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Entry: K4EP11_DATST
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Original site: K4EP11_DATST 
ID   K4EP11_DATST            Unreviewed;      1388 AA.
AC   K4EP11;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324};
DE            EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_01324};
DE   AltName: Full=PEP {ECO:0000256|HAMAP-Rule:MF_01324};
DE   AltName: Full=Plastid-encoded RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324};
DE            Short=RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324};
GN   Name=rpoC2 {ECO:0000256|HAMAP-Rule:MF_01324,
GN   ECO:0000313|EMBL:AEQ36928.1};
GN   ORFNames=Dast_Cp012 {ECO:0000313|EMBL:AEQ36928.1};
OS   Datura stramonium (Jimsonweed) (Common thornapple).
OG   Plastid; Chloroplast {ECO:0000313|EMBL:AEQ36928.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Datureae; Datura.
OX   NCBI_TaxID=4076 {ECO:0000313|EMBL:AEQ36928.1};
RN   [1] {ECO:0000313|EMBL:AEQ36928.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NN003 {ECO:0000313|EMBL:AEQ36928.1};
RA   Li X.W., Li Q., Lin X.H., Hu Z.G., Chen S.L.;
RT   "High-throughput multiplex sequencing reveals the feasibility of
RT   chloroplast genomes as a plant super-barcode.";
RL   Submitted (SEP-2011) 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:0000256|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:0000256|HAMAP-Rule:MF_01324};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01324};
CC       Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01324}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
CC       Rule:MF_01324}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01324}.
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DR   EMBL; JN662489; AEQ36928.1; -; Genomic_DNA.
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 {ECO:0000313|EMBL:AEQ36928.1};
KW   DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW   ECO:0000256|HAMAP-Rule:MF_01324};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01324};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_01324}; Plastid {ECO:0000313|EMBL:AEQ36928.1};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_01324};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01324};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01324}.
FT   DOMAIN          93..157
FT                   /note="RNA polymerase Rpb1"
FT                   /evidence="ECO:0000259|Pfam:PF05000"
FT   DOMAIN          172..365
FT                   /note="RNA polymerase Rpb1"
FT                   /evidence="ECO:0000259|Pfam:PF04998"
FT   DOMAIN          1192..1278
FT                   /note="RNA polymerase Rpb1"
FT                   /evidence="ECO:0000259|Pfam:PF04998"
FT   BINDING         220
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT   BINDING         291
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT   BINDING         298
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT   BINDING         301
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
SQ   SEQUENCE   1388 AA;  156976 MW;  D0C849617DD8487B CRC64;
     MAERANLVFH NKAIDGTAMK RLISRLIEHF GMAYTSHILD QVKTLGFQQA TATSISLGID
     DLLTIPSKGW LVQDAEQQSL ILEKHHHYGN VHAVEKLRQS IEIWYATSEY LRQEMNPNFR
     MTDPFNPVHI MSFSGARGNA SQVHQLVGMR GLMSDPQGQM IDLPIQSNLR EGLSLTEYII
     SCYGARKGVV DTAVRTSDAG YLTRRLVEVV QHIVVRRTDC GTARGISVSP RNGMMPERIF
     SQTLIGRVLA DDIYMGPRCI ATRNQDIGIG LVNRFITLRA QPISIRTPFT CRSTSWICRL
     CYGRSPTHGD LVELGEAVGI IAGQSIGEPG TQLTLRTFHT GGVFTGGTAE HVRAPSNGKI
     KFNEDLVHPT RTRHGHPAFL CSIDLYVTIE SEDILHNVNI PPKSLLLVQN DQYVESEQVI
     AEIRAGISTL NFKEKVRKHI YSDSDGEMHW STDVYHAPEF TYGNVHLLPK TSHLWILLGG
     PCRSSIVYLS IHKDQDQMNS HSLSGKRRYT SNLSVTNDQA RQKLFSSDFY GKKEDRIPDY
     SDLNRIICTG QYNLVYSPIL HENSDLLSKR RRNKFIIPLH SIQELENELM PCSGISIQIP
     VNGIFRRNSI LAYFDDPRYR RKSSGIIKYG TIETHSVIKK EDLIEYRGVK EFRLKYQMKV
     DRFFFIPEEV HILPGSSSIM VRNNSIVGVD TQITLNLRSR VGGLVRVEKK KKRIELKIFS
     GDIHFPGETD KISRHTGVLI PPGRGKINSK ESKKVKNWIY VQRITPSKKK FFVLVRPVVT
     YEITDGINLA TLFPPDPLQE RDNVQLRIVN YILYGNGKPI RGISDTSIQL VRTCLVLNWN
     QDKKSSSCEE ARASFVEIRT NGLIRHFLRI NLVKSPISYI GKRNDPSGSG LLSDNGSDCT
     NLNPFSSIYY YSKEKIQQSL NQPQGTIHTL LNRNKECQSL IILSAANCSR MGPFKDVKYH
     SVIKESIKKD PLIPIRNSLG PLGTCLPIEN FYSSYHLITH NQILVTNYLQ LDNLKQTFQV
     IKFKYYLMDE NGKIFHPDPC RNIILNPFNL NWYFLHHNYC EETSKIISLG QFICENVCIA
     KNGSPLKSGQ VILVQVDSIV IRSAKPYLAT PGATVHGHYG ETLYEGDTLV TFIYEKSRSG
     DITQGLPKVE QVLEVRSIDS ISMNLEKRVE GWNKCITRIL GIPWGFLIGA ELTIAQSRIS
     LVNKIQQVYR SQGVQIHNRH IEIIVRQITS KVLVSEDGMS NVFSPGELIG LLRAERMGRA
     LEEAICYQVV LLGITRASLN TQSFISEASF QETARVLAKA ALRGRIDWLK GLKENVVLGG
     VIPVGTGFKG LVYPSKQHNN IPLETKKKNL FEGEMRDILF HHRKLFDSCL SKKFHDIPEQ
     SFIGFNDS
//
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