RPOC1_PHAVU
ID RPOC1_PHAVU Reviewed; 684 AA.
AC A4GGA6; A8W811;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 57.
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 Phaseolus vulgaris (Kidney bean) (French bean).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Negro Jamapa;
RX PubMed=17623083; DOI=10.1186/1471-2164-8-228;
RA Guo X., Castillo-Ramirez S., Gonzalez V., Bustos P.,
RA Fernandez-Vazquez J.L., Santamaria R.I., Arellano J., Cevallos M.A.,
RA Davila G.;
RT "Rapid evolutionary change of common bean (Phaseolus vulgaris L) plastome,
RT and the genomic diversification of legume chloroplasts.";
RL BMC Genomics 8:228-228(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Moore M.J., Triplett E.W., Broughton W.J., Soltis P.S., Soltis D.E.;
RT "Complete nucleotide sequence of the plastid genome of the common bean,
RT Phaseolus vulgaris.";
RL Submitted (OCT-2007) 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_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; DQ886273; ABH88087.1; -; Genomic_DNA.
DR EMBL; EU196765; ABW22781.1; -; Genomic_DNA.
DR RefSeq; YP_001122807.1; NC_009259.1.
DR AlphaFoldDB; A4GGA6; -.
DR SMR; A4GGA6; -.
DR STRING; 3885.XP_007135456.1; -.
DR PRIDE; A4GGA6; -.
DR GeneID; 4961811; -.
DR KEGG; pvu:PhvuCp23; -.
DR eggNOG; ENOG502QPYA; Eukaryota.
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 3: Inferred from homology;
KW Chloroplast; DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Plastid; Transcription; Transferase; Zinc.
FT CHAIN 1..684
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353510"
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 491
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 493
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 495
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT CONFLICT 145
FT /note="V -> F (in Ref. 2; ABW22781)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 684 AA; 79179 MW; B61342C38B4B68EC CRC64;
MIDQYKHQQL RIGSVSPQQM SAWAKRILPN GEIVGEVTKP YTFHYKTNKP EKDGLFCERI
FGPIKSGICA CGNYRVIRDK KDDPKFCEQC GVEFIDSRIR RYQMGYIKLA CLVTHAWYLK
RLPSYIANLL DKPLKELESL VYGDVSFARP VVKKPTFLRL RGSFEYEIQS WKHSIPLFFT
TRGFDIFRNR EISSGAVAIR EQLADLDLRI IMDYSLIEWK ELGKEGSPDN ENEWEDRKVG
RRKNFLVRRI ELAKHFIRTN IEPEWMVLCL LPVLPPELRP IIQVDGGKLM SSDINELYRR
VIYRNNTLID LLTTSRSTPG ELVICQEKLV QEAVDTLLDN GIRGQPMRDG HNKVYKSFSD
IIEGKEGRFR ETLLGKRVDY SGRSVIIVGP SLSLHRCGLP GEIAIELFQT FLIRGLIRKH
FASNIGIAKS KIRQKEPIVW EILQEVMQGH PVLLNRAPTL HRLGIQAFQP ILVEGRAICL
HPLVCKGFNA DFDGDQMAVH VPLSLEAQAE ARLLMFSHTN LLSPAIADPI SVPTQDMLIG
LYILTSGNRR GIYSNRYNPR NCRNLKNERI PNNNYKYTKK KEPFFCNSYD AIGAYQQKRI
TFDSPLWLRW RLDLRIISSR EVPIEVHYES LGTYHEIYGH YLVVRSIKKQ MRSIYIRTNV
GHISFYREIE EAVQGFCRAY SYDI