ID   RPOC2_CHLVU             Reviewed;        1562 AA.
AC   P12465;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01324};
DE   AltName: Full=PEP {ECO:0000255|HAMAP-Rule:MF_01324};
DE   AltName: Full=Plastid-encoded RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
DE            Short=RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
GN   Name=rpoC2 {ECO:0000255|HAMAP-Rule:MF_01324};
OS   Chlorella vulgaris (Green alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX   NCBI_TaxID=3077;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAM C-27 / Tamiya;
RX   PubMed=9159184; DOI=10.1073/pnas.94.11.5967;
RA   Wakasugi T., Nagai T., Kapoor M., Sugita M., Ito M., Ito S., Tsudzuki J.,
RA   Nakashima K., Tsudzuki T., Suzuki Y., Hamada A., Ohta T., Inamura A.,
RA   Yoshinaga K., Sugiura M.;
RT   "Complete nucleotide sequence of the chloroplast genome from the green alga
RT   Chlorella vulgaris: the existence of genes possibly involved in chloroplast
RT   division.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:5967-5972(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1323-1562.
RC   STRAIN=IAM C-27 / Tamiya;
RX   AGRICOLA=IND92000630; DOI=10.1007/BF00027401;
RA   Yoshinaga K., Ohta T., Suzuki Y., Sugiura M.;
RT   "Chlorella chloroplast DNA sequence containing a gene for the large subunit
RT   of ribulose-1, 5-bisphosphate carboxylase and a part of a possible gene for
RT   the beta' subunit of RNA polymerase.";
RL   Plant Mol. Biol. 10:245-250(1988).
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_01324}.
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_01324};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01324};
CC       Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01324};
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_01324}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC       Rule:MF_01324}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01324}.
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DR   EMBL; AB001684; BAA57971.1; -; Genomic_DNA.
DR   EMBL; M20655; AAA84107.1; -; Genomic_DNA.
DR   PIR; JE0011; JE0011.
DR   PIR; T07323; T07323.
DR   RefSeq; NP_045895.2; NC_001865.1.
DR   AlphaFoldDB; P12465; -.
DR   SMR; P12465; -.
DR   PRIDE; P12465; -.
DR   GeneID; 809119; -.
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: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   HAMAP; MF_01324; RNApol_bact_RpoC2; 1.
DR   InterPro; IPR012756; DNA-dir_RpoC2_beta_pp.
DR   InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR   InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR   InterPro; IPR007083; RNA_pol_Rpb1_4.
DR   InterPro; IPR007081; RNA_pol_Rpb1_5.
DR   InterPro; IPR038120; Rpb1_funnel_sf.
DR   PANTHER; PTHR19376; PTHR19376; 4.
DR   Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR   Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR   TIGRFAMs; TIGR02388; rpoC2_cyan; 1.
PE   3: Inferred from homology;
KW   Chloroplast; DNA-directed RNA polymerase; Metal-binding;
KW   Nucleotidyltransferase; Plastid; Transcription; Transferase; Zinc.
FT   CHAIN           1..1562
FT                   /note="DNA-directed RNA polymerase subunit beta''"
FT                   /id="PRO_0000067920"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         275
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         338
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         345
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         348
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ   SEQUENCE   1562 AA;  178711 MW;  631E52784742B06B CRC64;
     MVKKKKFKTK NIQNPPFSSQ NSSHLFFSLK KKEEKESTPE VFVIDDHFNT FKTPKALKFR
     TPIFFNVSFD KNTLKTVIAW FLDQYGGKAT VDLVETLKQV GFHQATRAGV SLGLEDLQIP
     PQKASFLSAA SVSGVEAAQA LETGNLTSVE KSQRLIDTWN KTSESLRQAA VHNFRATNPV
     NPVYMMAFSG ARGNISQVRQ LVAMRGLMAD PQGAILEFPI QSNFREGLTI TEYLLSCYGA
     RKGLVDTALR TASAGYLTRR LVDAVQHVVI YTKNCKTEKG ITFKGLHIEQ NLLGRVLLKD
     VILNTTTVIP KDTLVSSSLA KKLAAINQKI FVRSPLTCQT EKTVCQLCYG LDLAQGKLVC
     FGEAVGIIAA QSIGEPGTQL TMRTFHTGGV GVFSEQAMKS FPAPFDGKIE FQEALPGRFV
     RTPYGKIVYL LKHTGTNPKQ VLLRVVSSSL TMRPLVYEIL HQDVPAGSLL WVKQGEDVRT
     GQLLVQGSRL QKSKQKMPES THIVRTPFSG ELFFEHMPIV SLEKIITRGP RTNPKEEFSP
     IKVFLKDLGR FWVFSSFIQK QTFSFLDQKK GKANSFFFKG DLVSAETPLS QYNLQIPVRG
     HLKKLGSSVV LAQTVFKFCF SKIYYFSKFY FLVENQNLIA STTTLNFTSL TWYPFFNQFE
     TSGYYVDLSF SSDSEVLKTT ELTKVKSETY DFTKNGGFFT SHQSFVGSTT RVFLLKTFEF
     FSAASKQTQK TALERLPFVD SMSFSLEKIQ LKKQNQKRKE NPLFSLEVGK VKRNTQQRLP
     QFGFMVTCEE NSLSRKGIFQ IKKAQEKNWS HKKTFQLSFL LNPKKRKKPL KKHFMCSSLF
     LEKAVKRAQT TFGIQTETKL IEKKCSWFSV SKNFTDFSSQ LTGIVLEPGK HMESFSFQHS
     YVSVNLISRE NVFLVKSKTK RSQFSYVLKD LLSSSRFCHK VFEKNFSEQK MESVEKISQI
     FSSQTESFFS RNNQLLSFFS QKKRIKNKLF FHSQLNFPSK MPRRSDVLNS SKLLFFTREF
     LSDFSFYKRK ELIQKRERKP HTLQNIKVKN KKFLQVIQPC FQLKKKRCLS NLFFLQKLSY
     QIFPERKFFY ETWLNQSSFD FSLPSPFSTK QFKTTGFFSK NELQKASFDF QPSFLSQKIS
     SSSQLTLRGS WVSMTNSFKI HFEVKTPKFF GKIEEFQQKK FFDKKLKFGI QSPSKSLSKA
     LSFGIPIPEF SLAVSRKIIF EKAHTYIFQS FQCRQVLPKV PITQVFLKSK TVGEFQRIQL
     KNQKGSSSFL RAEDTVTFLL PSLVPKKQSF LKKEEKVLVS CGQRIRWGQE IFPGFASSLS
     GRILDITATQ ITVRKALPFL GSRRGLVHVA QNDLLQKNHI LMTLRSKQLQ TEDIVQGIPK
     IEQLFEARET KDGEIIRYNM HFRLNSFFSL AKRVKPFLEA FDLSLLYIQR FLVKTLLEAY
     SNQGVNIAEK HVEVVVRQMT ARVRITFGKD TSLLPGEFIQ LRLLEEINRS LVEAKKEPAL
     YEPVILGLTK SVLQSESFLL AASFQQVSKV LVRSALATKT DFLRGLMKPL YVASLSQREQ
     EL