ID   RPOC2_PROMT             Reviewed;        1369 AA.
AC   Q46J24;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=PMN2A_1014;
OS   Prochlorococcus marinus (strain NATL2A).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59920;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NATL2A;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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; CP000095; AAZ58504.1; -; Genomic_DNA.
DR   RefSeq; WP_011295359.1; NC_007335.2.
DR   AlphaFoldDB; Q46J24; -.
DR   STRING; 59920.PMN2A_1014; -.
DR   EnsemblBacteria; AAZ58504; AAZ58504; PMN2A_1014.
DR   KEGG; pmn:PMN2A_1014; -.
DR   HOGENOM; CLU_000524_1_0_3; -.
DR   OMA; IEGKSDW; -.
DR   OrthoDB; 4373at2; -.
DR   PhylomeDB; Q46J24; -.
DR   Proteomes; UP000002535; 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; 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..1369
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000225328"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1294..1369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1309..1323
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         253
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         320
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"
FT   BINDING         330
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ   SEQUENCE   1369 AA;  149752 MW;  8E98ED8C6A69A941 CRC64;
     MTSSSPKTRK SSTKSKAKRG SKSKKAAEII AVQRLSKTPP PFRNKVVDKK VLKNLVAWAF
     KHHGTAATAA MADNLKDLGF RYATQAAVSI SVDDLKVPEA KQDLLGQAEE LITATEECYR
     LGEITEVERH TKVIDTWTET NERLVDAVKK NFNQNDPLNS VWMMANSGAR GNMSQVRQLV
     GMRGLMANPQ GEIIDLPIRT NFREGLTVTE YVISSYGARK GLVDTALRTA DSGYLTRRLV
     DVAQDVIVRE EDCGTTRSIL ISAEDGKFGN RLVGRLTSEQ VVNADEEVLA ERDTPIDPQL
     SKKFEQSNMQ GVRVRSPLTC EATRSVCRKC YGWALAHNQL VDLGEAVGIV AAQSIGEPGT
     QLTMRTFHTG GVSTAETGVV RSTLSGKVEF GSKARVRGYR TPHGVEAQQA EVDFNLSIVP
     TSGGKPQKID IPIGSLLFVD NGQNIDIDVT VAQIASGTVQ KSVEKATKDV ICDLAGQVRY
     ETIIQPREVT DRQGNITLKA QRLGRLWVLA GDVYNLPPNA LPVVSGNVSV KEGQVLAEAS
     QASEFGGEVR LRDSIGDSRE VQIVTTSMTL DDFKLLEEST HSGEIWHLEA QDNTRYRLNT
     IPGSKIGNNE VIAELSDDRF KTETGGLIKY APGLTIKKAR SAKNGYEVSK GGTLLWIPQE
     THEINKDISL LMIKDRQWIE AGTEVVKDIF SQTAGIVTVT QKNDILREII VRSGTFKLCK
     ESKALDRFEG DGQIVNPGET IAKGIKTDSM VMVQSVETPE GKGLLLRSVE EFNIPDQAQL
     PELKHVKQPK GPSLGVKASQ RLAYKDGELI KSVEGVELLK TQLMLETFDT TPQMTVDVEV
     IQDLNSKGDR LKLVILESIL VRRDTTSDSS HGSTHTELQI ENAQVVSAGD VVATTQILCK
     QEGVVQLPDA VDGDPVRRLI VEREEDTITI DSKGTTLLKV GQRVVDGDFV SKDQSIDACG
     EIENIDGKKV KLRLGRPYMV SPDSVLHVRD GDLVQRGDGL ALLVFERQKT GDIVQGLPRI
     EELLEARRPR DSAILCKKSG TVDIKKGDDD DSVVVSIIED NDVISEYPIL LGRNVMVRNS
     QQVIAGEFLT DGPVNPHELL ECFFTDLRDK KPLMDAAQEA IAKLQHRMVS EVQNVYKSQG
     VAIDDKHIEV IVRQMTSKVR IEDAGDTTFL PGELIELRQV EDTNQAISIT GGAPSEFTPV
     LLGITKASLN TDSFISAASF QETTRVLTEA AIEGKSDWLR GLKENVIIGR LIPAGTGFSG
     FVEELNAEAG PHPDILAEDP AGYRRIQNLR PDYTVDMPSS PVAKNTAVLD DPSEEDLEAT
     RSRHGIDPTT SNFAAFARPV GDDELSAEDQ MPDPAALEGL QEEGLLSDE