ID   RPOC2_ACAM1             Reviewed;        1330 AA.
AC   B0C385;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=AM1_3594;
OS   Acaryochloris marina (strain MBIC 11017).
OC   Bacteria; Cyanobacteria; Synechococcales; Acaryochloridaceae;
OC   Acaryochloris.
OX   NCBI_TaxID=329726;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBIC 11017;
RX   PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA   Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA   Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA   Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA   Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA   Blankenship R.E., Touchman J.W.;
RT   "Niche adaptation and genome expansion in the chlorophyll d-producing
RT   cyanobacterium Acaryochloris marina.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
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; CP000828; ABW28584.1; -; Genomic_DNA.
DR   RefSeq; WP_012163977.1; NC_009925.1.
DR   AlphaFoldDB; B0C385; -.
DR   SMR; B0C385; -.
DR   STRING; 329726.AM1_3594; -.
DR   EnsemblBacteria; ABW28584; ABW28584; AM1_3594.
DR   KEGG; amr:AM1_3594; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_1_0_3; -.
DR   OMA; IEGKSDW; -.
DR   OrthoDB; 4373at2; -.
DR   Proteomes; UP000000268; 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..1330
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000353519"
FT   REGION          1275..1301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         228
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         302
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         309
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         312
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ   SEQUENCE   1330 AA;  145388 MW;  44E29D0C26AE2D4E CRC64;
     MAENSTHSPR EATPPAFCNK IVNKGQLKSL VHWAFTHYGT ARTAEMADHL KDLGFRYATK
     AGVSISVDDL QVPPSKRRLL ETAEEEIRVT EDRYTRGEIT EVERFQKVID TWNGTSEELK
     DEVVKNFKSN NPLNSVYMMA FSGARGNLSQ VRQLVGMRGL MADPQGEIID LPIKTNFREG
     LTVTEYIISS YGARKGLVDT ALRTADSGYL TRRLVDVSQD VIIRELDCGT QRGIPVQSMT
     DGDRVLIPLA NRLLGRVVLQ EVVHPETGEV ILPKNEAVSE SIAKEIAKAG VEEVVVRSPL
     TCEAARSVCQ HCYGWSLAHA HLVDTGEAVG IIAAQSIGEP GTQLTMRTFH TGGVFTGEVA
     RQIRAPFNGK IKFPKKMRSR PFRTRHGEDA LTAEVSTSLT LEGDDQTETF EITQNSTLLV
     KDGQAVKMGQ MLAEVAAAGR NVRKTTEKAT KDVASDLAGE VQFSNLVPEE KHDRQGNTTR
     IAPRGGLIWV LSGEVYNLPP GAEPTVKNDD YIEGEDVLAE TKLVTEHGGV VRLPVQEEGK
     GGREVEIITA SVLLDQAKVW LESLQGRDQY VIEAQKKQRF LLKAAPGTKV INGQVVAELI
     DDHYRTKTGG ILKYAGVEVT KKGKAKQGYE VTQGGTLLWI AEESHEVNKD ISLLLVEDGQ
     YVEAGTEVVK DIFCQSNGVV EVTQKNDILR EVLVKPGDLH LVDDPEAVKG KDQSLLNPGE
     ELLPGLSTDE LRYIECVTTP EGEAVLLRPV TEFPVPDQPS VPSQESINEA GRAICLKAVQ
     RLPYKDGERV KSVEGVDLLR TQLVLEIDTD APQIAADIEI LPDEKDEEVS RLQLVILETL
     VIRRDVSADQ TQGSTKTRLL VEEGQQIDPG AVVARTEIKA KQGGKVRGIR SGNEATRRIL
     LMTDDDLITI ETQGKATSAS EGELLRAGDE VAAGVTVAES CQVIKVQDGQ VTLRIARPYL
     VSPGAVLQID DQDLVQRGDN LALLVFERTK TGDIIQGLPR IEELLEARKP KEMCTLAQRS
     GTCQVIYNDD DSIEVKIVEQ DGTITDYPIG PGQNPIVLDG QTVEAGEAVT DGPLNPHDIL
     EIYFRFHRET KGVYESALLS LQKVQNFLVN GVQSVYQSQG IDIADKHIEV VVRQMTSKVR
     IDDGGDTTML PGELIDLYQV EQVNAAMSIT GGAPAEYTPV LLGITKASLN TDSFISAASF
     QETTRVLTEA AIQGKSDWLR GLKENVIIGR LIPAGTGFNS YDDGGLGEPD PSFEGMPFTD
     DDDVIDDRTA RNYNINDVKP FSGERPAYDP SKPGEQQRSM LGIDPAAVGD DTLIDDQVAE
     KLNANLEGDQ