ID   RPOC2_NOSCO             Reviewed;         717 AA.
AC   P14564;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta';
DE            Short=RNAP subunit beta';
DE            EC=2.7.7.6;
DE   AltName: Full=RNA polymerase subunit beta';
DE   AltName: Full=Transcriptase subunit beta';
DE   Flags: Fragment;
GN   Name=rpoC2;
OS   Nostoc commune.
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=1178;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=UTEX 584 / SAG 1453-5;
RX   PubMed=2495268; DOI=10.1128/jb.171.4.1967-1973.1989;
RA   Xie W.-Q., Jaeger K., Potts M.;
RT   "Cyanobacterial RNA polymerase genes rpoC1 and rpoC2 correspond to rpoC of
RT   Escherichia coli.";
RL   J. Bacteriol. 171:1967-1973(1989).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
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:0000250|UniProtKB:P0A8T7};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P0A8T7};
CC       Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000250|UniProtKB:P0A8T7};
CC   -!- SUBUNIT: In cyanobacteria the RNAP catalytic core is composed of 2
CC       alpha, 1 beta, 1 beta', 1 gamma and 1 omega subunit. When a sigma
CC       factor is associated with the core the holoenzyme is formed, which can
CC       initiate transcription (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; M29747; AAA25518.1; -; Genomic_DNA.
DR   PIR; B32838; B32838.
DR   AlphaFoldDB; P14564; -.
DR   SMR; P14564; -.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.274.100; -; 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; 1.
DR   Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR   Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR   Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR   TIGRFAMs; TIGR02388; rpoC2_cyan; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase;
KW   Transcription; Transferase; Zinc.
FT   CHAIN           1..>717
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000067904"
FT   BINDING         218
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT   BINDING         291
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT   BINDING         298
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT   BINDING         301
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT   NON_TER         717
SQ   SEQUENCE   717 AA;  78244 MW;  E5505A9FA37D3C91 CRC64;
     MTNEKMIFRN RVVDKGQLRN LISWAFTYYG TARTAVMADK LKDLGFRYAT KAGVSISVDD
     LMVPPTKRLL LEAAEEEIRA TETRYQRGEI TEVERFQKVI DTWNGTSEAL KDEVVVHFKK
     TNPLSSVYMM AFSGARGNIS QVRQLVGMRG LMADPQGEII DLPIKTNFRE GLTVTEYIIS
     SYGARKGLVV QPSRTADSGY LTRRLVDVSQ VYYSGFDCGT PELSIRPMTE GAKTLIPLAT
     RLMGRVIGED VLHPVTKEVI AARNSPISED LAKKIEKSGV GEVVVRSPLT CEAARSVCQH
     CYGWSLAHAS MVDLGEAVGI IAAQSIGEPG TQLTMRTFHT GGVFTGEVAQ QVRSKIDGTV
     KLPRKLKTRT YRTRHGEDAL YVEANGIMLL EPTKVGDVTP ENQEVHLTQG STLYVFDGNK
     VNKVQLLAEV ALGGRTTRTN TEKAVKDVAS DLAGEVQFAE VVPEQKTDRQ GNTTTTRRTR
     GLIWILSGEV YNLPPGAELV VKNGDAIASN GVLAETKLAS LHGGVVRLPE ATPGKSTREI
     EIITASVVLD QATVTVQSSQ GRNNYLVSTG NNQVFNLRAT PGTKVQNGQV VAELIDDRYR
     TTTGGFLKFA GVEVQKKGKA KLGYEVVQGG TCCGSPEESH EVNKDISLLL VEDGQFVEAG
     TEVVKDIFCQ NSGVVEVTQK NDILREVVVK PGELLIVDDP ESVIGRDNTF IQPGEEF