RPOC2_SYNP6
ID RPOC2_SYNP6 Reviewed; 1318 AA.
AC Q5MZ21;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=syc2509_d;
OS Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS nidulans).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=269084;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT Synechococcus elongatus PCC 6301 chromosome: gene content and
RT organization.";
RL Photosyn. Res. 93:55-67(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; AP008231; BAD80699.1; -; Genomic_DNA.
DR RefSeq; WP_011244819.1; NC_006576.1.
DR AlphaFoldDB; Q5MZ21; -.
DR STRING; 269084.syc2509_d; -.
DR EnsemblBacteria; BAD80699; BAD80699; syc2509_d.
DR KEGG; syc:syc2509_d; -.
DR eggNOG; COG0086; Bacteria.
DR OMA; IEGKSDW; -.
DR Proteomes; UP000001175; 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..1318
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000225329"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 295
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 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1318 AA; 143828 MW; AADF8725956CE1FC CRC64;
MAETKSAPIF RNRVIDKKQL KKLIGWTFAH YGTAKTAVVA DDLKALGFRY ATRAGVSISI
DDLKVPGSKA ELLESAEKRI QETEDRYTRG EITEVERFQK VIDTWANTND ELTDRVVKNF
RESDPLNSVY MMAFSGARGN ISQVRQLVGM RGLMANPQGE IIDLPIKTNF REGLTVTEYI
ISSYGARKGL VDTALRTADS GYLTRRLVDV SQDVIIHEVD CGTSRGLFVE AMTDGDRILI
PISQRLLGRV TAEAVLDPST DEVLAEAGQD INEDLANRIE KAGIKKVKVR SPLTCEAARS
VCQKCYGWSL AHAQMVDMGE AVGIIAAQSI GEPGTQLTMR TFHTGGVFTG ETARLLRAPV
AGTIKLGKKA RTRPYRTRHG EEALLAEANF DLVLEGKGRK ETFAILQGST IFVQDGDKVA
AEAILAEVPV SGRTKRTVEK ATKDVATDLA GEIRFQDIVP EEKTDRQGNT TRIAQRGGLL
WVLAGDVYNL LPGAEPTVKN GDRVEVGDVL AETKLTTERG GTVRMGEDNG SSTHREVEII
TASVVLDTAT VKAEASQGRE HYVIETKGGQ RFNLLAAPGT KVTTGHVVAE LIDSRYRTQT
GGLLKYSGVE ISKKGRAKAK QGYEVTKGGT LLWIPEETHE VNKDISLLNV EDGQLVEAGT
EVVKDIFCQT TGIVSVTQNN DILREIVIKP GDVHVLDDPD TAAKYDEGRL VNAGEEVFPG
LTAEQLVWAE AVDGTDGPLL LLRPVQELVI PDEPPVPSQD SSQESSSRSI RLRAVQRLQF
QDGERIKSVE GVDLLRTQLV LESEEGSSQL SADIELLPDS KDPETLRLQL VIIEPVVTRR
DVASDTTHGS THTELRVKDG QKVKPGAVIA CTQIQCKEAG VVRGIQEGSE AVRRLLVERE
RDCVTLDLDV TAATQLQPGS LIVAGTQLVD GIIAPESGEA RAIAPGQLQL RIARPYRVSQ
GAVLHVEDKG LVQRGDNLVL LVFERAKTGD IIQGLPRIEE LLEARKPKEA CILARRPGVA
HINYSDDDAI DIQVIEADGT QADYPVGPGQ PLIISDGETV DAGQALTDGP ANPHDLLEIY
YDYFREQLGE DYEAALESLR RVQALLVNEV QSVYQSQGID ISDKHIEVIV RQMTSKVRID
DGGDTIMLPG ELHELREVYN SNNTMALTGM APAQFTPVLL GITKASLNTN SFISAASFQE
TTRVLTEAAI EGKSDWLRGL KENVIIGRLI PAGTGFKAYE ESLLTDVDGG YEDRVYDDDL
ADVVIDDRAA RSYTLNEGRD FSRSMTFAEG ESMILDDGEE LIDDSSASLR NLVDVDED
