RPOC2_CAPBU
ID RPOC2_CAPBU Reviewed; 1379 AA.
AC A4QKI2;
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 Capsella bursa-pastoris (Shepherd's purse) (Thlaspi bursa-pastoris).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=3719;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hosouchi T., Tsuruoka H., Kotani H.;
RT "Sequencing analysis of Capsella bursa-pastoris JO22 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; AP009371; BAF50187.1; -; Genomic_DNA.
DR RefSeq; YP_001123363.1; NC_009270.1.
DR AlphaFoldDB; A4QKI2; -.
DR PRIDE; A4QKI2; -.
DR GeneID; 4961728; -.
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..1379
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000353549"
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 1379 AA; 156925 MW; 754BBF55B3DA93DA CRC64;
MAERANLVFH NKVIDGTAIK RLISRLIDHF GMAYTSHILD QVKTLGFQQA TATSISLGID
DLLTIPSKGW LVQDAEQQSW ILEKHHHYGN VHAVEKLRQS IEIWYATSEY LRQEMNPNFR
MTDPFNPVHM MSFSGARGNA SQVHQLVGMR GLMSDPQGQM IDLPIQSNLR EGLSLTEYII
SCYGARKGVV DTAVRTSDAG YLTRRLVEVV QHIVVRRTDC GTIRGISVSP RNKNRMMSER
IFIQTLIGRV LADDIYIGSR CVAFRNQDLG IGLVNRLITF GTQSISIRTP FTCRSTSWIC
RLCYGRSPTH GDLVELGEAV GIIAGQSIGE PGTQLTLRTF HTGGVFTGGT AEHVRAPYNG
KIKFNEDLVH PTRTRHGHPA FLCYIDLSVI IESEDIIHSV TIPPKSFLLV QNDQYVESEQ
VIAEIREGTY TFHFKERVRK YIYSDSEGEM HWSTDVSHAP EFTYSNVHLL PKTSHLWILS
GGSCGSSLIL FSIHKDQDQM NIPFLSAERK SISSLSVNND QTSQKFFSSD FADKKKLGIS
YYSELNGNLG TSHYNFIYSA IFQENSDLLA KRRRNRFLIP FQSIQEQEKE FIPHSGISVE
IPINGIFRRN SIFAFFDDPR YRRKSSGILK YGALKADSII QKEDMIEYRG VQKFKTKYEM
KVDRFFFIPE EVHILPESSA IMVQNYSIIG VDTRLTLNIR SQVGGLIRVE RKKKRVELKI
FSGDIHFPDK TDKISRHSGI LIPPGRGKTN SKESKKFKNW IYVQRITPTK KKFFVLVRPV
ATYEIADSIN LATLFPQDLF REKDNIQLRV FNYILYGNGK PTRGIADTSI QLVRTCLVLN
WDQDNKNSAL EAVRAFFVEV STKGLIRDFI RIGLVKSHIS YIRKRKNSPD SGFISADHMN
PFYPISPKAG ILQQSLRQNR GTIRMFLNRN KESQSLLILS SSNCFRMGPF NHVKYHNVIN
QSIKKNTLIT IKNSSGPLGT ATQISNFYSF LPLLTYNQIS LIKYLQLDNF KYIFQVINSY
LIDENGRIFN LDPYSNVVLN PFKLNWYFLH QNYHHNYCEE TSTIISLGQF FCENVCIAKK
EPHLKSGQVL IVQRDSVVIR SAKPYLATPG AKVHGHYREI LYEGDTLVTF IYEKSRSGDI
TQGLPKVEQV LEVRSIDSIS LNLEKRIKGW NKCITRILGI PWGFLIGAEL TIVQSRISLV
NKIQKVYRSQ GVQIHNRHIE IIVRQITSKV LVSEEGMSNV FLPGELIGLL RAERTGRALE
EAICYRAVLL GITRASLNTQ SFISEASFQE TARVLAKAAL RGRIDWLKGL KENVVLGGVI
PAGTGFNKGL VHCSRQHTNI LLEKKTKNLA LFEGDMRDIL FYHREFCESS ISKSDFSRI
