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Database: UniProt
Entry: RPOC2_PELHO
LinkDB: RPOC2_PELHO
Original site: 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   27-MAR-2024, entry version 58.
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}.
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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:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR   CDD; cd02655; RNAP_beta'_C; 1.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.150.390; -; 1.
DR   Gene3D; 1.10.1790.20; -; 1.
DR   Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1.
DR   HAMAP; MF_01324; RNApol_bact_RpoC2; 1.
DR   InterPro; IPR012756; DNA-dir_RpoC2_beta_pp.
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   NCBIfam; TIGR02388; rpoC2_cyan; 1.
DR   PANTHER; PTHR48355; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 1.
DR   PANTHER; PTHR48355:SF1; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 1.
DR   Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR   Pfam; PF04998; RNA_pol_Rpb1_5; 2.
DR   SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 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
//
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