RPOC2_LOBMA
ID RPOC2_LOBMA Reviewed; 1371 AA.
AC A4QLI4;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 47.
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 Lobularia maritima (Sweet alyssum) (Alyssum maritimum).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Anastaticeae; Lobularia.
OX NCBI_TaxID=226051;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hosouchi T., Tsuruoka H., Kotani H.;
RT "Sequencing analysis of Lobularia maritima chloroplast DNA.";
RL Submitted (MAR-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_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; AP009375; BAF50539.1; -; Genomic_DNA.
DR RefSeq; YP_001123715.1; NC_009274.1.
DR AlphaFoldDB; A4QLI4; -.
DR SMR; A4QLI4; -.
DR GeneID; 4964876; -.
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..1371
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000353568"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 293
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"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1371 AA; 156263 MW; 37D4FB7F8B45635F CRC64;
MAERANLVFH NKVIDGTAIK RLISRLIDHF GMAYTSHILD QVKTLGFQQA TATSISLGID
DLLTIPSKGW LVQDAEQQSL ILEKHHHYGN VHAVEKLRQS IEIWYATSEY LRQEMNLNFR
MTDPFNPVHM MSFSGARGNA SQVHQLVGMR GLMSDPQGQM IDLPIQSNLR EGLSLTEYII
SCYGARKGVV DTAVRTSDAG YLTRRLVEVV QHIVVRRTDC GTIRGISVSP RNKNRMMSER
IFIQTLIGRV LADDIYIGSR CVAFRNQDLG IGLVNRFITF GTQSISIRTP FTCRSTSWIC
RLCYGRSPTH GDLVELGEAV GIIAGQSIGE PGTQLTLRTF HTGGVFTGGT AEHVRAPYNG
KIKFNEDLVH PTRTRHGHPA FLCYIDLSVI IESEDIIHSV TIPPKSFLLV QNDQYVESEQ
VIAEIREGTY TFHFKERVRK YIYSDSEGEM HWSTDVSHAP EFTYSNVHLL PKTSHLWILS
GSSCESSLIR FSIHKDQDQM NIPFFFVKSK AISSLSVNND QVSQKFFSSD FSDKKKSGIP
NYSELNEIVG TSHYNFIYSA IFHENSDLLA KRRRNRFLIP FQSIQEQEKE FIPHSGISIE
IPINGIFRRN SIFAFFDDPR YRRKSCGILK YGTLKADSII QKEDMIEYRG VQKFKTKYEM
KVDRFFFIPE EVHILPESSA IMVQNYSIIG VDTRITLNIR SQVGGLIRVE RKKKRIELKI
FSGDIHFPDK TDKISRHSGI LIPPGRGKTN SKEFKKLKNW IYVQRITPTK KKFFVLVRPV
ATYEIADSIN LATLFPQDLF REKDNIQLRV FNYILYGNGK PTRGISDTSI QLVRTCLVLN
WDQDNKNSSL EEVRSFFVEV STKGLIRDFI RIGLVKSHIS YIRKRQNPAD SGLISADHMN
PFYSISPKAG ILQQSLRQNH GTIRMFLNRN KESQSLLILS SSNCFRIGPF NHVKYHNVIN
QSIKKNPIIT IKNSSGPLGT AIQISNFYSF LPLLTYNQIS VIKYLQLDNL KYIFQVINSY
LIDENGRILN PDPYSNVVLN PFKLNWYFLH QNYHHNYCEE TSTIISLGQF FCENVCIAKK
EPHLKSGQVL IVERDSVVIR SAKPYLATPG AKVHGHYREI LYEGDTLVTF IYEKSRSGDI
TQGLPKVEQV LEVRSIDSIS LNLEKRIKGW NKCITRILGI PWGFLIGAEL TIVQSRISLV
NKIQKVYRSQ GVQIHNRHIE IIVRQITSKV LVSEEGMSNV FLPGELIGLL QAERTGRALE
EAICYRAILL GITRASLNTQ SFISEASFQE TARVLAKAAL RGRIDWLKGL KENVVLGGVI
PAGTGFNKGL VHCSRQHTNI LLEKKTKNFS LFEGNMRDIL FYHREFFDSS I
