RPOC2_SOLTU
ID RPOC2_SOLTU Reviewed; 1392 AA.
AC Q2VEI6; Q27S60;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 65.
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 Solanum tuberosum (Potato).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Desiree;
RX PubMed=16835751; DOI=10.1007/s00299-006-0196-4;
RA Chung H.-J., Jung J.D., Park H.-W., Kim J.-H., Cha H.W., Min S.R.,
RA Jeong W.-J., Liu J.R.;
RT "The complete chloroplast genome sequences of Solanum tuberosum and
RT comparative analysis with Solanaceae species identified the presence of a
RT 241-bp deletion in cultivated potato chloroplast DNA sequence.";
RL Plant Cell Rep. 25:1369-1379(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Desiree;
RA Gargano D., Scotti N., Vezzi A., Bilardi A., Valle G., Grillo S., Cardi T.;
RT "Complete chloroplast genome sequences of Solanum tuberosum cultivar
RT Desiree and comparative analyses with other Solanaceae genomes.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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; DQ231562; ABB90033.1; -; Genomic_DNA.
DR EMBL; DQ386163; ABD47047.1; -; Genomic_DNA.
DR RefSeq; YP_635629.1; NC_008096.2.
DR AlphaFoldDB; Q2VEI6; -.
DR SMR; Q2VEI6; -.
DR STRING; 4113.PGSC0003DMT400052303; -.
DR GeneID; 4099930; -.
DR KEGG; sot:4099930; -.
DR eggNOG; ENOG502QPYA; Eukaryota.
DR OrthoDB; 731145at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
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..1392
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000225338"
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"
FT CONFLICT 916
FT /note="P -> S (in Ref. 2; ABD47047)"
FT /evidence="ECO:0000305"
FT CONFLICT 1085
FT /note="E -> K (in Ref. 2; ABD47047)"
FT /evidence="ECO:0000305"
FT CONFLICT 1095
FT /note="F -> V (in Ref. 2; ABD47047)"
FT /evidence="ECO:0000305"
FT CONFLICT 1128..1131
FT /note="NQGN -> YEGD (in Ref. 2; ABD47047)"
FT /evidence="ECO:0000305"
FT CONFLICT 1142..1144
FT /note="ISD -> RSG (in Ref. 2; ABD47047)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1392 AA; 157158 MW; A904504F601FBCBA CRC64;
MEVLMAERAN LVFHNKAIDG TAMKRLISRL IEHFGMAYTS HILDQVKTLG FQQATATSIS
LGIDDLLTIP SKGWLVQDAE QQSLILEKHH HYGNVHAVEK LRQSIEIWYA TSEYLRQEMN
PNFRMTDPFN PVHIMSFSGA RGNASQVHQL VGMRGLMSDP QGQMIDLPIQ SNLREGLSLT
EYIISCYGAR KGVVDTAVRT SDAGYLTRRL VEVVQHIVVR RTDCGTARGI SVSPRNGIMP
ERIFSQTLIG RVLADDIYMG SRCIATRNQA IGIGLVNRFI TFRAQPISIR TPFTCRSTSW
ICRLCYGRSP THGDLVELGE AVGIIAGQSI GEPGTQLTLR TFHTGGVFTG GTAEHVRAPS
NGKIKFNEDL VHPTRTRHGH PAFLCSIDLY VTIESEDILH NVNIPPKSLL LVQNDQYVES
EQVIAEIRAG ISTLNFKEKV RKHIYSDSDG EMHWSTDVYH APEFTYGNVH LLPKTSHLWI
LLGGPCRSSL VYLSIHKDQD QMNAHSLSGK RRYTSNLSVT NDQARQKLFS SDFYGQKEDR
IPDYSDLNRI ICTGQYNLVY SPILHGNSDL LSKRRRNKFI IPLHSIQELE NELMPCSGIS
IEIPVNGIFR RNSILAYFDD PRYRRKSSGI IKYGTIETHS VIKKEDLIEY RGVKEFRPKY
QMKVDRFFFI PEEVHILPGS SSIMVRNNSI VGVDTQITLN LRSRVGGLVR VERKKKRIEL
KIFSGDIHFP GETDKISRHT GVLIPPGTGK RNSKEYKKVK NWIYVQRITP SKKRFFVLVR
PVVTYEITDG INLGTLFPPD PLQERDNVQL RIVNYILYGN GKPIRGISDT SIQLVRTCLV
LNWNQDKKSS SCEEARASFV EIRTNGLIRH FLRINLVKSP ISYIGKRNDP SGSGLLSDNG
SDCTNINPFS AIYSYPKAKI QQSLNQPQGT IHTLLNRNKE CQSLIILSAA NCSRMEPFKD
VKYHSVIKES IKKDPLIPIR NSLGPLGTCL PIENFYSSYH LITHNQILVT KYLQLDNLKQ
TFQVIKLKYY LMDENGKIFN PDPCRNIILN PVNLNWSFLH HNYCAETSKI ISLGQFICEN
VCIAENGPPL KSGQFILVQV DSIVIRSAKP YLATPGATVH GHYGETLNQG NTLVTFIYEK
SISDDITQGL PKVEQVLEVR SIDSISMNLE KRVESWNKCI PRILGIPWGF LIGAELTIAQ
SRISLVNKIQ QVYRSQGVQI HNRHIEIIVR QITSKVLISE DGMSNVFSPG ELIGLLRAER
MGRALEEAIC YRVVLLGITR ASLNTQSFIS EASFQETARV LAKAALRGRI DWLKGLKENV
VLGGVIPVGT GFKGLVHPSK QHNNIPLETK KTNLFEGEMR DILFHHRKLF DSCLSKKFHD
IPEQSFIGFN DS
