ID   RPOC2_PEA               Reviewed;        1163 AA.
AC   P12227;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta'';
DE            EC=2.7.7.6;
DE   AltName: Full=PEP;
DE   AltName: Full=Plastid-encoded RNA polymerase subunit beta'';
DE            Short=RNA polymerase subunit beta'';
DE   Flags: Fragment;
GN   Name=rpoC2;
OS   Pisum sativum (Garden pea).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3530249; DOI=10.1042/bj2360453;
RA   Cozens A.L., Walker J.E.;
RT   "Pea chloroplast DNA encodes homologues of Escherichia coli ribosomal
RT   subunit S2 and the beta'-subunit of RNA polymerase.";
RL   Biochem. J. 236:453-460(1986).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       {ECO:0000250}.
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:0000250|UniProtKB:P0A8T7};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P0A8T7};
CC       Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000250|UniProtKB:P0A8T7};
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X03912; CAA27545.1; -; Genomic_DNA.
DR   PIR; S07137; S07137.
DR   AlphaFoldDB; P12227; -.
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:InterPro.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR   InterPro; IPR007081; RNA_pol_Rpb1_5.
DR   PANTHER; PTHR19376; PTHR19376; 1.
DR   Pfam; PF04998; RNA_pol_Rpb1_5; 2.
PE   3: Inferred from homology;
KW   Chloroplast; DNA-directed RNA polymerase; Metal-binding;
KW   Nucleotidyltransferase; Plastid; Transcription; Transferase; Zinc.
FT   CHAIN           <1..1163
FT                   /note="DNA-directed RNA polymerase subunit beta''"
FT                   /id="PRO_0000067939"
FT   BINDING         16
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT   BINDING         87
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT   BINDING         94
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT   BINDING         97
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT   NON_TER         1
SQ   SEQUENCE   1163 AA;  133599 MW;  C92E7BE0A3FDB525 CRC64;
     RLVEVVQHIV VRRTDCGTIR GISVNTRNGM MPEIILIQTL IGRVVAENIY IGSRCIVVRN
     QDIGIGLINR FITFQTQPIF IRTPFTCRNT SWICRLCYGR SPIHGDLVEL GEAVGIIAGQ
     SIGEPGTQLT LRTFHTGGVF TGGTAEYVRA PSNGKIKLNE DLVHPTRTRH GYPAFICNID
     LYVTIESDDI IHNVIIPPKS FLLVQNDQYV KSEQVIAEIR AGTYTFNLKE RVRKHIYSDS
     EGEMHWSTDV YHASEFMYSN VHILPKTSHL WILSGKSCRS NTIHFLLRKD QDQITMDSLS
     NGKTNISNLL ERNDQVKHKL FRFNTFGTKE KGISDYSIFN EIICTDHSYP AIFHDTFYFL
     AKRRRNRFLI PFPFQSIQER KNERMSPSGV SIEIPINGIF HRNSIFAYFD DPQYRRHSSG
     ITKYRTIGIH SIFQKEDFIE YRGIKELKPK SQIQVDRFFF IPEEVHILPK SSSLMVRNNS
     LVGIGTPITF NIRSRVGGLV RLDKKKKKIE LKIFSGNIHF PGEMDKISRH SAILIPPGTV
     KKKKCNKSKK IKNWIYVQWI ATTKKKYFVL VRPVILYEIP DSNNFVKLFP QDLFQEKDNL
     ELKVVNYILY GNGKSIRGIS DTRIQLVRTC LVFNWDDGKN SSSIEEAPAS FIEVRTNGLI
     EYFLRIDLVK SNTSYIRKRN EPSGFGLIGD NKSDRINPFF SIHSKGKIQQ SLSQNHGTIR
     MLLNRNKECR SWIILSSSNC FQMRPFNNEK SHNGIKKDPI ISINNNGPLG IALQVANFYS
     LYHLITHNQI SIIKNLQLDK LTEIFQVIKY YLMDENDKIC KPDLYSNIIL NPFHLNWFFL
     HHFYCEKTFT RISLGQFICE NICIAQMKNR PHLKLKSGQV IIVQMDSVII RSANPYLATP
     GATIHGHYGE ILSQGDILVT FIYEKSRSGD ITQGLPKVEQ ILEIRSIDSI SMNLEKRIDA
     WNECITKIIG IPWGFLIGAE LTIAQSRISL VNKIQKVYRS QGVHIHNRHI EIIVRQITSK
     VLVSEDGMSN IFLPGELIGL LRAERTGRAL EEAICYRALL LGVTKTSLNT QSFISEASFQ
     ETARVLAKAA LRGRIDWLKG LKENVVLGGM IPVGTGFKRI MHRSRSRQHN KITRKKKLFE
     VEIRNLLFHH RKLLDFANFK EFM