RPOC2_SPIOL
ID RPOC2_SPIOL Reviewed; 1361 AA.
AC P11704;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 103.
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 Spinacia oleracea (Spinach).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3045324; DOI=10.1016/0022-2836(88)90477-9;
RA Hudson G.S., Holton T.A., Whitfeld P.R., Bottomley W.;
RT "Spinach chloroplast rpoBC genes encode three subunits of the chloroplast
RT RNA polymerase.";
RL J. Mol. Biol. 200:639-654(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Geant d'hiver, and cv. Monatol;
RX PubMed=11292076; DOI=10.1023/a:1006478403810;
RA Schmitz-Linneweber C., Maier R.M., Alcaraz J.-P., Cottet A., Herrmann R.G.,
RA Mache R.;
RT "The plastid chromosome of spinach (Spinacia oleracea): complete nucleotide
RT sequence and gene organization.";
RL Plant Mol. Biol. 45:307-315(2001).
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; AJ400848; CAB88715.1; -; Genomic_DNA.
DR PIR; A29959; A29959.
DR RefSeq; NP_054922.2; NC_002202.1.
DR AlphaFoldDB; P11704; -.
DR STRING; 3562.P11704; -.
DR GeneID; 2715634; -.
DR KEGG; soe:2715634; -.
DR OrthoDB; 731145at2759; -.
DR Proteomes; UP000054095; 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; 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..1361
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000067951"
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 1361 AA; 154769 MW; 19FF8C42BB1B17E8 CRC64;
MEVLMAERAN LVFHNKAIDG TAMKRLISRL IDHFGMAYTS HILDQLKTLG FQQATATSIS
LGIDDLLTIP SKGWLVQDAE QQSLILEKHH HYGNVHAVEK LRQSIEIWYS TSEYLRQEMN
PNFRMTDPYN PVHIMSFSGA RGNVSQVHQL VGMRGLMSDP QGQMIDLPIQ SNLREGLSLT
EYIISCYGAR KGVVDTAVRT SDAGYLTRRL VEVVQHIVVR RRDCGTIRGI SVSPQNSTMP
ERILIQTLIG RVLADDIYMG SRCIATRNQD IGVGLVNRFI TLRTQLISIR TPFTCRSASW
ICRLCYGRSP THGGLVELGE AVGIIAGQSI GEPGTQLTLR TFHTGGVFTG GTAEHVRAPS
NGKIQFNEDL VHPTRTRHGH PAFLCYIDLY VTIESDDILH NVNIPPKSFL LVQNDQYVES
EQVIAEIRAG TSTLNFKERV RKHIYSDSEG EMHWSTDVYH APEFTYGNVH LLPKTSHLWV
LSGKPYRSSV VPFSLSKDQD QMNTHSLSFE QIYISNPSVT NDQVKDKLSD SFSKKEDRIT
DYSELNRIGH CNLIYPAKNL DLLAKKRRNR FIIPFQGSQE RKKELMSLSG ISIEIPINGI
FRKNSIFAYF DDPRYRRKSS GITKYGTIEM HSIVKKEDLI EYRGVKEFRP KYQMKVDRFF
FIPEEVHILA GSSSIMVRNN SIIGVDTWIT LNTRSRIGGV VRVERKKKKI ELTIFSGDIH
FPGETDKISR HSGILIPPSR KNSKDSKNLK KWIYVQRITP TKKKYFVLVR PVVPYEITDG
INLATLFPQD LLQERDNVQL RVVNYILYGN GKVTRGISDT SIQLVRTCLV LNWNQDKKGS
SIEEARGSFV EVRTNGMIQD FLKVNLVKPA ISYISKRNDP SSEKKEGSDH TNMNPFYSIY
IYPKTKLQKS FNQNQGTVRT LLGINKECQF FLILSSSNCF RIGPFKGVKY PKELIKKDPL
IPIRNSFGPL GTALQIANFF SFYYLITHNQ ILVTNYLQLD NLKQTFQPFK FQYYLMDENG
RIYNPDPCSN IIFNPFKLNW YFLHYHFCEE TSTKIDLGQF VCENVCITKK GTHLKSGQVL
IVQFDSVVIR SAKPYLATPG ATLHGHYGEI IYEGDTLVTF IYEKSRSGDI TQGLPKVEQV
LEVRSIDSIS INLEKRIDSW NERITRILGS PWGFLIGAEL TIAQSRISLV NKIQKVYRSQ
GVQIHNRHIE IIVRQITSKV LVSEDGMSNV FLPGELIGLF RAERTGRALE EAICYRATLL
GITRASLNTQ SFISEASFQE TARVLAKAAL RGRIDWLKGL KENVVLGGMI PVGTGFKGFV
HHSSQHKDIP LKTKKQNLFE GEMGDILFYH RELFESCLSK N