RPOC2_PORPU
ID RPOC2_PORPU Reviewed; 1224 AA.
AC P51250;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 87.
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 Porphyra purpurea (Red seaweed) (Ulva purpurea).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Porphyra.
OX NCBI_TaxID=2787;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Avonport;
RA Reith M.E., Munholland J.;
RT "Complete nucleotide sequence of the Porphyra purpurea chloroplast
RT genome.";
RL Plant Mol. Biol. Rep. 13:333-335(1995).
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; U38804; AAC08136.1; -; Genomic_DNA.
DR PIR; S73171; S73171.
DR RefSeq; NP_053860.1; NC_000925.1.
DR AlphaFoldDB; P51250; -.
DR SMR; P51250; -.
DR GeneID; 809879; -.
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; IPR007066; RNA_pol_Rpb1_3.
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; 4.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 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..1224
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000067943"
FT BINDING 223
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 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 307
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1224 AA; 136764 MW; 74CE4603D7BB1661 CRC64;
MNSRKSLSQP SFSNKVIDKN QLKNLIVWAF RNYGIARAAN MADKLKDLGF HYATQAGISL
SLEDLRIPPS KKSLLLSTIE EIKNTENKYR RGEITTVERF QKVIDTWNNA SESLKQEVIE
YFKETDPLNS VYMMAFSGAR GNISQVRQLV GMRGLMADPQ GQIIDLPISS NSREGLTVTD
YFISSYGARK GLVDTALRTA DSGYLTRRLV DVSQDVIIRE VDCKTKKGII LEDLVDTQKV
LINLEQALAG RVLAENVFHP EKGSLIAHTR QDISPNLAQE IVRAGIKKVL VRSPVTCNSR
SSVCQYCYGW NLAHGRLVDL GEAVGIIAAQ SIGEPGTQLA MRTFHTGGVF TGELAEQIYS
PIDGKLTNLD FLSYMEVRTR HGEQALMTEK PTQVIIESSG KQKSIINLSK GTTLLVDNNE
VVSKDQVIAE SPRRNRLMIE RAQKHVLSDL SGKICFSNLT VEETDNNQYT TRITKTGGLI
WVLSGEVYNI PDSANIPVNK ADQVNPGTIL AQTELINQYS GKVRIYQNTS SSITNIQIIT
ESVTVPACYI RTDVINKKES YILETDKKQR FLFKSFPDQK ISDGHIVAEL ISDTYKTTSG
GIIKYLDLNV SKKKTGPEKD AYDILSPGYI LWISEETHEI NKDSSLLLVN NGDVIESGTE
LVKNIFSKSS GIIEIIQKDG IVREIIIKPG FIYKLTDFYS IHDKSRGFLR PGETLHGNIS
TDKLVYWEYI ENEQTPYILI RPVIVYSIPE IKSSLIENLT SQKVNQTKLK LVKRTVFRDG
ERVKSIDGVH LVTTNLVAEI NHHDPNLVSA IEFLAKEDSS NCFALGLSTF ETLSIKSIDN
KVEKEQSQTR IIVSDGEYIQ PLTVVASTEI ISMSKGFVEE IHVEKNTSRR ILLTTSIDNK
VFDLHQQNTL VQVGDWIRCG DLISESIISL DSGQITHISQ ESATLRIARP YLVSNAAILH
VDNNALIRKG ETLAVLVFDR AKTGDIIQGL PRIEEILEAR KKTDVLLNPH DILDASFNLY
IECGLALYEA ARLSFQEIQL LLVKEVQLVY QSQGVNISDK HIEVIVRQMT SKVKIENGEE
TGYLPGELVE LQKIEQTNKS MTSRNKLNAS YRPILLGITQ ASLNTESFIS AASFQETTKV
LTEAAISGKL DWLRGLKENV IIGRLIPAGT GFNMYDSHND VANKKDINKN ISTDNSPPSV
RDDLDDIILD DRTARNYFNN KTVD
