RPOC2_SYNE7
ID RPOC2_SYNE7 Reviewed; 1318 AA.
AC Q31N15;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Synpcc7942_1524;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000100; ABB57554.1; -; Genomic_DNA.
DR RefSeq; WP_011378066.1; NC_007604.1.
DR AlphaFoldDB; Q31N15; -.
DR SMR; Q31N15; -.
DR STRING; 1140.Synpcc7942_1524; -.
DR PRIDE; Q31N15; -.
DR EnsemblBacteria; ABB57554; ABB57554; Synpcc7942_1524.
DR KEGG; syf:Synpcc7942_1524; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_1_0_3; -.
DR OMA; IEGKSDW; -.
DR OrthoDB; 4373at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1524-MON; -.
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_0000353532"
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; 143838 MW; 0CEFF9039B1E4B59 CRC64;
MAEAKSAPIF 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 VIIEPVVIRR
DVASDTTHGS THTELRVKDG QKVKPGAVIA CTQIQCKEAG VVRGIQEGSE AVRRLLVERE
RDCVTLDLDV TAATQLQPGS LIVAGTQLVD GIIAPESGEV 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
