lettuce) plastids.";
RL Transgenic Res. 15:205-217(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Salinas;
RA Timme R.E., Kuehl J.V., Boore J.L., Jansen R.K.;
RT "A comparison of the first two published chloroplast genomes in Asteraceae:
RT Lactuca and Helianthus.";
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_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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABD47221.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY865171; AAX58143.1; -; Genomic_DNA.
DR EMBL; AP007232; BAE47582.1; -; Genomic_DNA.
DR EMBL; DQ383816; ABD47221.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_398317.1; NC_007578.1.
DR AlphaFoldDB; Q56P12; -.
DR SMR; Q56P12; -.
DR PRIDE; Q56P12; -.
DR GeneID; 3772823; -.
DR KEGG; lsv:3772823; -.
DR OrthoDB; 774084at2759; -.
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; 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; 2.
DR SMART; SM00663; RPOLA_N; 1.
PE 3: Inferred from homology;
KW Chloroplast; DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Plastid; Transcription; Transferase; Zinc.
FT CHAIN 1..689
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067877"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 489
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 491
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 493
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT CONFLICT 144
FT /note="N -> G (in Ref. 1; AAX58143 and 3; ABD47221)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="K -> E (in Ref. 1; AAX58143)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 689 AA; 80131 MW; 9122E577FB435C52 CRC64;
MIDRYTHQQL RIGLVSPQQI STWSKKILPN GEIVGEVTKP YTFHYKTNKP EKDGLFCERI
FGPIKSGICA CGNYRVIGDE KEDPQFCEQC GVEFVDSRIR RYQMGYIKLA YPVMHVWYLK
RLPSYIVTLL DKPLNELEDL VYCNFYFARP IDKKPTFLRL RGLLEYEIQP WKYRIPIFFT
TRSFDTFRNR EMSTGGGSIR QQLANLDLRI IIDYSLVEWK ELEEEEPTGN EWEDRKVGRR
KDFLLRRMEL AKHFIRTNIE PKWMVLRLLP VLPPELRPIY HIDEDKLVTS DINEIYRRII
YRNNTLTDLL TTSIATPEEL IISQEKLLQE AVDALLDNGI CGQPMRDDHN RVYKSLSDVI
EGKEGRVRET LLGKRVDYSG RSVIVVGPSL SLHRCGLPRE IAIELFQAFV IRDLIRKHLA
SNIGVAKSQI RKKKPIVWEI LQEILDDHPV LLNRAPTLHR LGIQAFLPVL VEGRAICLHP
LVCKGFNADF DGDQMAVHVP LSLEAQAEAR LLMFSHMNLL SPTIGDPISA PTQDMLSGLY
VLTSGNRRGI CVNRYNPCNR RNYQNEDNNY KYTKKKEPFF CNPYDAIGAY RQKRINLGSP
LWLRWRLDQR VIAAREVPIE IHYESVGTYY EIYGHYLIVR SIKKEILYIY IRTTLGHISL
YREIEEAIQG FWQGCCNSML PTGIRVSPG
