ID   RPOC2_PROM4             Reviewed;        1366 AA.
AC   A9BCH4;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=P9211_16051;
OS   Prochlorococcus marinus (strain MIT 9211).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=93059;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9211;
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; CP000878; ABX09536.1; -; Genomic_DNA.
DR   RefSeq; WP_012196157.1; NC_009976.1.
DR   AlphaFoldDB; A9BCH4; -.
DR   STRING; 93059.P9211_16051; -.
DR   EnsemblBacteria; ABX09536; ABX09536; P9211_16051.
DR   KEGG; pmj:P9211_16051; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_1_0_3; -.
DR   OMA; IEGKSDW; -.
DR   Proteomes; UP000000788; 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..1366
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000353525"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1299..1366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1307..1321
FT                   /note="Basic and acidic residues"
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   1366 AA;  149406 MW;  0519FFEED8060B87 CRC64;
     MTSTSPKSRR SSGKGRKGSK KKGKQVSQIP PLSKTPPSFR NRIVDKKALK QLVAWAYKNH
     GTAVTAAMAD NLKDLGFKYA TQAAVSISVD DLKVPDAKQD LLGEAEQQIT ATEECYRLGE
     ITEVERHTKV IDTWTETNER LVDAVKKNFN QNDPLNSVWM MANSGARGNM SQVRQLVGMR
     GLMANPQGEI IDLPIRTNFR EGLTVTEYVI SSYGARKGLV DTALRTADSG YLTRRLVDVA
     QDVIVREEDC GTSRAILVKA EDGRFGNRLV GRLTAEQIVG DADEIIAKKD TAIDPELSKK
     IEKAGLAGIM VRSPLTCEAT RSVCRKCYGW ALAHNNLVDL GEAVGIIAAQ SIGEPGTQLT
     MRTFHTGGVS TAETGVVRST IAGKVEFGPN ARVRGYRTPH GVEAQQAEVD FTLKVKPTGS
     GKTQTIEISN GSLIFVDNAQ EIAADVTVAQ ITAGAVKKSV EKATKDVICD LAGQVRYESV
     IQPREVTDRQ GNITLKAQRL GRLWVLAGDV YNLPPNARPV VKANSKVSKG MVLAEASQAS
     EFGGEVRLRD SIGDSREVQI VTTSMTLKDF KLLEESTHTG EIWNLEAKDG TRYRLNSIPG
     SKISSGEIVA ELADDRFRTK TGGLVKYAPG LAIKKARSAK NGFEVSNGGT LIWVPQETHE
     INKDISLLMI KDRQWIEAGT EVVKDIFSQT AGIVTVTQKN DILREIIVRS GEFHLCNESK
     VLERFEDEGQ MVNPGENIAK GLKADSMVLV QTVESRDGKG LLLRPVEEYT IPDQAQLPEL
     SHVKQEKGPS LGLRATQRLA FKDGELIKSV EGVELLKTQL ILDTFETTPQ MTVDVEVALD
     KRAKTINRLR LVILESILVR RDTMSDSSHG STHTELQIKD NQLVNADDVV ATTQILCKED
     GIVQLPNAVD DEPIRRLIVE RAQDTTVLTA KDNPILKVGE RVVDGDLLSK GEPINCCGEV
     EDIKGNKVTL RLGRPYMVSP DSVLHVRDGD LVQRGDGLAL LVFERQKTGD IVQGLPRIEE
     LLEARRPRES AILCKKPGIV EIKQEEDDES VVVKVIESDD SLSEYSILLG RNVMVSDGQE
     VHAGEFLTDG PVNPHELLEC FFGDLRDRKP LLEAAQESIA KLQHRLVTEV QNVYKSQGVS
     IDDKHIEVIV RQMTSKVRIE DAGDTTLLPG ELIEIRQVED TNQAISVTGG APAEFTPVLL
     GITKASLNTD SFISAASFQE TTRVLTEAAI EGKSDWLRGL KENVIIGRLI PAGTGFSGFV
     EELRAEAGPH PDILAEDPAG YRRMQNLRPD YTVEMPVSTA AKSTSVLDDP SEEDLEATRS
     RHGIDPTTSN FAAFARPSGD DPSQEDQKPD PIALEGLQEE GLLADE