RPOC2_PELHO
ID RPOC2_PELHO Reviewed; 1376 AA.
AC Q06FX1;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 53.
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 Pelargonium hortorum (Common geranium) (Pelargonium inquinans x Pelargonium
OS zonale).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Geraniales; Geraniaceae; Pelargonium.
OX NCBI_TaxID=4031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Ringo White;
RX PubMed=16916942; DOI=10.1093/molbev/msl089;
RA Chumley T.W., Palmer J.D., Mower J.P., Fourcade H.M., Calie P.J.,
RA Boore J.L., Jansen R.K.;
RT "The complete chloroplast genome sequence of Pelargonium x hortorum:
RT organization and evolution of the largest and most highly rearranged
RT chloroplast genome of land plants.";
RL Mol. Biol. Evol. 23:2175-2190(2006).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ897681; ABI17251.1; -; Genomic_DNA.
DR RefSeq; YP_784060.1; NC_008454.1.
DR AlphaFoldDB; Q06FX1; -.
DR SMR; Q06FX1; -.
DR GeneID; 4362770; -.
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; Transcription; Transferase; Zinc.
FT CHAIN 1..1376
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000277196"
FT REGION 895..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..919
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 297
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1376 AA; 155245 MW; B75560F5B32F51D0 CRC64;
MKEWPPNLAF HNKVIDGAAI KQLISRLIQR FGMLYTSHVL DQVKLLGFKQ ATASSISLGI
DDLLTIPSKR WLVQDAQQQS FLLEKYYQYG NVHAVEKLRQ SIEIWDAISA YLRQEMTPNF
GMTDPLNPVH IMSFSGARGN ASQVNQLIGM RGLMSDPLGQ MIDLPIQSNL REGLSLTEYI
ISSYGARKGV VDTAIRTADA GYLTRRLVDV VQHIIVRGTD CGTTRGLSLS PQNGGVPEST
QTLIGRVLAK DIYIGPRCIA VRNQDLGGGL VNRLITFKKK PIYVRTPFTC RSTSWICRFC
YGRSPTSACG DLVELGEAVG IIAGQSIGEP GTQLTLRTFH TGGVFTGGTA EQVRAPFNGK
IKFNEDLVHP TRTRHGQPAF LCYIDLYLTI ESEDIIHSVP IPPKSFLLVQ NDQYVESEQV
IAEISAGTST FAFKDRVRKH IYSDSSGEMH SNTGMYHARK FPFSNVHILP KTSHLWILLG
DLCGSGPVLF SMYKDQDQMS IHSLSVQGRN TPSLSVNNDQ LKHRRLSLYD KNGTGGGSIP
ILNYSEMTRS LSTARCNLLY PAILHENFSL LAKKRRTRFL IPFQSIQEHR RKNERILCSD
ISIKIPRNGL FRGNSILAYF DDPRYKIGVS GITKYGTIEV DSIVTKESFI NYGGVQPKDE
GKVDPLFFIP EEVHIFPETS SIMVRNNSII GINTKITLNK RSRVGGLVRV KKIHRGIKLQ
IFSGDISFPR KRDKRFIPQN KDILIPPQIR KRNFNKSKKA KNWIYVQKMR PTNKNSFFLL
QPVVTYEIAD GINLARLFPP DLLQEIDNIQ LRVGNYIRYG DGELIPGISG KNPRIQLVRT
FLVLNWDQDK KDSSIEEAHA SFVEVSTKGM VRDFLRIHLR KSQIAYAYMR KRNDPSGSGF
PSDNELDHSN RNPFSSSYPK ARVRQSLNGT IRTLLNRNKE CQSLLILSSS NCFRLGPFNN
VKYHNPKKES IKRDTDPLIP IRNFSGPLGT VPQIANFDVF YHLITKNRIS VFHYLPPEKG
KLQVIQSFLM DENGRIYKSD PYSNIFLNPF NFNWYFLQHN YHKNYPNYCE ETSTIINLGQ
FLFETVCIAK NGPRLKSGQV FILQVGYVII RSGKPYLAIP GATVHGHSGQ IVYGGDTLVT
FIYEKARSAD ITQGLPKVDA MFEVRSKNSI SMRLKARDEY WNEYITRNLG IYWGLLIGAK
LTIAQSSLSL VNEIQKVYRS QGVQIDNRHI ELIVRQITSK VLISEDGMSN LFLPGELIGL
LQAERTGRAL EKGICYRAIL VGITKASLNT QSFISEASFQ QTARVLAKAA LRGRIDWLKG
LKENVVLGGM SPAGTGFRGL VHPSSKKYKT LSLETQRKIL FDGKVRDLLF HHKRIV
