RPOC1_SINAL
ID RPOC1_SINAL Reviewed; 688 AA.
AC P46819; Q9THV6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01323};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01323};
DE AltName: Full=PEP {ECO:0000255|HAMAP-Rule:MF_01323};
DE AltName: Full=Plastid-encoded RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01323};
DE Short=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01323};
GN Name=rpoC1 {ECO:0000255|HAMAP-Rule:MF_01323};
OS Sinapis alba (White mustard) (Brassica hirta).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Sinapis.
OX NCBI_TaxID=3728;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=cv. Albatros; TISSUE=Cotyledon;
RX PubMed=10601874; DOI=10.1046/j.1432-1327.2000.00991.x;
RA Pfannschmidt T., Ogrzewalla K., Baginsky S., Sickmann A., Meyer H.E.,
RA Link G.;
RT "The multisubunit chloroplast RNA polymerase A from mustard (Sinapis alba
RT L.). Integration of a prokaryotic core into a larger complex with
RT organelle-specific functions.";
RL Eur. J. Biochem. 267:253-261(2000).
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_01323}.
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_01323};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01323};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01323};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01323};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01323};
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_01323}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC Rule:MF_01323}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01323}.
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DR EMBL; AJ243754; CAB48413.1; -; Genomic_DNA.
DR EMBL; X82417; CAA57815.1; -; Genomic_DNA.
DR PIR; S48843; S48843.
DR AlphaFoldDB; P46819; -.
DR SMR; P46819; -.
DR PRIDE; P46819; -.
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:0000287; F:magnesium ion binding; 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; 1.10.274.100; -; 1.
DR Gene3D; 4.10.860.120; -; 1.
DR HAMAP; MF_01323; RNApol_bact_RpoC1; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR034678; RNApol_RpoC1.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 2.
DR SMART; SM00663; RPOLA_N; 1.
PE 1: Evidence at protein level;
KW Chloroplast; DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Plastid; Transcription; Transferase; Zinc.
FT CHAIN 1..688
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067897"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 497
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 499
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 501
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
SQ SEQUENCE 688 AA; 79495 MW; 84AC511809872D16 CRC64;
MIDRYKHQQL RIGLVSPQQI SAWATKKIPN GEIVGEVTKP YTFHYKTNKP EKDGLFCERI
FGPIKSGICA CGNYRVIGDE KGDPKFCEQC GVEFVDSRIR RYQMGYIKLT CPVTHVWYLK
RLPSYIANLL DKPLKELEGL VYCDVCFDRN PNFSFARPIT KKPTFLRLRG SFEYEIQSWK
YSIPLFFTTQ GFEIFRNREI STGAGAIREQ LADLDLRIII ENSLVEWKQL GEEGPTGNEW
EDRKIVRRKD FLVRRMELAK HFIRTNIEPE WMVLCLLPVL PPELRPIIQI EGGKLMSSDI
NELYRRVIYR NNTLTDLLTT SRSTPGELVM CQEKLVQEAV DTLLDNGIRG QPMRDGHNKV
YKSFSDVIEG KEGRFRETLL GKRVDYSGRS VIVVGPSLSL HRCGLPREIA IELFQTFVIR
GLIRQHLASN IGVAKSQIRE KKPIVWEILQ EVMQGHPVLL NRAPTLHRLG IQSFQPILVE
GRTICLHPLV CKGFNADFDG DQMAVHVPLS LEAQAEARLL MFSHMNLLSP AIGDPISVPT
QDMLIGLYVL TSGTRRGICA NRYNPCNRKN YQNERIYETN YKYMKEPFFC NSYDAIGAYR
QKRINLDSPL WLRWQLDQRV IASKEVPIEV HYESFGNYHE IYAHYLIVRS VKKETLYIYI
RTTVGHISLY REIEEAIQGF SQACSYDT
