ID   RPOC2_LOLPR             Reviewed;        1466 AA.
AC   A8Y9G2;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 55.
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=LopeCp025;
OS   Lolium perenne (Perennial ryegrass).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Poodae; Poeae; Poeae Chloroplast Group 2 (Poeae type); Loliinae;
OC   Lolium.
OX   NCBI_TaxID=4522;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Cashel;
RX   PubMed=18665252; DOI=10.1371/journal.pone.0002813;
RA   Diekmann K., Hodkinson T.R., Fricke E., Barth S.;
RT   "An optimized chloroplast DNA extraction protocol for grasses (Poaceae)
RT   proves suitable for whole plastid genome sequencing and SNP detection.";
RL   PLoS ONE 3:E2813-E2813(2008).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM777385; CAO85968.1; -; Genomic_DNA.
DR   RefSeq; YP_001531275.1; NC_009950.1.
DR   AlphaFoldDB; A8Y9G2; -.
DR   GeneID; 5696651; -.
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..1466
FT                   /note="DNA-directed RNA polymerase subunit beta''"
FT                   /id="PRO_0000353569"
FT   REGION          615..725
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        618..633
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        661..688
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        705..722
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"
SQ   SEQUENCE   1466 AA;  168279 MW;  5D2CA8F379852BB7 CRC64;
     MAERANLVFH NKEIDGTGMK RLISRLIDHF GMGYTSHILD QLKTLGFHQA TTTSISLGIE
     DLLTIPSKGW LVQDAEQQSF LLEKHYYYGA IHAVEKLRQS VEIWYATSEY LKQEMNSNFR
     ITDPSNPVYL MSFSGARGNA SQVHQLVGMR GLMADPQGQM IDLPIQSNLR EGLSLTEYII
     SCYGARKGVV DTAVRTADAG YLTRRLVEVV QHIIVRRRDC GTIRGISVSP QNGMTEKLFV
     QTLIGRVLAD DIYIGSRCIA ARNQDIGIGL VNRFITAFRA QPFLAQPIYI RTPFTCRSTS
     WICQLCYGRS PTHSDLVELG EAVGIIAGQS IGEPGTQLTL RTFHTGGVFT GGTADLVRSP
     SNGKIQFTEN LVHPTRTRHG QPAFLCYIDL HVTIQSQDIL YSVNIPSKSL ILVQNDQYVK
     SEQVIAEIRA GTPTLHFKER VQKHIYSESD GEMHWSTDVY HAPEYQYGNL RRLPKTSHLW
     ILSVSRCRSS IASFSLHKDQ DQMNTYGKKD REIFDYSTLV RIMPNGHWNL IYPSIFKENS
     DLLAKKRRNR FVIPLQYHQE QEKELISCLG ISIEIPFMGV LHRNTIFAYF DDPRYRKDKK
     GSGIVKFRYR TLEEEYRTRE EDSEDEYETL EEEYRTREDE YEYETLEDEY GSPENEYGNP
     ENEYRTLEKD SEDEYGSPES KYGTLEEDSE DDYGSPGESS EDKYGTLEED LEEESEDEYE
     SPEEDSIFKK EGLIEHRGTK EFSLKYQKEV DRFFFILQEL HILPRSSSLK VLDNSIIGVD
     TQLTKNTRSR LGGLVRVKRK KSHTELKIFS GDIHFPEEAD KVLGGCLIPP ERQKKDSKES
     KKSKNWVYVQ RKKIIKSKEK YFVSIRPAVA YEMDEGRNLA TLFPQDLLQE EDNLQLRLVN
     FISHENSKLT QRIYHTNSQF VRTCLVVNWE QEKKEKAGAS LVEVRANDLI RDFLRIELIK
     CTISYTRKRY DRTSAGPIPH NRLDHTNLNS FYSKAKIESL SQHQEAIGTL LNRNKEYQSL
     MILSASNCSQ IGLFKNPKHP NTIKELNRRI PIREIFGPLG VIVPSISNFS SSYYLLTHNK
     ILLKKYLFLD NLKQTFQVLQ GLKYSLIDEN KRISNFDSNI MLDPFLLNCH FVHHDSWEET
     SAIIHLGQLI CENVCLFKSH IKKSGQIFII NMDSFVIRAA KPYLATTGAT VNGHYGEILY
     KGDRLVTFIY EKSRSSDITQ GLPKVEQIFE ARSIDSLSPN LERRIEDWNE RIPRILGIPW
     GFLIGAELTI AQSRISLVNK IQKVYRSQGV QIHNRHIEII IRQVTSKVRV SEDGMSNVFS
     PGELIGLLRA ERAGRALDES IYYRAILLGI TRASLNTQSF ISEASFQETA RVLAKAALRG
     RIDWLKGLKE NVVLGGIIPV GTGFQKFVHR SPQDKNLYFE IQKQNLFASE MRDFLFLHTE
     LVSSDSDITN NFYETLEPPF TPIYTS