RPOC2_SYNR3
ID RPOC2_SYNR3 Reviewed; 1368 AA.
AC A5GVF0;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, 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=SynRCC307_1956;
OS Synechococcus sp. (strain RCC307).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=316278;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC307;
RG Genoscope;
RL Submitted (MAY-2006) 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; CT978603; CAK28859.1; -; Genomic_DNA.
DR RefSeq; WP_011936371.1; NC_009482.1.
DR AlphaFoldDB; A5GVF0; -.
DR STRING; 316278.SynRCC307_1956; -.
DR EnsemblBacteria; CAK28859; CAK28859; SynRCC307_1956.
DR KEGG; syr:SynRCC307_1956; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_1_0_3; -.
DR OMA; IEGKSDW; -.
DR OrthoDB; 4373at2; -.
DR Proteomes; UP000001115; 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..1368
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353539"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1340..1368
FT /note="Disordered"
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 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 328
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1368 AA; 148028 MW; 43472365AF0782DF CRC64;
MTSSSKPARK TSKSKSKASK AAEAPAAPSN ELSREAPTFQ NKVIDKKALR SLVAWSYKHH
GTAATSALAD DLKDLGFRFA TQAAVSISVD DLRVPGDKST LLQEAEDQIT ATEERYRLGE
ITEVERHTKV IDTWTETNER LVQSVRRNFD ENDPLNSVWM MANSGARGNM SQVRQLVGMR
GLMANPQGEI IDLPIRTNFR EGLTVTEYVI SSYGARKGLV DTALRTADSG YLTRRLVDVA
QDVIVREDDC GTTRSIKVAA DDNGKYKSRL VGRLLAEDVV DGAGEVIATR NTEVDPPLSA
RIEAAGIAQV QVRSPLTCEA ARSVCRKCYG WALAHNELVD LGEAVGIIAA QSIGEPGTQL
TMRTFHTGGV STAETGVVRS VVEGSVEFSA KAKVRPHRTP HGVEAQLAET DFSLTVKPSG
KGKTQKLDVT AGSILFVNAG GSVPNDTILA QISSGSAVKK SVEKATKDVV CDLAGQVRYE
DVIQPKEVPD RQGNITLKAQ RLGRLWVFSG DVYNLPPNAM PVVQGGANVK TGEVLAESRQ
VSEFGGAVRL RESQGDSREV EIVTSSLTLK DCKLVATTTH SGQIWHLESK DNTRYRLNTE
PGTKIANGEV IAELADDRFR TQTGGLVKFA PGLAIKKARS AKNGFEVSKG GTLLWIPQET
HEINKDISLL MIEDGQWIEA GTEVVKDIFS QTAGIVTVTQ KNDILREIIV RSGQLHLVSD
SKVLARYTDG GGKMVNPGEE IAPGLKAEAM HMVEAVDTPE GGALLLRPVE EYAIPNEAHM
PELGSVKQAN GPSMGLKAVQ RLAFKDGELV KSVEGVELLR TQLLLETFDT TPQMTVDVES
AQDKRAKTIQ RLQLTILETH LVRRDTLSDA SHGSTHTEVK VADGDNIKRG DVVATVQILC
KDDGVAQLPD RKDDEPIRRL IVERPSDTIT VDLGGSKLSL KAGQRVVEGD DLGGGLTCPH
SGQVEEVKGS SLTLRVGRPY MVSPDSILHV RDGDLVLRGD TLAQLVFERA KTGDIVQGLP
RIEELLEARR PRESAVLCRK AGTIKVEQPE GEDNPTVSVN EGEELHTEYP ILLGRTVMVS
DGQEVKAGDL LTDGPINPHE LLEVIFEDLR GPLPTMDAAN QAIGRLQTAL VQEVQNVYKS
QGVTIDDKHL EVIVRQMTSK VRIEDAGDTT LLPGELIELR QVDQVNQAMA ITGGAPAEFT
PVLLGITKAS LNTDSFISAA SFQETTRVLT EAAIEGKSDW LRGLKENVII GRLIPAGTGF
SGFDEQLKAE ALPHPDILGE ENAGYRRATN LRPDYTVEMP LPQSNTAVLD DPSDTELEAT
RSRHGIEDRT NLAAFARPAA GEELAEEHVP DPGALEGLQE EGLLSQDS
