ID   RPOC2_PROMA             Reviewed;        1367 AA.
AC   Q7VA30;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 95.
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}; Synonyms=rpoC;
GN   OrderedLocusNames=Pro_1638;
OS   Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167539;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARG / CCMP1375 / SS120;
RX   PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA   Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA   Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA   Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA   Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT   "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT   nearly minimal oxyphototrophic genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(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; AE017126; AAQ00682.1; -; Genomic_DNA.
DR   RefSeq; NP_876029.1; NC_005042.1.
DR   RefSeq; WP_011125788.1; NC_005042.1.
DR   AlphaFoldDB; Q7VA30; -.
DR   SMR; Q7VA30; -.
DR   STRING; 167539.Pro_1638; -.
DR   PRIDE; Q7VA30; -.
DR   EnsemblBacteria; AAQ00682; AAQ00682; Pro_1638.
DR   GeneID; 54200962; -.
DR   KEGG; pma:Pro_1638; -.
DR   PATRIC; fig|167539.5.peg.1732; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_1_0_3; -.
DR   OMA; IEGKSDW; -.
DR   OrthoDB; 4373at2; -.
DR   Proteomes; UP000001420; 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..1367
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000067905"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1306..1367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..23
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1323..1346
FT                   /note="Polar 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   1367 AA;  149737 MW;  1FB0169FC8E1B66D CRC64;
     MTSTSPKSRK SSSKRKGSKK KAARSKNVIP PLSKTPPSFR NCVVDKKSLK QLVAWAFKNH
     GTAVTAAMAD NLKDLGFKYA TQAAVSISVD DLKVPEAKQD LLGQAEEQIT ATEECYRLGE
     ITEVERHTKV IDTWTETNER LVDAVKKNFN HNDPLNSVWM MANSGARGNM SQVRQLVGMR
     GLMANPQGEI IDLPIRTNFR EGLTVTEYVI SSYGARKGLV DTALRTADSG YLTRRLVDVA
     QDVIVREEDC GTTRAILINA EDGRFGNRLV GRLVAEDIVD QEDAVIAKRD TAIDPELSKK
     IEKANVNGVM IRSPLTCEAT RSVCRKCYGW ALAHNQLVDL GEAVGIIAAQ SIGEPGTQLT
     MRTFHTGGVS TAETGVVRSN LAGKVEFGPK ARVRGYRTPH GVEAQQAEVD FLLHIKPTEK
     GKGQKVEISS GSLIFVEDGQ EVDADVTLAQ IAAGAIKKSV EKATKDVICD LAGQVRYEEA
     IQPKEVTDRQ GNITLKAQRL GRLWVLAGDV YNLPPNAKPV IASNANVQAG KVLAEASQSS
     EFGGEVRLRD SIGDSREVQI VTTSMTLKDY NLLEESNHSG EIWNLEANDG TRYRINSIPG
     SKIGNNEVIA ELSDDRFRTK TGGLVKYAPG LAIKKARSAK NGFEVSNGGS LLWIPQETHE
     INKDISLLMI QDRQWIEAGT EVVKDIFSQT AGIVTVTQKN DILREIIVRS GEFHLCTDSN
     ILERFDNEGQ IVNPGETIAK GIKPEAMVFV QTIETTEGKG VLLRPVEEYT IPDKAQLPEL
     SHVTQQQGPS LGLKATQRLG YKDGELIKSV EGVELLKTQL ILETFDTTPQ MTVDVEVTED
     QSTKTIQRLR LVILESILVR RDTISDSSHG STHTELQVKD QQIVKAGDIV ATTQILCKEK
     GIVQLPEMKE DEPIRRLIVE RQEDTVTLTA ASKPVVKIGQ RVIDGDLLSN EEPINCCGEI
     EAIKENKVTL RLGRPYMVSP DSVLHVKNGD LVQRGDGLAL LVFERQKTGD IVQGLPRIEE
     LLEARRPRDS AILCKRRGIV EINQGDDDDS VVVKVIESDD LIEEYPILLG KNVMISDGQE
     VKAGELLTDG PVNPHELLEC FFGDLRDRKP LMEAAQEAIA KLQHRLVTEV QNVYKSQGVA
     IDDKHIEVIV RQMTSKVRIE DAGDTTLLPG ELIEIRQVED TNQAISITGG APAEFTPVLL
     GITKASLNTD SFISAASFQE TTRVLTEAAI EGKSDWLRGL KENVIIGRLI PAGTGFSGFV
     EELRAEAGPH PDILAEDPAG YRRIQNLRPD YTVEMPSSPA AANLTSVLDD PSDADLEATR
     NRHGIDPSTS NFAAFARPSG DDNFQEDQSP DPAALEGLQE EGLLSDE