ID   RPOC1_SOLLC             Reviewed;         681 AA.
AC   Q2MIA9;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 2.
DT   03-AUG-2022, entry version 80.
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};
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. LA3023;
RX   PubMed=16575560; DOI=10.1007/s00122-006-0254-x;
RA   Daniell H., Lee S.-B., Grevich J., Saski C., Quesada-Vargas T., Guda C.,
RA   Tomkins J., Jansen R.K.;
RT   "Complete chloroplast genome sequences of Solanum bulbocastanum, Solanum
RT   lycopersicum and comparative analyses with other Solanaceae genomes.";
RL   Theor. Appl. Genet. 112:1503-1518(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. IPA-6;
RX   PubMed=16830097; DOI=10.1007/s00239-005-0254-5;
RA   Kahlau S., Aspinall S., Gray J.C., Bock R.;
RT   "Sequence of the tomato chloroplast DNA and evolutionary comparison of
RT   solanaceous plastid genomes.";
RL   J. Mol. Evol. 63:194-207(2006).
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=ABC56291.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAJ32384.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; DQ347959; ABC56291.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AM087200; CAJ32384.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; AP_004919.1; AC_000188.1.
DR   RefSeq; YP_008563079.1; NC_007898.3.
DR   AlphaFoldDB; Q2MIA9; -.
DR   SMR; Q2MIA9; -.
DR   STRING; 4081.Solyc10g031560.1.1; -.
DR   PaxDb; Q2MIA9; -.
DR   PRIDE; Q2MIA9; -.
DR   GeneID; 3950486; -.
DR   KEGG; sly:3950486; -.
DR   OrthoDB; 774084at2759; -.
DR   Proteomes; UP000004994; 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; 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; Reference proteome; Transcription;
KW   Transferase; Zinc.
FT   CHAIN           1..681
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000277178"
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"
SQ   SEQUENCE   681 AA;  78580 MW;  9113C715172F76B1 CRC64;
     MIDRYKHQQL RIGSVSPQQI SAWATKILPN GEIVGEVTKP YTFHYKTNKP EKDGLFCERI
     FGPIKSGICA CGNYRVIGDE KEDPKFCEQC GVEFVDSRIR RYQMGYIKLA CPVTHVWYLK
     RLPSYIANLL DKPLKELEGL VYCDFSFARP ITKKPTFLRL RGLFEYEIQS WKYSIPLFFT
     TQGFDTFRNR EISTGAGAIR EQLADLDLRI IIENSLVEWE ELGEEGHTGN EWEDRKVGRR
     KDFLVRRVEL AKHFIRTNIE PEWMVLCLLP VLPPELRPII QIDGGKLMSS DINELYRRVI
     YRNNTLTDLL TTSRSTPGEL VMCQEKLVQE AVDTLLDNGI RGQPMRDGHN KVYKSFSDVI
     EGKEGRFRET LLGKRVDYSG RSVIVVGPSL SLHRCGLPRE IAIELFQTFV IRGLIRQHLA
     SNIGVAKSKI REKEPIVWEI LQEVMQGHPV LLNRAPTLHR LGIQAFQPVL VEGRAICLHP
     LVCKGFNADF DGDQMAVHVP LSLEAQVEAR LLMFSHMNLL SPAIGDPISV PTQDMLIGLY
     VLTSGNHRGI CVNRYNPCNR RNYQNQKRSD NSYYKYTKEP FFSNSYDAIG AYRQKRINLD
     SPLWLRWRLD QRVIASRETP IEVHYESLGT FYEIYGHYLI VRSLKKKILF IYIRTTVGHI
     ALYREIEEAI QGFSRAYSYA T