RPOC2_OSTTA
ID RPOC2_OSTTA Reviewed; 1011 AA.
AC Q0P3M4;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=OtCpg00280;
OS Ostreococcus tauri.
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Ostreococcus.
OX NCBI_TaxID=70448;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OTTH0595;
RX PubMed=17251180; DOI=10.1093/molbev/msm012;
RA Robbens S., Derelle E., Ferraz C., Wuyts J., Moreau H., Van de Peer Y.;
RT "The complete chloroplast and mitochondrial DNA sequence of Ostreococcus
RT tauri: organelle genomes of the smallest eukaryote are examples of
RT compaction.";
RL Mol. Biol. Evol. 24:956-968(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; CR954199; CAL36353.1; -; Genomic_DNA.
DR RefSeq; YP_717231.1; NC_008289.1.
DR AlphaFoldDB; Q0P3M4; -.
DR SMR; Q0P3M4; -.
DR STRING; 70448.Q0P3M4; -.
DR GeneID; 4238800; -.
DR KEGG; ota:OstapCp28; -.
DR eggNOG; ENOG502QPYA; Eukaryota.
DR InParanoid; Q0P3M4; -.
DR OrthoDB; 731145at2759; -.
DR Proteomes; UP000009170; Chloroplast.
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; IPR007066; RNA_pol_Rpb1_3.
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; 5.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 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..1011
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000361019"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 282
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1011 AA; 113458 MW; 2858C2002DFDB9EA CRC64;
MKTFFCNRTV DKGEMKRLIK WVLLNYGTEK TTRLIDKLKT MGFHYATHAG ISLGIDDLSI
PPIKSAFLLN AENDIYENDL RLKRGQITSV QRLEKALDIW NTTNDTLKTE VVKYFRSTDI
FNPVYMMAFS GARGNISQVR QLVGMRGLMA DPQGQILDFP IRRNFREGLT VTEYMISCYG
ARKGLVDTAL RTASSGYLTR RLVDVAQSVI IQQVDCQTTQ GLRIVPELEK IESQLIGRVL
FEDVVDLETG RMVGYKNQDI SPALALKLIK QPALTIRSPL TCRFHAVCQL CYGWNLAQQK
LVQLGEAVGV LAAQSIGEPG TQLTMRTFHT GGVFAGEATE KVYSPHNGIV FYSKQARGRK
IVSKYGEVAF LTFEPLKVKI KNDNTTSVLE FPSFTLLYIP PGQTVGEHQS LAELSRIENK
QNFQQFEVGT ENVQKEFMSN CSGQIFLPQR QNALINEDNA GTTTFNYSEM WLLAGKILDS
KTLVPGDQIK NALYPIRSKI NCEPSRLTTT LPLGYVFPID SNQTSLSKLQ STDAETLKQL
PLLQFSKLSA DNLKFARSYA LELNKTLFHC DSLSKYRFIT SDLEHLPFKS KNLFFNQDTP
TKKVPTFKIK FSRFGKADKF NAKEKFLLLR SVTKLVSTQT NPLKTQFANN LFVQNSINKN
KKTFLEVVKP LKTFQKKTNF FPSPTHENIK SFNPSLQNGN LMSVDADYVR LNVQYGKGFS
SLLNCGEVRA TNCMMTEKDQ IAFKSPVCDL KMKVGDYARV EDQLTTSTRI PLSGQINFIT
AENVLFRSVQ PYLLVPGSNV VVKHGSLVQE NSVLGTLMTS QSTAGDIVQG LPKVDELLEA
REPQHKVLTS MHAKLSTLFS QYGKIYGLRE GCELSFQKIR QFLVQEVQDV YQSQGVYIGD
KHVEIIVRQM TTHVVVVDAG KTGLLPGDIV DIRRIEQLEH TGFFAGVKYR PMLLGITRAA
LMAESFISAA SFQETKRVLS KAALEGQIDW LTGLKENVIL GRLIPAGTGL Y
