ID   RPOC2_SYNS3             Reviewed;        1365 AA.
AC   Q0I7L9;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=sync_2356;
OS   Synechococcus sp. (strain CC9311).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=64471;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9311;
RX   PubMed=16938853; DOI=10.1073/pnas.0602963103;
RA   Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H.,
RA   Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S.,
RA   Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R.,
RA   Paulsen I.T.;
RT   "Genome sequence of Synechococcus CC9311: insights into adaptation to a
RT   coastal environment.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006).
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; CP000435; ABI46015.1; -; Genomic_DNA.
DR   RefSeq; WP_011620263.1; NC_008319.1.
DR   AlphaFoldDB; Q0I7L9; -.
DR   SMR; Q0I7L9; -.
DR   STRING; 64471.sync_2356; -.
DR   EnsemblBacteria; ABI46015; ABI46015; sync_2356.
DR   KEGG; syg:sync_2356; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_1_0_3; -.
DR   OMA; IEGKSDW; -.
DR   OrthoDB; 4373at2; -.
DR   Proteomes; UP000001961; Chromosome.
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; 1.
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..1365
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000353534"
FT   BINDING         249
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         316
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         323
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         326
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ   SEQUENCE   1365 AA;  148213 MW;  031F0E2942B53AB9 CRC64;
     MTSTPSKSRK SAKAAKAAKA EAAAFAKSRA LSKTPPPFRN RVVDKKVLKE LVAWAFKNHG
     TAATASMADQ LKDLGFKYAT QAAVSISVND LKVPAAKKDL LDQAEELITE TEESYRLGVI
     TEVERHTKVI DTWTETNERL VDAVKKNFND NDPLNSVWMM ANSGARGNMS QVRQLVGMRG
     LMANPQGEII DLPIRTNFRE GLTVTEYVIS SYGARKGLVD TALRTADSGY LTRRLVDVAQ
     DVIVREDDCG TMRSIMVKAE DGRFGNRLVG RLTADQVLGA DGEVIAERNS EIDPPLSKRF
     EAAGVSALMV RSPLTCEANR SVCRKCYGWA LAHNQLVDLG EAVGIIAAQS IGEPGTQLTM
     RTFHTGGVST AESGVVRSKF EGTVEFGSKA KVRPYRTPHG VNAQQSDVDF SLTIKPSGSG
     KPQKIEITNG SLLFVDDGQK IASDVTVATI AAGAVQKSVE KATKDVICDL AGQVSYDPTI
     QPREVTDRQG NITHKAQRLG RMWVLAGDVY NLPPNARPVV SSGGSVIESQ VLAEASQASE
     YGGAIRLREA LGDSREVQIV TTSMTLRDFK LLGESTHAGE IWNLEAKDGT RYRLNTIPGS
     KIGNAEVIAE LADDRFRTQT GGLVKFAPGL AIKKARSAKN GYEVNKGGTL LWIPQETHEI
     NKDISLLMIT DGQWIEAGTE VVKDIFSQTA GIVSVTQKND ILREIIVRSG SFHLCTEKKA
     LERFQGDGVM VNPGEAIAKG ISSDAMVFVQ AVETPEGTGL LLRPVEEYTI PNEAQLPDLG
     HVKQPNGPHL GIKATQRLAF KDNELVKSVE GVELLRTQLM LETFDTTPQM TVDVEAVPDK
     RAKTIERLQL VILESILVRR DTISDSSHGS THTELQVEDG QSIKAGDVVA TTQILCKQAG
     VAEMPEATED EPVRRLIVER PEDTITINTS GAPVVTVGQR VVDGEELAQG QPSDCCGEVE
     QVSANSVTMR LGRPYMISPD SLLHVRDGDL VQRGDGLALL VFERQKTGDI VQGLPRIEEL
     LEARRPRESS ILCKKPGTVE IKQGEDDEFT TVTVIESDDA IAEYPILLGR NVMVSDGQQV
     NAGELLTDGP INPHELLECF FEDLRSRKPL MDAAQEAIAK LQHRLVTEVQ NVYKSQGVSI
     HDKHIEVIVR QMTSKVRIED AGDTTLLPGE LIELRQVENT NQAMSITGGA PAEFTPVLLG
     ITKASLNTDS FISAASFQET TRVLTEAAIE GKSDWLRGLK ENVIIGRLIP AGTGFSGFEE
     ELRAEAGPHP DILSEDPAGY RRMQNLRPDY TVDMPAAPAA KSTALLDDPS AADLEATRSR
     HGIEAEASNF AAFTRPDADN ELAEEQVLDP AAVENLQEQG LLSDE