ID   RPOC2_CUCSA             Reviewed;        1394 AA.
AC   Q4VZP3; A5J1S4;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 57.
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}; OrderedLocusNames=CsCp016;
OS   Cucumis sativus (Cucumber).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3659;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Baekmibaekdadagi;
RX   PubMed=16362300; DOI=10.1007/s00299-005-0097-y;
RA   Kim J.-S., Jung J.D., Lee J.-A., Park H.-W., Oh K.-H., Jeong W.J.,
RA   Choi D.-W., Liu J.R., Cho K.Y.;
RT   "Complete sequence and organization of the cucumber (Cucumis sativus L. cv.
RT   Baekmibaekdadagi) chloroplast genome.";
RL   Plant Cell Rep. 25:334-340(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Borszczagowski;
RX   PubMed=17607527; DOI=10.2478/s11658-007-0029-7;
RA   Plader W.W., Yukawa Y., Sugiura M., Malepszy S.;
RT   "The complete structure of the cucumber (Cucumis sativus L.) chloroplast
RT   genome: its composition and comparative analysis.";
RL   Cell. Mol. Biol. Lett. 12:584-594(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chipper, and cv. Gy14;
RX   PubMed=17546086; DOI=10.1139/g07-003;
RA   Chung S.-M., Gordon V.S., Staub J.E.;
RT   "Sequencing cucumber (Cucumis sativus L.) chloroplast genomes identifies
RT   differences between chilling-tolerant and -susceptible cucumber lines.";
RL   Genome 50:215-225(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_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; DQ119058; AAZ94641.1; -; Genomic_DNA.
DR   EMBL; AJ970307; CAJ00748.1; -; Genomic_DNA.
DR   EMBL; DQ865975; ABI97407.1; -; Genomic_DNA.
DR   EMBL; DQ865976; ABI98735.1; -; Genomic_DNA.
DR   RefSeq; YP_247589.2; NC_007144.1.
DR   AlphaFoldDB; Q4VZP3; -.
DR   STRING; 3659.XP_004174090.1; -.
DR   PRIDE; Q4VZP3; -.
DR   GeneID; 3429304; -.
DR   KEGG; csv:3429304; -.
DR   eggNOG; ENOG502QPYA; Eukaryota.
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; 1.
DR   Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR   Pfam; PF04998; RNA_pol_Rpb1_5; 2.
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..1394
FT                   /note="DNA-directed RNA polymerase subunit beta''"
FT                   /id="PRO_0000225331"
FT   BINDING         224
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         295
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         302
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         305
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ   SEQUENCE   1394 AA;  158204 MW;  0D44E0E29DA81262 CRC64;
     MEVLMAERAD LVFHNKVIDG TAIKRLISRL IDHFGMAYTS HILDQLKTLG FQQATATSIS
     LGIDDLLTIP SKGWLVQDAE QQSLILEKHH HYGNVHAVEK LRQSIEIWYA TSEYLRQEMN
     PNFRMTDPFN PVHIMSFSGA RGNASQVHQL VGMRGLMSDP QGQMIDLPIQ SNLREGLSLT
     EYIISCYGAR KGVVDTAVRT SDAGYLTRRL VEVVQHIVVR RTDCGTIRGI LVSPGNRMIP
     ERIFIQTLIG RVLADDIYMG PRCIGVRNQD IGIGLINRFI TFQTQPISIR TPFTCRSTSW
     ICRLCYGRSP THGDLVELGE AVGIIAGQSI GEPGTQLTLR TFHTGGVFTG GTAEHIRAPS
     NGKIKFNEDL VHPTRTRHGH PAFLCYIDLY VTIESEDIIH NVTIPPKSLL LVQNDQYVES
     EQVIAEIRAG TYTLNLKERV RKHIYSDSEG EMHWSTDVYH APEFTYSNVH LLPKTSHLWI
     LSGGSCGCSL VPFSLYKDQD QINVHSLCVE RRYISSLSVN NDKVGQKFYG PDLSGKNENG
     IPDYSELNPI LCTGQSNLTY PAIFHGNSDL LAKRRRNGFI IQFESLQERE KELRPPSGIS
     IEIPINGIFR RNSILAFFDD PQYRRNSSGI TKYGTIGVHS ILKKEDLIEY RGVKDFKPKY
     QMQMKVDRFF FIPEEVHILP ESSSIMVRNN SIIGVATRLT LSIRSRVGGL VRVEKKKKRI
     ELKIFSGDIH FPGEMDKISR HNGILIPPER VKKNSKKSKK SKNWIYVQWI TPTKKKYFVF
     VRPVIIYELA DGINLVKLFP QDLLQERDNL ELRVANYILY GNGKPIRGIS GTSIQLVRTC
     LLLNWDRDKK SSSIEDARAS FVEVSTNGLV RNFLRIDLGK SDTAYIRKRK DPSGSGLIFN
     NESDRTNINP FFSIYSKTRV PQSPSQNQGT IRTLLNRNKE RQSLIILSAS NCLQIDLFND
     VKDYNVIKES SKKDPLISIR NSLGPLGAAP QIVNFYSFYY LITHNPISLT KYLQLDNLKQ
     IFQVLKYYLM DENGGILNSD PCINIVFNTF NLNWHFLHDN YHNNYCEETP TRISLGQFFF
     ENVCIAKNRP HLKSGQIIIV QVDSLVIRSA KPYLATSGAT VHRHYGEILY EGDTLVTFIY
     EKSRSGDITQ GLPKVEQVLE VRSIDSISMS LEKRIEGWNE RITRILGIPW GFLIGAELTI
     VQSRISLVNK IQKVYRSQGV EIHNRHIEII VRQITSKVLV SEDGMSNVFS PGELIGLLRA
     ERTGRALEEA ICYRAVLLGI TKASLNTQSF ISEASFQETA RVLAKAALRG RIDWLRGLKE
     NVVLGGMIPV GTGFRELAHR SRQHNNIPLE TPPKKIFEGE MRDILFHHKE LFDFFISTNL
     HDTSEQEFLG FNDS