ID   RPOC2_CROS5             Reviewed;        1306 AA.
AC   B1WZT6;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
DE            Short=RNAP subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01324};
DE   AltName: Full=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
DE   AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
GN   Name=rpoC2 {ECO:0000255|HAMAP-Rule:MF_01324}; OrderedLocusNames=cce_3487;
OS   Crocosphaera subtropica (strain ATCC 51142 / BH68) (Cyanothece sp. (strain
OS   ATCC 51142)).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Aphanothecaceae; Crocosphaera; Crocosphaera subtropica.
OX   NCBI_TaxID=43989;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51142 / BH68;
RX   PubMed=18812508; DOI=10.1073/pnas.0805418105;
RA   Welsh E.A., Liberton M., Stoeckel J., Loh T., Elvitigala T., Wang C.,
RA   Wollam A., Fulton R.S., Clifton S.W., Jacobs J.M., Aurora R., Ghosh B.K.,
RA   Sherman L.A., Smith R.D., Wilson R.K., Pakrasi H.B.;
RT   "The genome of Cyanothece 51142, a unicellular diazotrophic cyanobacterium
RT   important in the marine nitrogen cycle.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:15094-15099(2008).
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 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. {ECO:0000255|HAMAP-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; CP000806; ACB52835.1; -; Genomic_DNA.
DR   RefSeq; WP_009545345.1; NC_010546.1.
DR   AlphaFoldDB; B1WZT6; -.
DR   STRING; 43989.cce_3487; -.
DR   EnsemblBacteria; ACB52835; ACB52835; cce_3487.
DR   KEGG; cyt:cce_3487; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_1_0_3; -.
DR   OMA; IEGKSDW; -.
DR   OrthoDB; 4373at2; -.
DR   Proteomes; UP000001203; Chromosome circular.
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   DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase;
KW   Reference proteome; Transcription; Transferase; Zinc.
FT   CHAIN           1..1306
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000353521"
FT   REGION          1234..1263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1281..1306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         214
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         285
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         292
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         295
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ   SEQUENCE   1306 AA;  143093 MW;  1AE4F29FED83885A CRC64;
     MTFYNQIVDK GRLKKLISWA YRNYGAARSS QVADNLKDLG FRYATKAGVS ISIDDLTVPP
     TKRGMLDSAE KEINITEARY ARGEITEVER FQKVIDTWNS TSEELKDEVV RNFRQTDPLN
     SVYMMAFSGA RGNMSQVRQL VGMRGLMADP QGQIIDQPIK TNFREGLTVT EYVISSYGAR
     KGLVDTALRT ADSGYLTRRL VDVSQDVIVR EIDCGTRRGL KVTAMKDGDR VKIALGDRLL
     GRVLAEDVMV GDEVIASRNQ SIDAALAAKI GKSVESVMVR SPLTCEAARS VCRCCYGWSL
     ATGRPVDLGE AVGIIAAQSI GEPGTQLTMR TFHTGGVFTG EVAEQIKAPD HGTVKWGKGL
     STRKVRTRHG EDAFQVELAG DLIWTPTGSG KKMTYSVTPG SVLFAADGDT VEKDKMLAEV
     TAAKSTRSTE RATKDVSTDL AGEVFFANLI AEEKTDRQGN TTHIAQRGGL VWVLSGEVYN
     LPPGAEPVVS NGDEVAEGTV LAETKLISVN GGVVRYQPQS REIDIITASV LLDQAEVRKE
     STGGHEQYVI YTADGQRFLL KATPETKVQN HAIIAELIDD RYQTTTGGML RYGGIEVAKG
     SRKTGYEVVQ GGTLLWVPEE THEVNKDISL LVVEDGQYVE AGTEVVKDIF CQCSGAIEVV
     QKNDILREII IKPGEFHLDV DPDEVSYKNE DLIPPGTEVL PGVVTTDLRQ VEWIESTEGL
     GLLLRPVEEY PVSNEPAAPS QGSINEEEVG RHIELRSVQR LFYKDGERVK SVDGIHLLST
     QLVLEIETGS EQAAANLAAD IELKNDEEED CQRLQLVILE SLILRRDLDT DPHGGTITTS
     VLVTDGDQIA PGAVVAKTEI QCREEGEVRG IRRGLEAVRR VLIVRDEDLE IITLKEKPTV
     AKDDLIVAGT EFAPGVVAAE SGLVVAVNQG EEGYEIKLRL ARPYRVSPGA ILHIADGDLV
     QRGDNLVLLV YERAKTGDII QGLPRIEELL EARKPKEACV LSRKPGVCQV EYLEDESVDV
     KVIEDDGTVS EYPILLNQNV IVSDNQRVDV GEHLTDGPAN PHELLEVFFD YYVDKKGVYE
     AALIGLQAAQ KFLVDQVQSV YQSQGIDISD KHIEVIVRQM TAKVRVDDGG DTTMLPGELV
     ELRQIEQVNE AMAITGGAPA RYTPVLLGIT KASLNTDSFI SAASFQETTR VLTEAAIEGK
     SDWLRGLKEN VIIGRLIPAG TGFNAHEEMV MGTLDNGEDS LNNRYGQGER DNNNSDKKPP
     NRLIGATLDE VDENMILDDN IARAYTEADP PWSVESKQEK DDDDDK