ID   RPOC2_MAIZE             Reviewed;        1527 AA.
AC   P16025;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 121.
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   Zea mays (Maize).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2381419; DOI=10.1007/bf00259403;
RA   Igloi G.L., Meinke A., Doery I., Koessel H.;
RT   "Nucleotide sequence of the maize chloroplast rpo B/C1/C2 operon:
RT   comparison between the derived protein primary structures from various
RT   organisms with respect to functional domains.";
RL   Mol. Gen. Genet. 221:379-394(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2308853; DOI=10.1093/nar/18.3.663;
RA   Igloi G.L., Meinke A., Doery I., Koessel H.;
RT   "Nucleotide and derived amino acid sequence of rps2 from maize
RT   chloroplasts.";
RL   Nucleic Acids Res. 18:663-663(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. B73;
RX   PubMed=7666415; DOI=10.1006/jmbi.1995.0460;
RA   Maier R.M., Neckermann K., Igloi G.L., Koessel H.;
RT   "Complete sequence of the maize chloroplast genome: gene content, hotspots
RT   of divergence and fine tuning of genetic information by transcript
RT   editing.";
RL   J. Mol. Biol. 251:614-628(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52.
RX   PubMed=2304916; DOI=10.1073/pnas.87.4.1531;
RA   Hu J., Bogorad L.;
RT   "Maize chloroplast RNA polymerase: the 180-, 120-, and 38-kilodalton
RT   polypeptides are encoded in chloroplast genes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:1531-1535(1990).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1316-1527.
RC   STRAIN=cv. FR9cms X FR37; TISSUE=Leaf;
RX   PubMed=2140888; DOI=10.1093/nar/18.10.3073;
RA   Stahl D., Rodermel S., Subramanian A.R., Bogorad L.;
RT   "Nucleotide sequence of a 3.46 kb region of maize chloroplast DNA
RT   containing the gene cluster rpoC2-rps2-atpI-atpH.";
RL   Nucleic Acids Res. 18:3073-3074(1990).
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; X17318; CAA35197.1; -; Genomic_DNA.
DR   EMBL; M31208; AAA84489.1; -; Genomic_DNA.
DR   EMBL; X86563; CAA60278.1; -; Genomic_DNA.
DR   EMBL; X52270; CAA36511.1; -; Genomic_DNA.
DR   PIR; S12802; RNZMB2.
DR   RefSeq; NP_043017.1; NC_001666.2.
DR   AlphaFoldDB; P16025; -.
DR   STRING; 4577.GRMZM5G892247_P01; -.
DR   PaxDb; P16025; -.
DR   PRIDE; P16025; -.
DR   GeneID; 845227; -.
DR   KEGG; zma:845227; -.
DR   MaizeGDB; 69586; -.
DR   eggNOG; ENOG502QPYA; Eukaryota.
DR   HOGENOM; CLU_000524_1_0_1; -.
DR   OMA; IEGKSDW; -.
DR   OrthoDB; 731145at2759; -.
DR   Proteomes; UP000007305; Chloroplast.
DR   Genevisible; P16025; ZM.
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; Reference proteome; Transcription;
KW   Transferase; Zinc.
FT   CHAIN           1..1527
FT                   /note="DNA-directed RNA polymerase subunit beta''"
FT                   /id="PRO_0000067929"
FT   REGION          644..681
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          712..793
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        644..659
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        712..738
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        739..782
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         220
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         296
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         303
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         306
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   CONFLICT        25
FT                   /note="R -> S (in Ref. 4; AAA84489)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1527 AA;  176083 MW;  98BEA0C3165A8C3D CRC64;
     MAERANLVFH NKEIDGTAMK RLISRLIDHF GMGYTSHILD QIKTLGFHQA TTTSISLGIE
     DLLTIPSKGW LVQDAEQQSF LLEKHYYYGA IHAVEKLRQS VEIWYATSEY LKQEMNSNFR
     ITDPSNPVYL MSFSGARGNA SQVHQLVGMR GLMADPQGQM IHLPIQSNLR EGLSLTEYII
     SCYGARKGVV DTAVRTADAG YLTRRLVEVV QHIIVRRRDC GTIQGISVSP QNGMTEKLFV
     QTLIGRVLAD DIYIGSRCIA SRNQDIGIGL VNRFITAFRA QPFRAQPIYI RTPFTCRSTS
     WICQLCYGRS PTHGDLVELG EAVGIIAGQS IGEPGTQLTL RTFHTGGVFT GGTADLIRSP
     SNGKIQFNED LVHPTRTRHG QPAFLCYIDL HVTIQSQDIL HSVNIPLKSL ILVQNDQYVE
     SEQVIAEIRA GTSTLHFKEK VQKHIYSESD GEMHWSTDVY HAPEYQYGNL RRLPKTSHLW
     ILSVSMCRSS IASFSLHKDQ DQMNTYSFSV DGRYIFDFSM ANDQVSHRLL DTFGKKDREI
     LDYLTPDRIV FNGHWNCFYP SILQDNSDLL AKKRRNRLVV PLQYHQEQEK ERISCLGISM
     EIPFMGVLRR NTIFAYFDDP RYRKDKRGSG IVKFRYRTLE EEYRTQEEEY RTREEEYRTR
     EEDSEDEYES PENKYRTREG EGEYKILEDE YRTLEDEYET LEDEYGILED EYRTLEKDSE
     EEYGSLENKY RTREGEGEYE ILEEESEEEY GSSEDGSEKE YGTLEEDSEE DSEEDSEDEY
     GSPEEDSILK KEGFIEHRGT KEFSLKYQKE VDRFFFILQE LHILPRSSSL KVLDNSIIGV
     DTQLTKNTRS RLGGLVRVKR KKSHTELKIF SGDIHFPEEA DKILGGSLIP PEREKKDSKE
     SKKRKNWVYV QRKKFLKSKE KYFVSVRPAV AYEMDEGINL ATLFPQDLLQ EEDNLQLRLV
     NFISHENSKL TQRIYHTNSQ FVRTCLVVNW EQEEKEGARA SLVEVKTNDL IRDFLRIELV
     KSTILYTRRR YDRTSVGLIP NNRLDRNNTN SFYSKAKIQS LSQHQEVIGT LLNRNKEYPS
     LMILLASNCS RIGLFKNSKY PNAVKESNPR IPIRDIFGLL GVIVPSISNF SSSYYLLTHN
     QILLKKYLFL DNLKQTLQVL QGLKYSLIDE NKRISNFDSN IMLEPFHLNW HFLHHDSWEE
     TLAIIHLGQF ICENLCLFKL HIKKSGQIFI VNMDSFVLRA AKPYLATIGA TVHGHYGKIL
     YKGDRLVTFI YEKSRSSDIT QGLPKVEQIF EARSIDSLSP NLERRIEDWN ERIPRILGVP
     WGFLIGAELT IAQSRISLVN KIQKVYRSQG VQIHNRHIEI IIRQVTSKVR VSEDGMSNVF
     LPGELIGLLR AERAGRALDE SIYYRAILLG ITRASLNTQS FISEASFQET ARVLAKAALR
     GRIDWLKGLK ENVVLGGIIP VGTGFQKFVH RSPQDKNLYL EIQKKNLFAS EMRDILFLHT
     ELVSSDSDVT NNFYETSETP FTPIYTI