ID   RPOC2_PARMW             Reviewed;        1364 AA.
AC   Q7U8K2;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=SYNW0615;
OS   Parasynechococcus marenigrum (strain WH8102).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Parasynechococcus; Parasynechococcus marenigrum.
OX   NCBI_TaxID=84588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH8102;
RX   PubMed=12917641; DOI=10.1038/nature01943;
RA   Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA   Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA   Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT   "The genome of a motile marine Synechococcus.";
RL   Nature 424:1037-1042(2003).
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; BX569690; CAE07130.1; -; Genomic_DNA.
DR   RefSeq; WP_011127482.1; NC_005070.1.
DR   AlphaFoldDB; Q7U8K2; -.
DR   STRING; 84588.SYNW0615; -.
DR   EnsemblBacteria; CAE07130; CAE07130; SYNW0615.
DR   KEGG; syw:SYNW0615; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_1_0_3; -.
DR   OMA; IEGKSDW; -.
DR   OrthoDB; 4373at2; -.
DR   Proteomes; UP000001422; 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; 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; 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   Transcription; Transferase; Zinc.
FT   CHAIN           1..1364
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000067909"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         250
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         317
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         324
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         327
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ   SEQUENCE   1364 AA;  148443 MW;  29AB2BD02198F088 CRC64;
     MTSSSSKSNK SRKSSKAAKD TTPVHESASR PLSKTPPPFR NHIVDKRGLK QLVAWAYKNH
     GTAVTSSMAD KLKDLGFRYA TQAAVSISVN DLQVPEAKKA LLGEAEEQIT ATEERYRLGE
     ITEVERHTKV IDTWTETNER LVDAVKKNFN QNAPLNSVWM MANSGARGNM SQVRQLVGMR
     GLMANPQGEI IDLPIRTNFR EGLTVTEYVI SSYGARKGLV DTALRTADSG YLTRRLVDVA
     QDVIVREDDC GTTRHIVVEA EDGRFGNRLV GRLTASQVVS AVGEVLAERD TEIDPPLSKR
     IEKAGVTAVS VRSPLTCEAN RSVCRKCYGW ALAHNELVDL GEAVGIIAAQ SIGEPGTQLT
     MRTFHTGGVS TAETGVVRSV VAGTIEFSAK ARVRPYRTPH GVNAQQAEVD FNLSIKPVGK
     GKTQKIEITN GSLLFVENGQ TIDADVTVAQ IAAGAVKKSV EKATKDVICD LAGQVRYEEA
     IQPREVTDRQ GNITLKAQRL GRMWVLAGDV YNLPPNAQPV VQGDTEVTEG QVLAEASQRS
     EYGGDVRLRD SIGDSREVQI VTTAMTLKDF KLLEESTHSG EIWNLEAKDG TRYRLNTIPG
     SKIGSGEVVA ELADDRFRTG TGGLVKFAPG LAIKKARSAK NGYEVNKGGT LLWIPQETHE
     INKDISLLMI TDGQWIEAGT EVVKDIFSQT AGVVTVTQKN DILREIIVRS GDFHLSSDSK
     ALERFEGDGH MVNPGEEIAK GLSIQDMKYV QTVETPEGKG LLLRPVEEYT IPNEAQLPEL
     SHVKQANGPH LGIKATQRLA FKDNELIKSV EGVELLKTQL ILETFDTTPQ MTVDVEKAPD
     KRAKTISRLR LVILESILVR RDTMSDSSHG STHTELQVED GISVKAGDVI ATTQILCKQA
     GVAQLPEATE ADPVRRLLVE RPEDTTTLST SGKPVVAVGQ RIVDGELLAE GDPSSCCGEV
     EAVDSNSVTL RLGRPYMVSP DSVLHVRDGD LVQRGDGLAL LVFERQKTGD IVQGLPRIEE
     LLEARRPRES AVLCKKPGTV EIKQGDDDES LTVTVIEADD AIGEYPILLG RNVMVSDGQQ
     VTAGELLTDG PINPHELLEC FFEDLRSRKP LMDAAQEAIA NLQHRLVTEV QNVYKSQGVS
     IDDKHIEVIV RQMTSKVRVE DAGDTTLLPG ELIELRQVED TNQAMAITGG APAEFTPVLL
     GITKASLNTD SFISAASFQE TTRVLTEAAI EGKSDWLRGL KENVIIGRLI PAGTGFSGFE
     EELQKEAGPH PDILSEDPAG YRRMQNLRPD YTVEMPPAAS STAVLDDPSD ADLEATRTRH
     NIDPSASNFA AFARPDADNE LKEEQVVDAE AVEGLQEEGL LSDD