ID   RPOC2_PROM1             Reviewed;        1369 AA.
AC   A2C4N0;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
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};
GN   OrderedLocusNames=NATL1_18841;
OS   Prochlorococcus marinus (strain NATL1A).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NATL1A;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000553; ABM76440.1; -; Genomic_DNA.
DR   RefSeq; WP_011824419.1; NC_008819.1.
DR   AlphaFoldDB; A2C4N0; -.
DR   STRING; 167555.NATL1_18841; -.
DR   EnsemblBacteria; ABM76440; ABM76440; NATL1_18841.
DR   KEGG; pme:NATL1_18841; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_1_0_3; -.
DR   OMA; IEGKSDW; -.
DR   Proteomes; UP000002592; 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   Transcription; Transferase; Zinc.
FT   CHAIN           1..1369
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000353531"
FT   REGION          1..43
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;  149774 MW;  09543485BDE1A347 CRC64;
     MTSSSPKTRK SSTKSKAKRG SKSKKAAEIK 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 VVNADQEVLA ERDTPIDPQL
     SKKFEQSNLQ GVRVRSPLTC EATRSVCRKC YGWALAHNQL VDLGEAVGIV AAQSIGEPGT
     QLTMRTFHTG GVSTAETGVV RSTLSGKVEF GSKARVRGYR TPHGVEAQQA EVDFNLSIVP
     TSGSKPQKID IPIGSLLFVD NGQNIDIDVT VAQIASGTVQ KSVEKATKDV ICDLAGQVRY
     ETIIQPREVT DRQGNITLKA QRLGRLWVLA GDVYNLPPNA LPVVSGNVSV KEGQVLAEAS
     QASEFGGEVR LRDSIGDSRE VQIVTTSMIL NDFKLLEEST HSGEIWHLEA QDNTRYRLNT
     IPGSKIGNNE VIAELSDDRF KTETGGLIKY APGLTIKKAR SAKNGYEVSK GGTLLWIPQE
     THEINKDISL LMIKDRQWIE AGTEVVKDIF SQTAGIVTVT QKNDILREII VRSGTFKLCK
     ESKALDRFEG DGQIVNPGET IAKGIKTDSM VMVQSVETPE GKGLLLRSVE EFTIPDQAQL
     PELKHVKQPK GPSLGIKASQ RLAYKDGELI KSVEGVELLK TQLMLETFDT TPQMTVDVEV
     IHDLNSKGDR LKLVILESIL VRRDTTSDSS HGSTHTELQI ENAQVVSAGD VVATTQILCK
     QEGVVQLPDA VDGDPVRRLI VERDEDTITI 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 DPSDEDLEAT
     RSRHGIDPTT SNFAAFARPT GDDELSAEDQ MPDPAALEGL QEEGLLSDE